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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q91VM4 | MMCLECASAAAGGAEEEEADAERRRRRRGAQPGAGGSACCGARGVGGAGVVSADEEVQTLSGSVRRVPSGLPSIPSTPGCAAAAKGPSAPQPKPASLGRGRGAAAAILSLGNVLNYLDRYTVAGVLLDIQQHFGVKDRGAGLLQSVFICSFMVAAPIFGYLGDRFNRKVILSCGIFFWSAVTFSSSFIPQQYFWLLVLSRGLVGIGEASYSTIAPTIIGDLFTKNTRTLMLSVFYFAIPLGSGLGYITGSSVKQAAGDWHWALRVSPVLGMITGTLILILVPATKRGHADQLGGQLKARTSWLRDMKALIRNRSYVFSSLATSAVSFATGALGMWIPLYLHRAQVVQKTAETCNSPPCGAKDSLIFGAITCFTGFLGVVTGAGATRWCRLRTQRADPLVCAVGMLGSAIFICLIFVAAKTSIVGAYICIFVGETLLFSNWAITADILMYVVIPTRRATAVALQSFTSHLLGDAGSPYLIGFISDLIRQSTKDSPLWEFLSLGYALMLCPFVVVLGGMFFLATALFFLSDRAKAEQQVNQLVMPPASVKV | Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate (sphing-4-enine 1-phosphate, S1P) and sphinganine-1-phosphate in the lymph, thereby playing a role in lymphocyte trafficking . S1P is a bioactive signaling molecule that regulates many physiological processes important for the development and for the immune system . Regulates levels of S1P and the S1P gradient that exists between the high circulating concentrations of S1P and low tissue levels that control lymphocyte trafficking . Required for the egress of T-cells from lymph nodes during an immune response by mediating S1P secretion, which generates a gradient that enables activated T-cells to access lymph . Also required for the egress of immature B-cells from the bone marrow . In contrast, it does not mediate S1P release from red blood cells . Involved in auditory function: S1P release in the inner ear is required for maintenance of the endocochlear potential in the cochlea . In addition to export, also able to mediate S1P import .
Catalytic Activity: sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58196
Sequence Length: 549
Subcellular Location: Cell membrane
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B0JZE1 | MCLESDGVGTVSNSQGCIPGAEERGLETLPGRMNPTSLDVKAVELESSSSKPDKAYNWKRASVAAAGILSVGNVLNYLDRYTVAGVLLDIQQHFEVKDSGAGLLQTVFICSFMVAAPIFGYLGDRFNRKVILSSGIFFWSAITFSSSFIPKKYFWLLVLSRGLVGIGEASYSTIAPTIIGDLFTKNTRTLMLSVFYFAIPLGSGLGYITGSSVKQVAGDWRWALRVSPVLGVITGTLLLIFVPTAKRGHAEQLKGSSWIRDMRGLIKNRSYVFSSLATSTVSFATGALGMWIPLYLYRAQVVQKSVEPCNIPPCSTKDSLIFGAITCLTGFLGVIIGAGATKWCRRKTQRADPLVCAVGMLGSAIFICLVFVAAKSSIIAAYICIFAGETLLFSNWAITADMLMYVVIPTRRATAVALQSFTSHLLGDAGSPYLIGFISDLIQQSTTKSSLWEFLSLGYALMLCPFVVVLGGMFFLATALFFLEDREKAEKLEPCSDPFTVGNCSDSEEASIL | Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate (sphing-4-enine 1-phosphate, S1P) and sphinganine-1-phosphate.
Catalytic Activity: sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-phosphate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55447
Sequence Length: 513
Subcellular Location: Cell membrane
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F4IKF6 | MVTKEEDCLPPVTETTSRCYSTSSSTPLAELETVRSLEIVESSSSLSPVWLLVIFCIINLLNYMDRGAIASNGVNGSTRSCNDKGKCTLATGIQGHFNLSNFEDGVLSSSFMVGLLIASPIFASLAKRLIGVGLTVWTIAVLGCGSSFAFWFIVLCRMFVGVGEASFISLAAPFIDDNAPQEQKAAWLGLFYMCIPSGVALGYVYGGYVGKHFSWRYAFWGEAVLMAPFAVLGFLMKPLQLKGSETLKNNNRLQVDNEIEHDQFEVSIETSKSSYANAVFKSFTGFAKDMKVLYKEKVFVVNVLGYVSYNFVIGAYSYWGPKAGYNIYKMKNADMIFGAVTIICGIVGTLSGGFILDRVTATIPNAFKLLSGATFLGAVFCFTAFTLKSLYGFIALFALGELLVFATQAPVNYVCLHCVKPSLRPLSMAISTVAIHIFGDVPSSPLVGIVQDHINSWRKTTLILTSILFLAAAIWFIGKINLNSFYSNDESFLVQIKLFVANLCFCKGYS | Function: Probable sphingolipid transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55667
Sequence Length: 510
Subcellular Location: Mitochondrion inner membrane
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Q6ZMD2 | MAGGMSAECPEPGPGGLQGQSPGPGRQCPPPITPTSWSLPPWRAYVAAAVLCYINLLNYMNWFIIAGVLLDIQEVFQISDNHAGLLQTVFVSCLLLSAPVFGYLGDRHSRKATMSFGILLWSGAGLSSSFISPRYSWLFFLSRGIVGTGSASYSTIAPTVLGDLFVRDQRTRVLAVFYIFIPVGSGLGYVLGSAVTMLTGNWRWALRVMPCLEAVALILLILLVPDPPRGAAETQGEGAVGGFRSSWCEDVRYLGKNWSFVWSTLGVTAMAFVTGALGFWAPKFLLEARVVHGLQPPCFQEPCSNPDSLIFGALTIMTGVIGVILGAEAARRYKKVIPGAEPLICASSLLATAPCLYLALVLAPTTLLASYVFLGLGELLLSCNWAVVADILLSVVVPRCRGTAEALQITVGHILGDAGSPYLTGLISSVLRARRPDSYLQRFRSLQQSFLCCAFVIALGGGCFLLTALYLERDETRAWQPVTGTPDSNDVDSNDLERQGLLSGAGASTEEP | Function: Sphingolipid transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54769
Sequence Length: 512
Subcellular Location: Membrane
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Q9D232 | MSTECLKPQTGGPQSQSLSQGGQYGALASGTCLPPSTPVPWSLPRWRAYLAAAVLCYINLLNYMNWFIIPGVLLDVQKYFHISDSHAGLLQTVFISCLLVSAPVFGYLGDRYNRKAILSFGILLWSGAGLSSSFISYQYSWLFFLSRGFVGTGAASYSTIAPTVLGDLFVKDQRTCALAVFYIFIPVGSGLGYVLGSTVAELTGNWRWALRLMPCLDAMALALLILLVPDVPRGAAEKQGEVAVRAPRSSWCEDVRYLGRNWSFVFSTLGVTAIAFVTGALGFWAPKFLFEARVVHGLQLPCFQEQCHSQDSLIFGALTVATGIIGVMLGAEASRRYKKVNPRAEPLICASSLFATAPCLYLALILASRTLLASYVFLALGELLLSCNWAVVADILLSVVVPRCRGTAEALQITVAHVLGDAGSPYLTGLISSVLQAERPDSYLQHFLSLQHSFLCCAFAIVLGGGFFLLTALHLEKDQARARQPGKGTLDSKDIASRNTESQGLLSGTSTPTE | Function: Sphingolipid transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55456
Sequence Length: 514
Subcellular Location: Membrane
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Q9ALP0 | MSRVSDTFAETSSVYSPDHADIYDAIHSARGRDWAAEAGEVVQLVRTRLPEAQSLLDVACGTGAHLERFRAEYAKVAGLELSDAMREIAIRRVPEVPIHIGDIRDFDLGEPFDVITCLCFTAAYMRTVDDLRRVTRNMARHLAPGGVAVIEPWWFPDKFIDGFVTGAVAHHGERVISRLSHSVLEGRTSRMTVRYTVAEPTGIRDFTEFEILSLFTEDEYTAALEDAGIRAEYLPGAPNGRGLFVGIRN | Function: Involved in the biosynthesis of forosamine ((4-dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly deoxygenated sugar component of several bioactive natural products such as the insecticidal spinosyns A and D . Catalyzes the dimethylation of the C-4 amino group from dTDP-4-amino-2,3,4,6-tetradeoxy-alpha-D-glucose to yield dTDP-D-forosamine .
Catalytic Activity: dTDP-4-amino-2,3,4,6-tetradeoxy-alpha-D-erythro-hexopyranose + 2 S-adenosyl-L-methionine = dTDP-alpha-D-forosamine + 2 H(+) + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 27669
Sequence Length: 249
EC: 2.1.1.324
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Q9M4A2 | MEGKFAISESTNLLQRIKDFTQSVVVDLAEGRSPKISINQFRNYCMNPEADCLCSSDKPKGQEIFTLKKEPQTYRIDMLLRVLLIVQQLLQENRHASKRDIYYMHPSAFKAQSIVDRAIGDICILFQCSRYNLNVVSVGNGLVMGWLKFREAGRKFDCLNSLNTAYPVPVLVEEVEDIVSLAEYILVVEKETVFQRLANDMFCKTNRCIVITGRGYPDVSTRRFLRLLMEKLHLPVHCLVDCDPYGFEILATYRFGSMQMAYDIESLRAPDMKWLGAFPSDSEVYSVPKQCLLPLTEEDKKRTEAMLLRCYLKREMPQWRLELETMLKRGVKFEIEALSVHSLSFLSEVYIPSKIRREVSSP | Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination . Together with MTOPVIB, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination . The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles .
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 41804
Sequence Length: 362
Subcellular Location: Nucleus
EC: 5.6.2.2
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Q22236 | MYEYSFNPNIDHEPGSVESQQSTIYSDSDDSDDSFLDDEVIPPKEQAMRKIEFALADIKRQMDNKEKSLTLRISTSKSHFCLRYTAKRKGKLDRDLHCLHQVYDLLENDKRSTKRELYYEHKAVYGNQKYLDSSIKSICELLNESRANLNILSCGRGIIRGAITFLVENVGVIDARVQEVLITDALLFSNIISEADFILVVEKDTTFQKLMDENFQAMFPRGILATSKGYPDIATRNVLKMLSEKRKFPIYGLFDADPHGIEIYLTYKYGPTKEFAEGRGAFVPTIEWIGLFPTDFHRFTIDQSQCLPLVRTDFVKIEKMIPRSIQLGEIVVTRELDWMIQNKFKMELESINMCGQEYMARFLIAPRVMSIEKEIPIQPETIINEYHEDSQCSLSTDDDREAKDDDYIDSDAEEKFQNMIDNDSD | Function: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 49169
Sequence Length: 425
Subcellular Location: Nucleus
EC: 5.6.2.2
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Q7KPA5 | MDEFSENIERIALELLSNLVHGNATLSVPRNSSGNVISEYRRVSYNNRGSRHSFCVLIYMLSRVHRLQVRGGSFTVRGLYYDNPLLVRSQSRIAEARLDVCRMLRTSPLSLGILAASKGLVAGDLRLLMTNGDVLDSSLYGGPLTLPTDPEKIDRIETLAEFVLIVEKESVFESLLSRNVFGTFERRFILITGKGYPDCCTRRIVHRLTEENQLAAYILVDADPFGVEIMLVYRHGSKSMSFSSQGLTTPALRWIGLHPSEIPALGTGAVALVAGDNKKINDLLARHDLEPGVRQELRMLQDVQLKAEIESVIDFLTDDYIPNKINRNLFL | Function: Required for meiotic recombination . Together with mei-P22, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 37064
Sequence Length: 331
Subcellular Location: Nucleus
EC: 5.6.2.2
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Q8SVS9 | MALAPTSSAISGSLRSSMLKLLMRLKSRTLATRLRLYEIIIEMQELGITRNEREIFYMDVNVFRTQSVVRRLVSSIASELQISKHDLGVRNTLKGIFIGRLGFVRHHGLGMVEMSSKGGCPQLIPDMSDIAEVLCDYKKTVVVEKDTVLQRIASEIEREKCLEEILFVCGKGYPCKNTVLLLKMIEHKTAVAGLFDLDPFGIHIFCIYKYGSKETPDIRVETIMRIGVCMEDVLEKNAYKDVFVKLNVHDLKMINRLVRFGELSADLLFLRKIDGKVEMEALFSKEPRRLRYFLFRMLERISS | Function: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 34749
Sequence Length: 303
Subcellular Location: Nucleus
EC: 5.6.2.2
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Q9Y5K1 | MAFAPMGPEASFFDVLDRHRESLLAALRRGGREPPTGGSRLASSSEVLASIENIIQDIITSLARNEAPAFTIDNRSSWENIKFEDSVGLQMVSHCTTRKIKSDSPKSAQKFSLILKILSMIYKLVQSNTYATKRDIYYTDSQLFGNQTVVDNIINDISCMLKVSRRSLHILSTSKGLIAGNLRYIEEDGTKVNCTCGATAVAVPSNIQGIRNLVTDAKFVLIVEKDATFQRLLDDNFCNKLSPCIMITGKGVPDLNTRLLVKKLWDTFHVPVFTLVDADPHGIEIMCIYKYGSMSMSFEAHHLTVPAIRWLGLLPSDLKRLNVPKDSLIPLTKRDQMKLDSILRRPYVTCQPFWRKEMEIMADSKMKAEIQALTFLSSDYLSRVYLPNKLKFGGWI | Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with TOP6BL, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles. Essential for the phosphorylation of SMC3, HORMAD1 and HORMAD2.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 44537
Sequence Length: 396
Subcellular Location: Nucleus
EC: 5.6.2.2
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Q9WTK8 | MAFAPMGPEASFFDALDRHRASLLAMVKRGAGETPAGATRVASSSEVLTAIENIIQDIIKSLARNEVPAFTIDNRSSWENIMFDDSVGLRMIPQCTTRKIRSDSPKSVKKFALILKVLSMIYKLIQSDTYATKRDIYYTDSQLFGNQAAVDSAIDDISCMLKVPRRSLHVLSTSKGLIAGNLRYMEEDGTRVQCTCSATATAVPTNIQGMQHLITDAKFLLIVEKDATFQRLLDDNFCSRMSPCIMVTGKGVPDLNTRLLVKKLWDTFHIPVFTLVDADPYGIEIMCIYKYGSMSMSFEAHNLTIPTIRWLGLLPSDIQRLNIPKDSLIPLTKHDQMKLDSILKRPYITYQPLWKKELEMMADSKMKAEIQALTLLSSDYLSRVYLPNKLRFGGWI | Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with TOP6BL, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination . The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles. Essential for the phosphorylation of SMC3, HORMAD1 and HORMAD2 .
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 44570
Sequence Length: 396
Subcellular Location: Nucleus
EC: 5.6.2.2
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C4VB43 | MKNNLKVKLEELVIYILKNIKRYPNIIQRLKFYEQIHLGLTLNKIKNKREIYYNSVSIFKKQSIVDMLIKDTCNKLKCTQSDLLISTTLKGVFYGNITFYKNNKLVHVNLKGTSLIPDMNQIDRIEYTQKKCLIIEKDTIFSKTVREYISNDILFICGKGYPCRNTLLLVNKLNIRKYGIFDFDPYGLEICTKYPSIKKIGIDIKDINLIDKQHFMILNKYDIRKINTLLKQKVYEIELFYMLKNNIKIEIEGLFSAKGFDINNYFYTKII | Function: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 32095
Sequence Length: 271
Subcellular Location: Nucleus
EC: 5.6.2.2
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Q5ZPV8 | MAGREKRRRVAALDGEERRRRQEEAATLLHRIRGLVRWVVAEVAAGRSPTVALHRYQNYCSSASAAAASPCACSYDVPVGTDVLSLLHRGSHASRLNVLLRVLLVVQQLLQQNKHCSKRDIYYMYPSIFQEQAVVDRAINDICVLFKCSRHNLNVVPVAKGLVMGWIRFLEGEKEVYCVTNVNAAFSIPVSIEAIKDVVSVADYILIVEKETVFQRLANDKFCERNRCIVITGRGYPDIPTRRFLRYLVEQLHLPVYCLVDADPYGFDILATYKFGSLQLAYDANFLRVPDIRWLGVFTSDFEDYRLPDCCLLHLSSEDRRKAEGILSRCYLHREAPQWRLELEAMLQKGVKFEIEALSACSISFLSEEYIPKKIKQGRHI | Function: Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity). May be involved in plant growth and development, and stress tolerance.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 43560
Sequence Length: 381
Subcellular Location: Nucleus
EC: 5.6.2.2
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Q8BWU1 | MNWTAATCWALLLAAAFLCDSCSAKGGRGGARGSARGVRGGARGASRVRVRPAPRYGSSLRVAAAGAAAGAAAGVAAGLATGSGWRRTSGPGELGLEDDENGAMGGNGTDRGVYSYWAWTSGSGSVHSPRICLLLGGTLGALELLRP | Function: Prion-like protein that has PrP(C)-like neuroprotective activity. May act as a modulator for the biological actions of normal and abnormal PrP.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 14591
Sequence Length: 147
Subcellular Location: Cell membrane
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Q5BIV7 | MNWTTATCWALLLATAFLCDSCSAKGGRGGARGSARGVRGGARGASRVRVRPAPRYSSSLRVAAAGAAAGAAAGVAAGLATGSGWRRTSGPGELGLEDDENGAMGGNGTDRGVYSYWAWTSGSGSVHSPRICLLLSGTLGALELLRP | Function: Prion-like protein that has PrP(C)-like neuroprotective activity. May act as a modulator for the biological actions of normal and abnormal PrP (By similarity).
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 14712
Sequence Length: 147
Subcellular Location: Cell membrane
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A2BDG5 | MRGTSAVCWSLLLLIALLSQNVTAKGGRGGARGGARGASRGASRVRLKTSSRYGSLRVASQAAAAGAAARAAARLSENTWRNNDHSGMDTQFGNSTNEGMYSYRAWTSGTCPLSSHLSFRLIISIGAILTCSSSSIYVSTKINLGK | Function: Prion-like protein that has PrP(C)-like neuroprotective activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 15246
Sequence Length: 146
Subcellular Location: Cell membrane
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Q93704 | MNYEVYCGNAHAEPNSSAVQQLAEACVEQDASYFDGCSRTCVKDKYLLPLTQFDNLEIVVYGQIFPILVLFAVFANAAVALVLSKKHMITPTNVVLKYMAIAELLVGLVPLPWTLFFFSMGNIKETHRLELWWCYLQKYSMDAFPPVFHMIAMWLTVLLAAQRYVSISHPLHSRSACNVKNVRLATMIITVTSFLCGLPKSFDYEYETVHGWIYSHGNWTYASSCVMMPTAILTNMGQTVYFNIYFWTRALGFIILPSFLLVLLNGLLIKGIRRAQRRKLRLLREKRSEEAARQRDSNSTSLMLVAIVSIFLIVNLPQAIFMGLLCVCETFTIKIPILEGTFPAVFLIASNMIVIATYPINFGIYCFMSSSFRQTFKLLFCPGASQLQCERRIEAASAVHSSRRRSDICSHLVNVCTNSEGFMQVSHHCLHVDYLVSDRQSTQFTTMDRSD | Function: G-protein coupled receptor for the neuropeptide like protein nlp-38 . Plays a role in several types of aversive gustatory associative learning including gustatory plasticity and salt avoidance learning . Its role in salt avoidance learning may be through activation of the transcription factor crh-1/CREB and de novo transcription and translation, which in turn promotes the formation of long-term memory .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51217
Sequence Length: 451
Subcellular Location: Cell membrane
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Q96PI1 | MSSQQQQRQQQQCPPQRAQQQQVKQPCQPPPVKCQETCAPKTKDPCAPQVKKQCPPKGTIIPAQQKCPSAQQASKSKQK | Function: Cross-linked envelope protein of keratinocytes. Involved in UV-induced cornification.
PTM: Cross-linked to membrane proteins by transglutaminase.
Sequence Mass (Da): 8793
Sequence Length: 79
Subcellular Location: Cytoplasm
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A6LKE9 | MKIAFFNPQGNFDKKDSHLTEHPDFGGQLIYVKELAKAMGKMGNKVDIITRKIIDKKWPEFSGDFDYYPDAENVRIVRIAFGGDKFLNKERLWDFLGEYVKNIYRFYQKEGFPDFVTTHYGDGGIAGAMFKKLTHIPYSFTAHSLGAQKKDKFKNAKDAEERYRFSIRISAEKVAMKYASFIVTSTQQEKEEQYSHNEYIDVYPEIKDKIFVIPPGVNTNIFYPDDTDEYKFSKLPIIVSSRLDPKKNIEFVIESFNKYLKDGFELIIVLRKKPEEYTGYERQLIEKAKKAKGKFLVITSQKELAKLYNSAAKHRGIFALTSHYEPFGLAIIEAMACKLPVISTRNGGPVEILDNGKYGHLVSTHEEFKEAALKIKDNYEKLSEESYKRVMEKYTWERCAKEYLNLIEKENVILPEFFEKQMG | Function: Plays a role in sucrose synthesis by catalyzing the first step of sucrose biosynthesis from UDP-glucose and fructose-6-phosphate.
Catalytic Activity: beta-D-fructose 6-phosphate + UDP-alpha-D-glucose = H(+) + sucrose 6(F)-phosphate + UDP
Sequence Mass (Da): 49174
Sequence Length: 423
EC: 2.4.1.14
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Q96N96 | MTSASPEDQNAPVGCPKGARRRRPISVIGGVSLYGTNQTEELDNLLTQPASRPPMPAHQVPPYKAVSARFRPFTFSQSTPIGLDRVGRRRQMRASNVSSDGGTEPSALVDDNGSEEDFSYEDLCQASPRYLQPGGEQLAINELISDGNVVCAEALWDHVTMDDQELGFKAGDVIQVLEASNKDWWWGRSEDKEAWFPASFVRLRVNQEELSENSSSTPSEEQDEEASQSRHRHCENKQQMRTNVIREIMDTERVYIKHLRDICEGYIRQCRKHTGMFTVAQLATIFGNIEDIYKFQRKFLKDLEKQYNKEEPHLSEIGSCFLQNQEGFAIYSEYCNNHPGACLELANLMKQGKYRHFFEACRLLQQMIDIAIDGFLLTPVQKICKYPLQLAELLKYTTQEHGDYSNIKAAYEAMKNVACLINERKRKLESIDKIARWQVSIVGWEGLDILDRSSELIHSGELTKITKQGKSQQRTFFLFDHQLVSCKKDLLRRDMLYYKGRLDMDEMELVDLGDGRDKDCNLSVKNAFKLVSRTTDEVYLFCAKKQEDKARWLQACADERRRVQEDKEMGMEISENQKKLAMLNAQKAGHGKSKGYNRCPVAPPHQGLHPIHQRHITMPTSVPQQQVFGLAEPKRKSSLFWHTFNRLTPFRK | Function: Acts as guanine nucleotide exchange factor (GEF) for RHOA, RAC1 and CDC42 GTPases. Regulates cell migration and adhesion assembly and disassembly through a RAC1, PI3K, RHOA and AKT1-dependent mechanism. Increases both RAC1 and CDC42 activity, but decreases the amount of active RHOA. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Involved in tumor angiogenesis and may play a role in intestinal adenoma formation and tumor progression.
Sequence Mass (Da): 74820
Sequence Length: 652
Domain: The C-terminal tail is required for its GEF activity.
Subcellular Location: Cytoplasm
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P21454 | MLILNGFSSATLALITPPFLPKGGKALSQSGPDGLASITLPLPISAERGFAPALALPYSSGGGNGPFGVGWSCATMSIARRTSHGVPQYNDSDEFLGPDGEVLVQTLSTGDAPNPVTCFAYGDVSFPQSYTVTRYQPRTESSFYRLEYWVGNSNGDDFWLLHDSNGILHLLGKTAAARLSDPQAASHTAQWLVEESVTPAGEHIYYSYLAENGDNVDLNGNEAGRDRSAMRYLSKVQYGNATPAADLYLWTSATPAVQWLFTLVFDYGERGVDPQVPPAFTAQNSWLARQDPFSLYNYGFEIRLLRLCRQVLMFHHFPDELGEADTLVSRLLLEYDENPIRTQLCAARTLAYEGDGYRRAPVNNMMPPPPPPPMMGGNSSRPKSKWAIVEESKQIQALRYYSAQGYSVINKYLRGDDYPETQAKETLLSRDYLSTNEPSDEEFKNAMSVYINDIAEGLSSLPETDHRVVYRGLKLDKPALSDVLKEYTTIVNIIIDKAFMSTSPDKAWINDTILNIYLEKGHKGRILGDVAHFKGEAEMLFPPNTKLKIESIVNCGSQDFASQLSKLRLSDDATADTNRIKRIINMRVLNS | Function: Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin on 'Arg-177'. ADP-ribosylates all actins tested, has more activity on nonmuscle beta/gamma-actin than on muscle alpha-actin. Prefers monomeric G-actin but can weakly ADP-ribosylate F-actin. ADP-ribosylation prevents the polymerization of G-actin to F-actin, causing actin filament depolymerization, destruction of the cytoskeleton and cytotoxicity. Does not possess NAD(+)-glycohydrolase activity, unlike most mART enzymes.
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 65441
Sequence Length: 591
Subcellular Location: Secreted
EC: 2.4.2.31
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P0DPK6 | MTVNEIDLPPIFCPLESARHPRAHLVDERAREWIRTSPMCTTDEERTWVAASCSTDFFARFAPDAATDDRLLWTSLWVYWGFAFDDHRCDNGPFSNRPAAFSALAGRVQRALEAPSARDESDGFIPALQEIAAQFRSFGTPLQVRRFAAAHRAWLSGVTWQIGNAAAGRMPGLDEYVAMRLLSAGGEPPFAMLELATGLEVPAQDLERPAVRALTEMAIMVAALDNDRHSLRKELARGQTDQNVYSVLMQETGLPLQEAVAAATRLRDRVLLRFMAVHDRVRPGAGLELSTYLQGLRYGIRGNAEWGLRVPRYLSLGRVPDPMDEAPLEWAESPADDDRSAPRGLPTVAWWWDDALLGV | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the formation of (3R,6R,10S,11R,14R)-spiroviolene from geranylgeranyl diphosphate (GGPP) via a 1,11-cyclization and a 10Re,14Si-cyclization.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = (-)-spiroviolene + diphosphate
Sequence Mass (Da): 39968
Sequence Length: 359
Domain: The Asp-Asp-Xaa-Xaa-Xaa-Asp (DDXXXD) and Asn-Xaa-Xaa-Xaa-Ser-Xaa-Xaa-Xaa-Glu (NSE) motifs are important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.158
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O82422 | MESLQGKESNGAVPVCNGGGGAAAPPAKQQLPEGTDALRYANILRSRNKFADALQLYTTVLDKDGANVEALIGKGICLQAQSLPRQALDCFTEAVKVDPKNACALTHCGMIYKDEGHLVEAAEAYQKARSADPSYKAASEFLAIVLTDLGTSLKLAGNTEDGIQKYCEALEVDSHYAPAYYNLGVVYSEMMQFDVALTCYEKAALERPLYAEAYCNMGVIYKNRGELDAAIACYDRCLTISPNFEIAKNNMAIALTDLGTKVKIEGDINQGVAYYKKALFYNWHYADAMYNLGVAYGEMLNFEMAIVFYELALHFNPRCAEACNNLGVIYKDRDNLDKAVECYQMALSIKPNFSQSLNNLGVVYTVQGKMDAAASMIEKAILANPTYAEAYNNLGVLYRDAGSITLSVQAYERCLQIDPDSRNAGQNRLLAMNYIDEGSDDKLYDAHREWGKRFMKLYAQYTSWDNPKVADRPLVIGYVSPDFFTHSVSYFVEAPLTHHDYTKCKVVVYSGVVKADAKTLRFKDKVLKKGGVWRDIYGIDEKKVATLVREDKVDILVELTGHTANNKLGTMACRPAPIQVTWIGYPNTTGLPAIDYRITDSLADSPNTNQKHVEELVRLPESFLCYTPSPEAGPVCPTPAISNGFITFGSFNNLAKITPKVMQVWARILCAVPNSRLVVKCKPFCCDSIRQKFLSTLEELGLESLRVDLLPLIHLNHDHMQAYSLMDISLDTFPYAGTTTTCESLYMGVPCVTMAGSVHAHNVGVSLLTKVGLGRLVAKTEDEYVSLALDLASDVSALEELRKSLRELMIKSPVCDGESFTRGLESAYRSMWHRYCDGDSPALRRLEVLADQTGEDLNKTAVKLADLKAQRVNATAEEDNQSPVTKFDATSKGGEQPQPQIMVNGVTSPEGNQAVKAQPQIMVNGVSSPHSPSGRCEANGHSSR | Function: Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins.
Catalytic Activity: L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP
Sequence Mass (Da): 103828
Sequence Length: 944
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Nucleus
EC: 2.4.1.255
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Q32L17 | MEVPTLSKTRKPPDLNEESLDLGIMIALFEIGSIPPVSCSSLPSLKSSDHEATEQRIAKKFESLLKEIKDIVKHVTSYEQKVTETKEPFKETNMFEVSELREKIIELDEINKELVKKLLASLDLGKKENAKKQEMRLDNQNSEDTVQDCSGDLVNCSKGQKALPETQLSKEKAKHGFPHIQEENIRLRNNMERLLQEAEHWSVEHTELSKLIKSYQKSQNDIKTLKNNGTHSPTQTNNESAKQELEEQVKRLKEDTYSLHLIATLLENECQILEQRVELLDELHHQKEEPLQGEPMQINHEQSDKEQKLPEAEKVKIHEKNMPEVEGTFHKRDQFFTSLDICHNKKAHNNQFNTRIAKRALVVKRPASSLS | Function: Transcription factor that binds to the DNA sequence 5'-CANNTG-3'(E box) and the G-box motif. May play an important role in the regulation of cell proliferation and differentiation during spermatogenesis (By similarity).
PTM: Phosphorylated by MAPK1/ERK2 and MAPK3/ERK1.
Sequence Mass (Da): 42777
Sequence Length: 371
Subcellular Location: Cytoplasm
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Q9BXG8 | MASSAKSAEMPTISKTVNPTPDPHQEYLDPRITIALFEIGSHSPSSWGSLPFLKNSSHQVTEQQTAQKFNNLLKEIKDILKNMAGFEEKITEAKELFEETNITEDVSAHKENIRGLDKINEMLSTNLPVSLAPEKEDNEKKQEMILETNITEDVSAHKENIRGLDKINEMLSTNLPVSLAPEKEDNEKKQQMIMENQNSENTAQVFARDLVNRLEEKKVLNETQQSQEKAKNRLNVQEETMKIRNNMEQLLQEAEHWSKQHTELSKLIKSYQKSQKDISETLGNNGVGFQTQPNNEVSAKHELEEQVKKLSHDTYSLQLMAALLENECQILQQRVEILKELHHQKQGTLQEKPIQINYKQDKKNQKPSEAKKVEMYKQNKQAMKGTFWKKDRSCRSLDVCLNKKACNTQFNIHVARKALRGKMRSASSLR | Function: Transcription factor that binds to the DNA sequence 5'-CANNTG-3'(E box) and the G-box motif. May play an important role in the regulation of cell proliferation and differentiation during spermatogenesis (By similarity).
PTM: Phosphorylated by MAPK1/ERK2 and MAPK3/ERK1.
Sequence Mass (Da): 49445
Sequence Length: 430
Subcellular Location: Cytoplasm
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Q99MY0 | MSDTDNSAEMPARCPSPNPAPGAKQEPPNSGITISLLEIGSLPTVCYHSFPPPKNSICPVEKRGRVQKFSNLLKDVKDVLKNIAGVEEKSTVGEPFDDAYIPEDLSELNVRGVEKKNKIRFKDDLFIHFDPEREQNTMKQMLLKNQSAKNMVPKFARDLCNAEETRGFDGMLLSVKRPRNGSLHLRGEYRKLRNNMEQLLQEADHWSKQHNELSELMRSYQECQNETQETTDKDRACLQNQPNNGLSTKQKLEEQVKKLSHDTHALHLIAALLENECQVLQQRVDILKDFHLHEAGLGHEKPLQMSCEQDKKCPKLAEADKTDAFKHTTRATEGTIRKPKILRSPDVCFTKKARNNRFNARVAKKSLVGKRRTVSSFR | Function: Transcription factor that binds to the DNA sequence 5'-CANNTG-3'(E box) and the G-box motif. Directly binds to a guanine-rich region of the PCNA promoter and up-regulates its expression which in turn induces cell transformation and tumor formation. May play an important role in the regulation of cell proliferation and differentiation during spermatogenesis.
PTM: Phosphorylated by MAPK1/ERK2 and MAPK3/ERK1.
Sequence Mass (Da): 43091
Sequence Length: 378
Subcellular Location: Cytoplasm
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Q96JX3 | MSLAAYCVICCRRIGTSTSPPKSGTHWRDIRNIIKFTGSLILGGSLFLTYEVLALKKAVTLDTQVVEREKMKSYIYVHTVSLDKGENHGIAWQARKELHKAVRKVLATSAKILRNPFADPFSTVDIEDHECAVWLLLRKSKSDDKTTRLEAVREMSETHHWHDYQYRIIAQACDPKTLIGLARSEESDLRFFLLPPPLPSLKEDSSTEEELRQLLASLPQTELDECIQYFTSLALSESSQSLAAQKGGLWCFGGNGLPYAESFGEVPSATVEMFCLEAIVKHSEISTHCDKIEANGGLQLLQRLYRLHKDCPKVQRNIMRVIGNMALNEHLHSSIVRSGWVSIMAEAMKSPHIMESSHAARILANLDRETVQEKYQDGVYVLHPQYRTSQPIKADVLFIHGLMGAAFKTWRQQDSEQAVIEKPMEDEDRYTTCWPKTWLAKDCPALRIISVEYDTSLSDWRARCPMERKSIAFRSNELLRKLRAAGVGDRPVVWISHSMGGLLVKKMLLEASTKPEMSTVINNTRGIIFYSVPHHGSRLAEYSVNIRYLLFPSLEVKELSKDSPALKTLQDDFLEFAKDKNFQVLNFVETLPTYIGSMIKLHVVPVESADLGIGDLIPVDVNHLNICKPKKKDAFLYQRTLQFIREALAKDLEN | Function: Plays an important role in the phosphatidylglycerol remodeling that is essential for both mitochondrial function and intracellular cholesterol trafficking. May catalyze the remodeling of phosphatidylglycerol and be involved in the transacylation-acylation reaction to produce phosphatidylglycerol-36:1. May be involved in bis(monoacylglycerol)phosphate biosynthetic pathway.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74147
Sequence Length: 654
Subcellular Location: Membrane
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Q60598 | MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDRSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYKTGFGGKFGVQSERQDSSAVGFDYKERLAKHESQQDYAKGFGGKYGVQKDRMDKNASTFEEVVQVPSAYQKTVPIEAVTSKTSNIRANFENLAKEREQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARAKKQTPPASPSPQPIEDRPPSSPIYEDAAPFKAEPSYRGSEPEPEYSIEAAGIPEAGSQQGLTYTSEPVYETTEAPGHYQAEDDTYDGYESDLGITAIALYDYQAAGDDEISFDPDDIITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ | Function: Contributes to the organization of the actin cytoskeleton and cell shape . Plays a role in the formation of lamellipodia and in cell migration (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density . Plays a role in focal adhesion assembly and turnover (By similarity). In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (By similarity). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane . Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity). Required for stabilization of KCNH1 channels at the cell membrane (By similarity).
PTM: Acetylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 61250
Sequence Length: 546
Domain: The SH3 motif may mediate binding to the cytoskeleton.
Subcellular Location: Cytoplasm
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Q66HL2 | MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDKSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYAKGFGGKYGVQKDRMDKNASTFEEVVQVPSAYQKTVPIEAVTSKTSNIRANFENLAKEREQEDRRKAEAERAQRMAQERQEQEEARRKLEEQARAKKQTPPASPSPQPAEDRPPSSPIYEDAAPLKAEPSYGSSEPEPEYSTEAAGLPEASNQQGLAYTSEPVYETTEVPGHYQAEDDTYDGYESDLGITAIALYDYQAAGDDEISFDPDDVITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ | Function: Contributes to the organization of the actin cytoskeleton and cell shape . Plays a role in the formation of lamellipodia and in cell migration . Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones . Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (By similarity). Plays a role in focal adhesion assembly and turnover . In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (By similarity). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (By similarity). Plays a role in receptor-mediated endocytosis via clathrin-coated pits . Required for stabilization of KCNH1 channels at the cell membrane (By similarity).
PTM: Acetylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56942
Sequence Length: 509
Domain: The SH3 motif may mediate binding to the cytoskeleton.
Subcellular Location: Cytoplasm
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Q4WND5 | MNNEALAEDPPTPLWELVLEQFKDQLVLILLGSAAVSFVLALFEEGDDWTAFVDPVVILTILILNAVVGVTQESSAEKAIAALQEYSANEATVVRDGKTQRIKAEDLVPGDIIHIGVGDRVPADCRLLAIQSNSFRVDQAVLTGESESVSKDTRSIKDEQAVKQDQTNILFSGTSVVNGHATAIVVLTGASTAIGGIHESITSQISEPTPLKQKLNDFGDMLAKVITVICVLVWLINVEHFNDPAHGGWAKGAIYYLKIAVSLGVAAIPEGLAVVITTCLALGTRKMAAKNAVVRSLPSVETLGSCSVICSDKTGTLTTNQMSVEKLVYLNASGDDLEEIDVEGTTFAPEGKLSRNGKVLQNLAVTSSTVRQMAEVMALCNSATLAHDPKSGTFSCIGEPTEGALRVLVEKIGTDDMATNEKLFRLPASQRLHVSSAHYESRLPLLATYEFSRDRKSMSVLVTKDKAQRLLVKGAPESILERCSYVLLGPDGPRVPLTRVYSDLLAREVVEYGNRGLRVIALASVDDIADNPLLHNAQTTEEYAQLERNMTLIGLVGMLDPPRTEVADSVKKCRAAGIRVIVITGDNRNTAESICRQIGVFGEDEDLTGKSFTGREFDALSESEKLEAVKKASLFSRTEPSHKSKLVDLLQSLGHVVAMTGDGVNDAPALKKADIGVAMGTGTDVAKLAADMVLTDDNFATITVAVEEGRSIYSNTQQFIRYLISSNIGEVVSIFLTAALGMPEALIPVQLLWVNLVTDGLPATALSFNPPDHDVMRRAPRKRDEPLVGGWLLFRYLAIGTYVGAATVFGYIWWFVYNPEGPQISFWQLSHFHKCSAQFPEIGCEMFSNEMSRSASTVSLSILVVIEMLNAMNALSSSESLLAFPLWNNMMLVYAIILSMTLHFAILYIPFLQTLFSILPLNWTEWKAVLAISAPVVAIDELLKYAERRLYTLPAIAGEQQNGVAFKPKKA | Function: Magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the endoplasmic reticulum lumen (Probable). Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the endoplasmioc reticulum is important for redox homeostasis, virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling . With pmrA, promotes radial growth and conidiation .
Catalytic Activity: ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105361
Sequence Length: 971
Subcellular Location: Endoplasmic reticulum membrane
EC: 7.2.2.10
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Q86TD4 | MRALVLLGCLLASLLFSGQAEETEDANEEAPLRDRSHIEKTLMLNEDKPSDDYSAVLQRLRKIYHSSIKPLEQSYKYNELRQHEITDGEITSKPMVLFLGPWSVGKSTMINYLLGLENTRYQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMAADSARSFSPLEKFGQNFLEKLIGIEVPHKLLERVTFVDTPGIIENRKQQERGYPFNDVCQWFIDRADLIFVVFDPTKLDVGLELEMLFRQLKGRESQIRIILNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVYVSSFWPQEYKPDTHQELFLQEEISLLEDLNQVIENRLENKIAFIRQHAIRVRIHALLVDRYLQTYKDKMTFFSDGELVFKDIVEDPDKFYIFKTILAKTNVSKFDLPNREAYKDFFGINPISSFKLLSQQCSYMGGCFLEKIERAITQELPGLLGSLGLGKNPGALNCDKTGCSETPKNRYRKH | PTM: N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54431
Sequence Length: 473
Subcellular Location: Sarcoplasmic reticulum lumen
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Q7TQ48 | MKALLLLCCFLASLLLSGQAEVEDASEEAPLRDRSHIDKTLMLNEDKPADDYSAVLQRLRKIYHTSIKPLEQSYKYNELRQHEITDGEITSKPMVLFLGPWSVGKSTMINYLLGLEDTRYQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMAADSARSFSPLEKFGQNFLEKLIGIEVPHKLLERVTFVDTPGIIENRKQQERGYPFNDVCQWFIDRADLIFVVFDPTKLDVGLELEMLFRQLKGRESQIRIILNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVYVSSFWPQDYKPDTHRELFLKEEISLLEDLNQVIENRLENKIAFIRQHAIRVRIHALLVDRYLQTYKDKMTFFSDGELVFKDIVEDPDKFYIFKTILAKTNVSKFDLPNREAYKDFFGINPISNFKLLSQQCSYMGGCFLEKIERAITQELPSLLGSIGLGKNPGAPNCDKTGCGETPKNRYKKH | PTM: N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54287
Sequence Length: 472
Subcellular Location: Sarcoplasmic reticulum lumen
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Q55025 | MIRIRNRWFRWLAIALASLVASIGIATVGFAATGVTPDQVLSAIEGTFGVNVGQRRNHIKGTCAVGNFVATTEAKTYSRSPLFSGQSIPVVARFSLAGGNPKAPDTAKNPRGLGLQFQLPNNRFLNMALLNTPVFGVASPEGFYENILAIRPDPTTGKPDPEKVKAFREKYPENKAQAAFLASNNPPTSYANTSYFGLHAFKFINQTNQTRLVRWQFVPQDGEKRLTDAELQAAPANFLEQKLIERTQDSPVKWDFWITLGQPGDAEDNPTIAWPSDRQQVKVGTLTLTAASPQPGAACEGINYDPLVLSDGIEPTNDPVLQFRSGVYALSYSKRTRGL | Function: Has an organic peroxide-dependent peroxidase activity.
Sequence Mass (Da): 37055
Sequence Length: 339
Subcellular Location: Periplasm
EC: 1.11.1.-
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O13950 | MDGTSQAFKIIVATIIIGAIISTLGIFFTRKTIQKKLPAVFLIGPSDSGKTSLFCELIYKEKKTTVPSIEPNEAVWKYGAWLVDLPGHPRAKRWITTKFSGNYNVKAVVFVLNSATIDRDVHEVGLMLFDTILKCRKHHVPHLLIACNKFDLFTAQPAEKIQQLLKAELHNILEEKNLQLESIVSEDVDWESVADQIEDTDLKFLPGSVAKMSNIEEWISWMESALQ | Function: Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25612
Sequence Length: 227
Subcellular Location: Endoplasmic reticulum membrane
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P36057 | MLSNTLIIACLLVIGTTIALIAVQKASSKTGIKQKSYQPSIIIAGPQNSGKTSLLTLLTTDSVRPTVVSQEPLSAADYDGSGVTLVDFPGHVKLRYKLSDYLKTRAKFVKGLIFMVDSTVDPKKLTTTAEFLVDILSITESSCENGIDILIACNKSELFTARPPSKIKDALESEIQKVIERRKKSLNEVERKINEEDYAENTLDVLQSTDGFKFANLEASVVAFEGSINKRKISQWREWIDEKL | Function: Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26974
Sequence Length: 244
Subcellular Location: Endoplasmic reticulum membrane
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Q59967 | MSLSPRSDRTEIRRSWGLDSIVSALSQASTDPLPHHLLSDQFYPLPSRESLGLILHGLRSVLFPRHFGDPELSVETTHYFIGNTLDKTLNLLNEQIRRELWLQHVTQGTPEATPAVLSQHASELTQAFAQALPEIKRLLDSDVNAAYLGDPAAQSISEILFCYPGITAITFHRLAHRLYQLGLPLLARITAEVSHSETGIDIHPGAAIGGSFFIDHGTGVVIGETCVIGDRVRIYQAVTLGAKSFPRDETGALIKGQARHPVIEDDVVIYAGATLLGRITVGRGSTIGGNVWLTRSVPAGSFISQAQIRSDNFESGGGI | Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Sequence Mass (Da): 34570
Sequence Length: 319
Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.3.1.30
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Q96SB4 | MERKVLALQARKKRTKAKKDKAQRKSETQHRGSAPHSESDLPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVERPLKENPPNKMTQEKLEESSTIGQDQTLMERDTEGGAAEINCNGVIEVINYTQNSNNETLRHKEDLHNANDCDVQNLNQESSFLSSQNGDSSTSQETDSCTPITSEVSDTMVCQSSSTVGQSFSEQHISQLQESIRAEIPCEDEQEQEHNGPLDNKGKSTAGNFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEEYTRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLPMLELIPEKRATAAECLRHPWLNS | Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 74325
Sequence Length: 655
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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O70551 | MERKVLALQARKKRTKAKKDKAQRKPETQHRGSAPHSESDIPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNGEMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVDRPLTENPPNKMTQEKLEESNSIGQDQTLTERGGEGGAPEINCNGVIGVVNYPENSNNETLRHKEDLHNANDCDVHTLKQEPSFLNSSNGDSSPSQDTDSCTPTASETMVCQSSAEQSLTRQDITQLEESIRADTPSGDEQEPNGALDSKGKFSAGNFLINPLEPKNAEKLQVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEDYTRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLLEVLVEKYEWPQEEAAGFTDFLLPMLELMPEKRATAAECLRHPWLNS | Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Phosphorylates SFRS2, ZRSR2, LBR and PRM1. Phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Can induce splicing of exon 10 in MAPT/TAU (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 73088
Sequence Length: 648
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P78362 | MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPPPLPDPTPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKIIEENITSAAPSNDQDGEYCPEVKLKTTGLEEAAEAETAKDNGEAEDQEEKEDAEKENIEKDEDDVDQELANIDPTWIESPKTNGHIENGPFSLEQQLDDEDDDEEDCPNPEEYNLDEPNAESDYTYSSSYEQFNGELPNGRHKIPESQFPEFSTSLFSGSLEPVACGSVLSEGSPLTEQEESSPSHDRSRTVSASSTGDLPKAKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS | Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing . Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression . This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression . Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation . Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 . Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA . Can mediate hepatitis B virus (HBV) core protein phosphorylation . Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles .
PTM: Phosphorylation at Thr-492 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB. It also enhances its protein kinase activity toward ACIN1 and SRSF2, promotes its nuclear translocation and prevents its proteolytic cleavage.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 77527
Sequence Length: 688
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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O54781 | MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPLPDPAPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKILEENITSAEASGEQDGEYQPEVTLKAADLEDTTEEETAKDNGEVEDQEEKEDAEKENAEKDEDDVEQELANLDPTWVESPKANGHIENGPFSLEQQLEDEEDDEDDCANPEEYNLDEPNAESDYTYSSSYEQFNGELPNGQHKTSEFPTPLFSGPLEPVACGSVISEGSPLTEQEESSPSHDRSRTVSASSTGDLPKTKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS | Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing . Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression . This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression (By similarity). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (By similarity). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (By similarity). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (By similarity).
PTM: Phosphorylation at Thr-485 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB. It also enhances its protein kinase activity toward ACIN1 and SRSF2, promotes its nuclear translocation and prevents its proteolytic cleavage (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 76757
Sequence Length: 681
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q05738 | MEGHVKRPMNAFMVWSRGERHKLAQQNPSMQNTEISKQLGCRWKSLTEAEKRPFFQEAQRLKILHREKYPNYKYQPHRRAKVSQRSGILQPAVASTKLYNLLQWDRNPHAITYRQDWSRAAHLYSKNQQSFYWQPVDIPTGHLQQQQQQQQQQQFHNHHQQQQQFYDHHQQQQQQQQQQQQFHDHHQQKQQFHDHHQQQQQFHDHHHHHQEQQFHDHHQQQQQFHDHQQQQQQQQQQQFHDHHQQKQQFHDHHHHQQQQQFHDHQQQQQQFHDHQQQQHQFHDHPQQKQQFHDHPQQQQQFHDHHHQQQQKQQFHDHHQQKQQFHDHHQQKQQFHDHHQQQQQFHDHHQQQQQQQQQQQQQFHDQQLTYLLTADITGWKGIKHCTGPDPEPF | Function: Transcriptional regulator that controls a genetic switch in male development . It is necessary and sufficient for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells . Involved in different aspects of gene regulation including promoter activation or repression . Binds to the DNA consensus sequence 5'-[AT]AACAA[AT]-3' . SRY HMG box recognizes DNA by partial intercalation in the minor groove and promotes DNA bending . Also involved in pre-mRNA splicing (By similarity). In male adult brain involved in the maintenance of motor functions of dopaminergic neurons (By similarity).
PTM: Degraded due to the presence of a degron at the C-terminus that promotes its degradation.
Sequence Mass (Da): 49124
Sequence Length: 392
Domain: DNA binding and bending properties of the HMG domains of mouse and human SRY differ form each other. Mouse SRY shows less extensive minor groove contacts with DNA and a higher specificity of sequence recognition than human SRY.
Subcellular Location: Nucleus speckle
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Q8ZNG2 | MNICVNSLYRLSIPQFHSLYTEEVSDEALTLLFSAVENGDQNCIDLLCNLALRNDDLGHRVEKFLFDLFSGKRTGSSDIDKKINQACLVLHQIANNDITKDNTEWKKLHAPSRLLYMAGSATTDLSKKIGIAHKIMGDQFAQTDQEQVGVENLWCGARMLSSDELAAATQGLVQESPLLSVNYPIGLIHPTTKENILSTQLLEKIAQSGLSHNEVFLVNTGDHWLLCLFYKLAEKIKCLIFNTYYDLNENTKQEIIEAAKIAGISESDEVNFIEMNLQNNVPNGCGLFCYHTIQLLSNAGQNDPATTLREFAENFLTLSVEEQALFNTQTRRQIYEYSLQ | Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease targets the host cell ubiquitin pathway by acting as a deubiquitinase in infected host cells. Specifically hydrolyzes mono- and polyubiquitin substrates in vitro with a preference for 'Lys-63'-linked ubiquitin chains, suggesting that it interferes with a signaling pathway rather than inhibiting proteasomal-dependent degradation of its targets. Does not possess desumoylating activity. Is required for the Salmonella-induced delayed cytotoxicity in macrophages and full virulence. Is not required for intracellular bacterial replication.
Sequence Mass (Da): 38221
Sequence Length: 340
Subcellular Location: Secreted
EC: 3.4.22.-
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P84766 | ATGSGGMNLVFVGAEMAPXXX | Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate + H(+)
Sequence Mass (Da): 2043
Sequence Length: 21
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.4.1.242
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Q9MAQ0 | MATVTASSNFVSRTSLFNNHGASSCSDVAQITLKGQSLTHCGLRSFNMVDNLQRRSQAKPVSAKSSKRSSKVKTAGKIVCEKGMSVIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYDQYKDAWDTCVVVQIKVGDKVENVRFFHCYKRGVDRVFVDHPIFLAKVVGKTGSKIYGPITGVDYNDNQLRFSLLCQAALEAPQVLNLNSSKYFSGPYGEDVVFVANDWHTALLPCYLKSMYQSRGVYMNAKVVFCIHNIAYQGRFAFDDYSLLNLPISFKSSFDFMDGYEKPVKGRKINWMKAAILEAHRVLTVSPYYAQELISGVDRGVELHKYLRMKTVSGIINGMDVQEWNPSTDKYIDIKYDITTVTDAKPLIKEALQAAVGLPVDRDVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQILELEEKFPGKAVGVAKFNVPLAHMITAGADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFHIGRFNVKCEVVDPDDVIATAKAVTRAVAVYGTSAMQEMVKNCMDQDFSWKGPARLWEKVLLSLNVAGSEAGTEGEEIAPLAKENVATP | Function: Required for the synthesis of amylose . Destroyed as it is released from the starch granules during the night . The circadian expression is controlled by CCA1 and LHY transcription factors .
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate + H(+)
Sequence Mass (Da): 66879
Sequence Length: 610
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.4.1.242
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P84633 | GMNLVFVGAEVAPWSKTGGLGDVLA | Function: Required for the synthesis of amylose in endosperm.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate + H(+)
Sequence Mass (Da): 2489
Sequence Length: 25
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.4.1.242
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P09842 | MAALATSQLATSGTVLGVTDRFRRPGFQGLRPRNPADAALGMRTIGASAAPKQSRKAHRGSRRCLSVVVSATGSGMNLVFVGAEMAPWSKTGGLGDVLGGLPPAMAANGHRVMVVSPRYDQYKDAWDTSVISEIKVADEYERVRFFHCYKRGVDRVFIDHPWFLEKVRGKTKEKIYGPDAGTDYEDNQQRFSLLCQAALEAPRILNLNNNPYFSGPYGEDVVFVCNDWHTGLLACYLKSNYQSNGIYRTAKVAFCIHNISYQGRFSFDDFAQLNLPDRFKSSFDFIDGYDKPVEGRKINWMKAGILQADKVLTVSPYYAEELISGEARGCELDNIMRLTGITGIVNGMDVSEWDPTKDKFLAVNYDITTALEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKGPDVMIAAIPEILKEEDVQIILLGTGKKKFEKLLKSMEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQGMRYGTPCVCASTGGLVDTIVEGKTGFHMGRLSVDCNVVEPADVKKVATTLKRAVKVVGTPAYQEMVKNCMIQDLSWKGPAKNWEDVLLELGVEGSEPGIVGEEIAPLAMENVAAP | Function: Required for the synthesis of amylose in endosperm.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate + H(+)
Sequence Mass (Da): 66211
Sequence Length: 603
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.4.1.242
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Q5AHK2 | MSYSSASFRKLNNVGISQPSQTTTTTTSANQPQSQSQQQPLQQSQQQHLHMKPNPHIPHHQLPGTVGTRTSIPQPALMASNSILTLGPFKHRKDLTRESVLSTYQIMGYIAAGTYGKVYKAKLKSNKLNKTDDDSGIDGINNKDIFSESMNDLHHDNSSSIMINTTTNITINNSLPQFFAIKKFKSDNHHHHINNNNNGGNHLSKGNNSIHQDEVLHYTGISQSAIREMSLCRELNNKNITKLVDIILENKSIYMVFEFCEHDLLQIIHYQSHPDFKPIPCPTIKSLIWQILNGVTFLHKNWILHRDLKPANIMVSSQGVVKIGDLGLARKFKSPLQSLYTGDKVVVTIWYRAPELLLGTRHYTPAVDLWAVGCILAELLSLRPIFKGEEAKIDLNNKKSVPFQKNQLQKIIEILGTPTTDIWNNLNKYPEYLSFTQHFNQNYPNNLSNWFKLINGGNNQNSEKCLELLSGLLKYDPELRLTADQALLHPYFLELPKVNENAFEGLNYKYPNRKIYTDDNDIMTTAANNNNNNNNNNNNNNNNNNNNNNNNNNNSGHQLSQQQNVQIQQVHQMQQQIHSQQLQSHGANSTYKRSGIDDLPGGIRKKRG | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68962
Sequence Length: 608
Subcellular Location: Nucleus
EC: 2.7.11.22
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P0CS77 | MATIPGGGTIMDPMHLYRARRDKERRGVLKTYKILGFISSGTYGRVYKAVLLPPPKTASAKSALPSSTRAALSLPKDKLPSPSFTEDSDPLNNPEMCMRPGDRPAKRGDVFAIKKFKPDKEGDVLTYAGISQSGAREIMLNRELHHRNLVSLREVILEDKSIYMVFEYAEHDFLQIIHYHSQTARASIPPSTLRRLLHQLLCGVHFLHSNFVLHRDLKPANILVTSQGVVKIGDLGLARLWHKPLAQQGLYGGDKVVVTIWYRAPELILGAKHYTAAVDIWAVGCIYAELLSLRPIFKGDEAKMDGKKSLPFQRDQMGKICEVLGPVKPEQWPGIVHMPEYRTYQATGPYPHSNPLAPWYHARSNSSEGYDILVKMFEWDPARRITARDALRHPWFQEEGGVDTKSVFEGSSITYPTRRVTHEDNGDAKMGSLPQSMAGGRLPSSSNFRPASGNIVQPAARKKARI | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52124
Sequence Length: 466
Subcellular Location: Nucleus
EC: 2.7.11.22
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Q6BM25 | MNSGYNPGNANHITSHSNRTKNGVPTIPQPALMASNAILTIGPYKHRKDLIRESVLTKYQIIGYIAAGTYGKVYKAKSKTNGNSNSNSALMNDNVISIGNGQKEAGLQKTNNESMEDKNQLFAIKKFKSDNHSNKNNHDINGNEVIHYTGISQSAIREMSLCRELSNKNITKVVDILLENKSIYMVFEYCEHDLLQIIQYHSHPDVKPIPDFTIKSITWQILNGVTFLHKNWIFHRDLKPANIMVSSSGVVKIGDLGLARKFNNPLQSLYTGDKVVVTIWYRAPELLLGARHYTPSIDLWAVGCILAELLSLRPIFKGEEAKIDMNNKKSVPFQKNQLQKIVEVLGTPTTKNWPTITKYPEYSAFQQHFSNTYPPNLISWYKLIGRTSKQCLNLLRCLLEYDPTIRITADDALTHAFFLELPKMSENSFEGLSQKYPKRRIYTHENDIVSNSQHVNNKRHGYDDNMTRKRQR | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 53783
Sequence Length: 472
Subcellular Location: Nucleus
EC: 2.7.11.22
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Q4FCZ5 | MPLRPHIGLGFPAHAYQKRHVEPHDRSTGYQPKVRITDRYRIIGFISSGTYGRVYKAVGRNGKPVGEFAIKKFKPDKEGEQISYTGISQSAIREMSLCSELHHINVIRLCEIVLEDKCIFMVFEYAEHDLLQIIHHHTQQPRHPIPPATIKSIMFQLLNGCQYLHINWVLHRDLKPANIMVTSSGEVKIGDLGLARRFDKPLHSLFSGDKVVVTIWYRAPELILGSYHYTPAIDMWAVGCIFAELLSLRPIFKGEEAKMDSKKTVPFRRNQMQKIIEIMGVPTKDKWPLLSTMPEYNQLNTLANSMASSHHNHHSHHHPHHHHGHYGSRNPPPPGGSNLEKWYYSTINHTSAPGGTPPLASLGSEGYKLLAGLLEYDPSKRLTAAQALQSPFFSTGDRVSANCFEGCKNEYPCRRVSQDDNDIRTSSLPGTKRSGLPDDSLIRPAKRQKE | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity). Required for normal growth and secondary metabolism.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 50892
Sequence Length: 450
Subcellular Location: Nucleus
EC: 2.7.11.22
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A4QXX4 | MSHSNPPTGASGGPGSASASAAPARGYYSLKRSIQTAFNDPLDRGLGPPAYQSKVRVMDKYQVIGFISSGTYGRVYKARGRQGQPGEFAIKKFKPDKEGEQITYTGISQSAIREMALCSELRHPNVIRLVETILEDKAIFMVFEYAEHDLLQIIHHHTQQPKHPIPPQTIKSIMFQLLNGCQYLHTNWVLHRDLKPANIMVTSSGEVKVGDLGLARIFWKPVRTLMQGDKVVVTIWYRAPELLMGSHHYTPAVDMWAVGCIFAELLSLRPIFKGEEAKMDNTKKGGSRDMPFQRHQMQKIVDIMGMPTKERWPLLTSMPDYDKLPLLQPPLSASGYSQQPAHSHHHHQHYNQGPQYGGRAGGPTSSSSANSSSAAAAASQSHLDKWYYHTVSQGQTAGPMPHAPPGSLASLGVEGYKLLAGLLEYDPEKRLTAAAALQHNFFSTGDRVSANCFEGCKAEYPHRRVSQEDNDIRTGSVPGTKRSGMPDDSMGRPGKRVKE | Function: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 55094
Sequence Length: 499
Subcellular Location: Nucleus
EC: 2.7.11.22
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Q0TWJ7 | MERKRGREMNPPSADPPSATPVARANLPGSVAAAFHGRPCSQGTTTLKRVNERYKIVGFISSGTYGRVYKAEGKNGRTGEFAIKKFKPDKEGELQYSGISQSAIREMALCTELAHPNVVHTVEIILEEKCIFIVFEYAEHDLLQIIHHHNQPQRQAIPARTIKSILYQLLQGLVYLHRNWVMHRDLKPANIMVTSAGKVKIGDLGLARLFYKPLQSLFSGDKVVVTIWYRAPELLLGSRHYTPAVDLWAVGCIFAELLSLRPIFKGEEAKMDSKKTVPFQRNQMQKIVEIMGMPSKDRWPLLTAMPEYPQLSSLIAGNAARFARPQGGDGLDRWYNQTLINNQYPAGPGPETPGAEGLALLKQLLEYDPQKRLTAEKALEHRYFTEHGKPSDNCFEDSKIKYPVRRVSQEDNDIRTSSLPGTKRSGLPDDSLMGRPAKRLKEG | Function: Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The srb8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 49756
Sequence Length: 443
Subcellular Location: Nucleus
EC: 2.7.11.22
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A3LUB9 | MASNSILTLGPFKHRKDLTRESVLSTYQIIGYIAAGTYGKVYKAKLKNTASAEQLFAIKKFKSDNHSSNRSHHNHDINGNEIVHYTGISQSAIREMSLCRELNNKNITKLVDIILENKSIYMIFEFCEHDLLQIIHYHSHPEVKPIPQATVKSLIWQILNGVTFLHQNWIFHRDLKPANIMVSSSGVVKIGDLGLARKFNNPLQSLYTGDKVVVTIWYRAPELLLGARHYTPAIDLWAVGCILAELLSLRPIFKGEEAKIDINNKKSVPFQKNQFQKIVEVLGTPSMKNWPALNKYPEFISFQQQLTTNYPPNLVNWYKMIGSSNKQCLELLKGLLEYDPLVRLTADNALVHPYFLELPKVQENAFEGLNLKYPKRRIYTDDNDIISNQAINQNFKRHGGAYDDQHNNSNNNTNNSLNANNANNVPRKRAR | Function: Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The srb8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 49251
Sequence Length: 431
Subcellular Location: Nucleus
EC: 2.7.11.22
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Q14714 | MGKNKQPRGQQRQGGPPAADAAGPDDMEPKKGTGAPKECGEEEPRTCCGCRFPLLLALLQLALGIAVTVVGFLMASISSSLLVRDTPFWAGIIVCLVAYLGLFMLCVSYQVDERTCIQFSMKLLYFLLSALGLTVCVLAVAFAAHHYSQLTQFTCETTLDSCQCKLPSSEPLSRTFVYRDVTDCTSVTGTFKLFLLIQMILNLVCGLVCLLACFVMWKHRYQVFYVGVRICSLTASEGPQQKI | Function: Component of the dystrophin-glycoprotein complex (DGC), a complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. Preferentially associates with the sarcoglycan subcomplex of the DGC.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26618
Sequence Length: 243
Subcellular Location: Cell membrane
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Q62147 | MGRKPSPRAQELPEEEARTCCGCRFPLLLALLQLALGIAVTVLGFLMASISPSLLVRDTPFWAGSIVCVVAYLGLFMLCVSYQVDERTCVQFSMKVFYFLLSALGLMVCMLAVAFAAHHYSLLAQFTCETSLDSCQCKLPSSEPLSRAFVYRDVTDCTSVTGTFKLFLIIQMVLNLVCGLVCLLACFVMWKHRYQVFYVGVGLRSLMASDGQLPKA | Function: Component of the dystrophin-glycoprotein complex (DGC), a complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. Preferentially associates with the sarcoglycan subcomplex of the DGC (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23859
Sequence Length: 216
Subcellular Location: Cell membrane
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Q1C1S0 | MTTLTHIPQGTPITLESIGKRYGNRTVLDNLQLRITAGQFVAVVGRSGCGKSTLLRLLAGLEAASDGTLLSGNALLSHAKDETRLMFQEARLLPWKKVIDNVGLGLRGHWRDEALQVLDTVGLADRANEWPAALSGGQKQRVALARALIHRPRLLLLDEPLGALDALTRIEMQGLIERLWQQHGFTVLLVTHDVSEAIALADRVLLIEEGRIGLDLAIDLPRPRRKGSAKLAALEAEVLERVLSPPQGIEASRQGIKASRQGTATSRRVAN | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29469
Sequence Length: 271
Subcellular Location: Cell inner membrane
EC: 7.6.2.14
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P40401 | MMKAEAAGSLPKTNAEAVRKKPGRKRYGWMKGLLLPAVIIAIWQVIGGLGVVSATVLPTPVTIVLTFKELILSGELFGHLQISIYRAALGFLLGAGLGLMIGILAGFSKRTELYLDPSLQMLRTVPHLAVTPLFILWFGFDEVSKILLIALGAFFPVYINTFNGIRGVDAKLFEVARVLEFKWHQQISKVILPAALPNILLGIRLSLGIAWLGLVVAELMGSSSGVGYMIMDARQFSQTNKVFAGIIIFAVVGKLTDSFVRLLERKLLKWRNSYEG | Function: Part of a binding-protein-dependent transport system for aliphatic sulfonates. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30240
Sequence Length: 276
Subcellular Location: Cell membrane
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P75851 | MATPVKKWLLRVAPWFLPVGIVAVWQLASSVGWLSTRILPSPEGVVTAFWTLSASGELWQHLAISSWRALIGFSIGGSLGLILGLISGLSRWGERLLDTSIQMLRNVPHLALIPLVILWFGIDESAKIFLVALGTLFPIYINTWHGIRNIDRGLVEMARSYGLSGIPLFIHVILPGALPSIMVGVRFALGLMWLTLIVAETISANSGIGYLAMNAREFLQTDVVVVAIILYALLGKLADVSAQLLERLWLRWNPAYHLKEATV | Function: Part of a binding-protein-dependent transport system for aliphatic sulfonates. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28925
Sequence Length: 263
Subcellular Location: Cell inner membrane
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P40402 | MEILWFIPTHGDARYLGSESDGRTADHLYFKQVAQAADRLGYTGVLLPTGRSCEDPWLTASALAGETKDLKFLVAVRPGLMQPSLAARMTSTLDRISDGRLLINVVAGGDPYELAGDGLFISHDERYEATDEFLTVWRRLLQGETVSYEGKHIKVENSNLLFPPQQEPHPPIYFGGSSQAGIEAAAKHTDVYLTWGEPPEQVKEKIERVKKQAAKEGRSVRFGIRLHVIARETEQEAWEAAERLISHLDDDTIAKAQAALSRYDSSGQQRMAVLHQGDRTKLEISPNLWAGIGLVRGGAGTALVGDPQTIADRIAEYQALGIESFIFSGYPHLEEAYYFAELVFPLLPFENDRTRKLQNKRGEAVGNTYFVKEKNA | Function: Catalyzes the desulfonation of aliphatic sulfonates.
Catalytic Activity: an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + 2 H(+) + H2O + sulfite
Sequence Mass (Da): 41802
Sequence Length: 376
EC: 1.14.14.5
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Q9LDU6 | MAETVHSPIVTYASMLSLLAFCPPFVILLWYTMVHQDGSVTQTFGFFWENGVQGLINIWPRPTLIAWKIIFCYGAFEAILQLLLPGKRVEGPISPAGNRPVYKANGLAAYFVTLATYLGLWWFGIFNPAIVYDHLGEIFSALIFGSFIFCVLLYIKGHVAPSSSDSGSCGNLIIDFYWGMELYPRIGKSFDIKVFTNCRFGMMSWAVLAVTYCIKQYEINGKVSDSMLVNTILMLVYVTKFFWWEAGYWNTMDIAHDRAGFYICWGCLVWVPSVYTSPGMYLVNHPVELGTQLAIYILVAGILCIYINYDCDRQRQEFRRTNGKCLVWGRAPSKIVASYTTTSGETKTSLLLTSGWWGLARHFHYVPEILSAFFWTVPALFDNFLAYFYVIFLTLLLFDRAKRDDDRCRSKYGKYWKLYCEKVKYRIIPGIY | Function: Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC). Lesions in the gene coding for the enzyme cause dwarfism.
Catalytic Activity: cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49591
Sequence Length: 432
Pathway: Lipid metabolism; steroid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.3.1.21
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Q9M881 | MALLLNSTITVAMKQNPLVAVSFPRTTCLGSSFSPPRLLRVSCVATNPSKTSEETDKKKFRPIKEVPNQVTHTITQEKLEIFKSMENWAQENLLSYLKPVEASWQPQDFLPETNDEDRFYEQVKELRDRTKEIPDDYFVVLVGDMITEEALPTYQTTLNTLDGVKDETGGSLTPWAVWVRAWTAEENRHGDLLNKYLYLSGRVDMRHVEKTIQYLIGSGMDSKFENNPYNGFIYTSFQERATFISHGNTAKLATTYGDTTLAKICGTIAADEKRHETAYTRIVEKLFEIDPDGTVQALASMMRKRITMPAHLMHDGRDDDLFDHYAAVAQRIGVYTATDYAGILEFLLRRWEVEKLGMGLSGEGRRAQDYLCTLPQRIRRLEERANDRVKLASKSKPSVSFSWIYGREVEL | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain (By similarity). Exhibits delta-9 palmitoyl-[acyl-carrier-protein] desaturase (PAD) activity. Involved in omega-7 monounsaturated fatty acid biosynthesis, especially in the endosperm oil .
Catalytic Activity: 2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 46950
Sequence Length: 411
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.2
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E3PZS2 | MELHLALRASPLPAADPGRRPPPPRGNFATNCTAAINSTHISQEKFRSLDSWVEHNMLTFLKPVEKCWQPQDFLPDPSHLSAEELGDAVREIHERAAEIPDEVWVCMVGNMVTEEALPTYQSLISSVLGGTVAGSTPWDRWIRGWSAEENRHGDLLNKYLYLTGRLDMRQVEKTIQYLIGSGMDVGVGNSILCGFIYTCFQEKATFISHGNTARLAKHHGDTTLAKICGLVAADEKRHAVAYTNLMKKLFEVAPNESMLAFAHIMRAHVTMPASRMFDGRDPRLFTHFSAVTQKIGVYTVRDYGEMLDFFLKEWEISAVVDDLSPEGRQAQEYVCGLPEVMGKMAERADDRRKKLVNVGEPRYIPFSWIFNKQVCV | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis double bond between carbons 4 and 5 of the acyl chain. Catalyzes the desaturation of saturated fatty acid 18:0 and 16:0 to generate 18:1 (delta-9) and 16:1 (delta-4) intermediates, expected to give rise to 9-alkenes and 12-alkenes, respectively.
Catalytic Activity: 2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = (4Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 42359
Sequence Length: 376
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.11
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Q9LF05 | MSMALLLTSPAMKQKPAVITSPRRGSSPSRRLRVSCVTTNPARKKNETCNHFRPIKEVNNQLTHTIPQEKLEIFKSMENWAEQKLLPYLKPVEDSWQPQDFLPAPENDDEFYDRVKEIRERTKEIPDDYFVVLVGDMITEEALPTYQTTLNTLDGVKDETGGSLSPWAVWIRAWTAEENRHGDLLNKYLYLTGRVDMRHVEKTIQYLIGSGMDSKFENNPYNGFIYTSFQERATFISHGNTARLATTYGDVTLAKICGTIAADEKRHETAYTKIVEKLFEIDPDGSVQALASMMKKRITMPAHLMHDGRDNDLFDHYAAVAQRIGVYTAADYAGILEFLLRRWKVESLGLGLSGEGRRAQEYLCTLPQRIKRLEERANDRVKLVSKPSVSFSWVFGRDVKL | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Also able to convert palmitoyl-ACP to palmitoleoyl-ACP at the C9 position. Exhibits delta-9 palmitoyl-[acyl-carrier-protein] desaturase (PAD) activity. Involved in omega-7 monounsaturated fatty acid biosynthesis, especially in the endosperm oil .
Catalytic Activity: 2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 45860
Sequence Length: 401
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.2
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B9F058 | MSLTGCLPPRPPCSMRRRTSGGGASVSPVVAMASTAGVGGIGNPTPRGKKPFAPWREVPPQVTHTLPPEKKEVFDSLEGWAADTILPYLKPVEESWQPQDHLPDPRSPSFGDEVAALRERAAGLPDDHLVCLVGDMVTEEALPTYQTMLNTMDGGVRDETGAGGSAWAVWTRAWAAEENRHGDLMNKYLYLTGRVDMRQVEKTIQYLIGSGMDPRTENDPYMGFIYTTFQERATSISHGNTARHAGRHGDAALARVCGTVAADEKRHEAAYAAIVAKLFEVDPDYTVRAFARMMRRKVAMPARLMYDGADDRLFARFAAVAQRLGVYTAADYAGIIEFLVARWGVPGLAAGLSGEGRRAQDFVCSLGPRFRRMEERAQEAAKRAPPAAAAPFSWIHGRQVQL | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Sequence Mass (Da): 43956
Sequence Length: 402
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.-
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Q9M879 | MAMAMDRIVFSPSSYVYRPCQARGSRSSRVSMASTIRSATTEVTNGRKLYIPPREVHVQVKHSMPPQKLEIFKSLEGWADETLLTYLKPVEKSWQPTDFLPEPESEGFYDQVKELRERCKELPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTPWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPKTENNPYLGFIYTSFQERATFISHGNTARLAKDRGDLKLAQICGTIAADERRHETAYTKIVEKLFEIDPDGTILGLADMMKKKISMPAHLMYDGQDDNLFEHFSTVAQRLGVYTAKDYADILEFLVERWNVETLTDLSSEGHRAQDFVCGLPARIRKIEERAQGRAKEAAKNIPFSWIFGRNIRA | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Catalytic Activity: 2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 45303
Sequence Length: 396
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.2
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Q84VY3 | MLAHKSLLSFTTQWATLMPSPSTFLASRPRGPAKISAVAAPVRPALKHQNKIHTMPPEKMEIFKSLDGWAKDQILPLLKPVDQCWQPASFLPDPALPFSEFTDQVRELRERTASLPDEYFVVLVGDMITEDALPTYQTMINTLDGVRDETGASESAWASWTRAWTAEENRHGDLLRTYLYLSGRVDMLMVERTVQHLIGSGMDPGTENNPYLGFVYTSFQERATFVSHGNTARLAKSAGDPVLARICGTIAADEKRHENAYVRIVEKLLEIDPNGAVSAVADMMRKKITMPAHLMTDGRDPMLFEHFSAVAQRLEVYTADDYADILEFLVGRWRLEKLEGLTGEGQRAQEFVCGLAQRIRRLQERADERAKKLKKTHEVCFSWIFDKQISV | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Catalytic Activity: 2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 44156
Sequence Length: 391
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.2
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Q0J7E4 | MAATATMAMPLANRLRCKPNTNSSSPSRTLFGRRVTMISSSRWGSAVSGSAIMSAAADVAAAVRREEDEEMRSYLSPEKLEVLTQMEPWVEEHVLPLLKPVEAAWQPSDLLPDPAVLGGEGFHAACAELRERAAGVPDLLLVCLVANMVTEEALPTYQSSLNRVRAVGDLTGADATAWARWIRGWSAEENRHGDVLNRYMYLSGRFDMAEVERAVHRLIRSGMAVDPPCSPYHAFVYTAFQERATAVAHGNTARLVGARGHGDAALARVCGTVAADEKRHEAAYTRIVSRLLEADPDAGVRAVARMLRRGVAMPTSPISDGRRDDLYACVVSLAEQAGTYTVSDYCSIVEHLVREWRVEELAAGLSGEGRRARDYVCELPQKIRRMKEKAHERAVKAQKKPISIPINWIFDRHVSVMLP | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Sequence Mass (Da): 46101
Sequence Length: 419
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.-
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O22832 | MALKFNPLVASQPYKFPSSTRPPTPSFRSPKFLCLASSSPALSSGPKEVESLKKPFTPPREVHVQVLHSMPPQKIEIFKSMENWAEENLLIHLKDVEKSWQPQDFLPDPASDGFEDQVRELRERARELPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPRTENNPYLGFIYTSFQERATFISHGNTARQAKEHGDIKLAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVMAFADMMRKKISMPAHLMYDGRNDNLFDNFSSVAQRLGVYTAKDYADILEFLVGRWKIQDLTGLSGEGNKAQDYLCGLAPRIKRLDERAQARAKKGPKIPFSWIHDREVQL | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Required for the activation of certain jasmonic acid (JA)-mediated responses and the repression of the salicylic acid (SA) signaling pathway.
Catalytic Activity: 2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 45693
Sequence Length: 401
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.2
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P13018 | MKISVIPEQVAETLDAENHFIVREVFDVHLSDQGFELSTRSVSPYRKDYISDDDSDEDSACYGAFIDQELVGKIELNSTWNDLASIEHIVVSHTHRGKGVAHSLIEFAKKWALSRQLLGIRLETQTNNVPACNLYAKCGFTLGGIDLFTYKTRPQVSNETAMYWYWFSGAQDDA | Function: Involved in resistance to streptothricin, a broad-spectrum antibiotic produced by streptomycetes . Detoxifies streptothricin via acetylation of the beta amino group of the first beta-lysyl moiety of streptothricin (By similarity).
Catalytic Activity: acetyl-CoA + streptothricin F = CoA + H(+) + N(beta)-acetylstreptothricin F
Sequence Mass (Da): 19671
Sequence Length: 174
EC: 2.3.-.-
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P08457 | MTTTHGSTYEFRSARPGDAEAIEGLDGSFTTSTVFEVDVTGDGFALREVPADPPLVKVFPDDGGSDGEDGAEGEDADSRTFVAVGADGDLAGFAAVSYSAWNQRLTIEDIEVAPGHRGKGIGRVLMRHAADFARERGAGHLWLEVTNVNAPAIHAYRRMGFAFCGLDSALYQGTASEGEHALYMSMPCP | Function: Involved in resistance to streptothricin, a broad-spectrum antibiotic produced by streptomycetes. Detoxifies streptothricin via acetylation of the beta amino group of the first beta-lysyl moiety of streptothricin.
Catalytic Activity: acetyl-CoA + streptothricin F = CoA + H(+) + N(beta)-acetylstreptothricin F
Sequence Mass (Da): 20032
Sequence Length: 189
EC: 2.3.-.-
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P42845 | MSQPQMSPEKEQELASKILHRAELAQMTRQLKLGLSNVPSTKRKQDSTTKKRSGEDAEDVDEDHKTLLEAISPAKKPLHDDTNKMTVISPVKFVEKPNTPPSSRQRKAEDRSQQIKPRKEDTPSTPRASATPIILPHASSHYQRPHDKNFMTPKRNNNNSSNHSNNNNNIKKKAAGSKDAPQDSDNTAGADLLMYLATSPYNKSSHHGTPMAVRMPTTPRSYHYASQLSLNGNTASTSNDAVRFSHIKPSASSPQSTFKSNLLPNFPDESLMDSPSLYLSNNNGSVQATLSPQQRRKPTTNTLHPPSNVPTTPSRELNGTNFNLLRTPNFNMGDYLHNLFSPSPRVPAQQGASNTSASIPSVPAMVPGSSSNTSAIATAAISSHTTNNFLDMNANGIPLIVGPGTDRIGEGESIDDKLTD | Function: Involved in the regulation and timing of MBF-dependent transcription in late G1 of the cell cycle.
PTM: Phosphorylated by CDC28 in a cell cycle-dependent manner, inhibiting the interaction with SWI6.
Sequence Mass (Da): 45684
Sequence Length: 420
Subcellular Location: Cytoplasm
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Q0UK53 | MMNPFFQNTSCSPYYRTDQPCSLGNYVSYAIPVAGVADIVAAINFTQTHNVRLVIKNTGHDYMGKSTGRGALSLWTHNLKSRQLVNYSSAHYTGPAIKVGAGVTGGEALVHASASGYRIVSGDCPTVGYSGGYSSGGGHSILNSVHGLAADNVLEWEVVTADGRHVVASPDQNSDLYWAMSGGGGGTFAVALSMTSRVHADSIIGAASLSFNATSAPSNDSFVSALNAWWAFLPSLVDVGATPSWNIFAGNFLVPNTTAPGRTAADMDTLYSPFLSELKRLGIPYAFESFSAPNYLQHYNDTDGPLPDGPLAAWA | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations . The C-terminal reductase (R) domain of sthA catalyzes the reductive release of the polyketide chain . Because sthA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase sthE . The short-chain dehydrogenase/reductase sthC then catalyzes reduction of dehydroprobetaenone I to probetaenone I . The cytochrome P450 monooxygenase sthF catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I . The FAD-linked oxidoreductase sthB is responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A . Finally, the cytochrome P450 monooxygenase sthD catalyzes the hydroxylation of C-15 to afford the final metabolite stemphyloxin II .
Catalytic Activity: betaenone C = betaenone A
Sequence Mass (Da): 33144
Sequence Length: 315
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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Q0UK52 | MAPAETTGNVQRPEAGKQSMGSFWTQMFPPKPTYTEEQVPDLTGKIFIVTGSSSGVGKEAARMLYAKNAKVYMAARPGPKLPAAINSVQEAVPKSGGALIPLELDLADLAVVKKAVEKFTSLETKLHGLINNAAVQALKDTDGDARTAQGHEIHMGVNVLAPFLFTRLLTGVLTATARQEPPGTVRVVWVSSMGTETIGEKRRGLSPDYVDYWPLMSPLERYGLSKAGNWLHGVEFARRYAADGIASFPINPGHLKSDLYREGGALFKFALKPVLYPPTYGAYVELFAALSPTLTLKDSGAWSKYVEMVYFPDC | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations . The C-terminal reductase (R) domain of sthA catalyzes the reductive release of the polyketide chain . Because sthA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase sthE . The short-chain dehydrogenase/reductase sthC then catalyzes reduction of dehydroprobetaenone I to probetaenone I . The cytochrome P450 monooxygenase sthF catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I . The FAD-linked oxidoreductase sthB is responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A . Finally, the cytochrome P450 monooxygenase sthD catalyzes the hydroxylation of C-15 to afford the final metabolite stemphyloxin II .
Catalytic Activity: AH2 + dehydroprobetaenone I = A + probetaenone I
Sequence Mass (Da): 34055
Sequence Length: 314
Pathway: Mycotoxin biosynthesis.
EC: 1.1.1.-
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Q0UK51 | MAAYFLLGLYGSTLVYRLIFHPLNRFPGPLAARISDLWLCTQLGGHDMHHLSERLSKRYGEFVRIGSSTLMLTHPKAVAAIYGPGSPCRKGTFYDLEQPNRGIATRDESLHAGRRRVWSRGFGDKALRTYEPRVAAYVHMLLGRLADARGKPVDMARLAEAFAFDTMGDLGLGADFGMLRQARTHEAVEQLVQGMTIMGRRLPMWLMRLLIDVAQALVPTAATTGFLGFCHHHLDRFMADPRRSERPSLMAPLLSHYEKQNIADRDLSILRNDCRFIIIAGSDTVAATLTFAFFYLAKHPGHVTRLREELFPLRAADGTFSHQRIFDAPHLNAVINETLRLHPPASTIPRVTPPQGLVVADTFIPGDMTVFSSQYALGRSEAIYSKASDFIPERWCSRPDLIKDGSAYAPFSIGHHSCLGRPLALMEMRLVLAETLSRFDIAFAPGFDANHFLQHVHDCMSWHIGKLGLTFTAIE | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations . The C-terminal reductase (R) domain of sthA catalyzes the reductive release of the polyketide chain . Because sthA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase sthE . The short-chain dehydrogenase/reductase sthC then catalyzes reduction of dehydroprobetaenone I to probetaenone I . The cytochrome P450 monooxygenase sthF catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I . The FAD-linked oxidoreductase sthB is responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A . Finally, the cytochrome P450 monooxygenase sthD catalyzes the hydroxylation of C-15 to afford the final metabolite stemphyloxin II .
Catalytic Activity: betaenone A + H(+) + NADPH + O2 = H2O + NADP(+) + stemphyloxin II
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 53121
Sequence Length: 475
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q0UK49 | MGLQFLAPGEKVFPSLHRIIISTFALIAAYIFIVRPLRNILFHPLKKYPGPKLFGASSIPYGFYYMTGKWHLKIRNLHATYGPIVRIGPDELSYACPEAWEDIYGRYVPTKRRENPKPVWYCSPDAHDMVGASLGDHGRMRRVMAPGFTYSAMCKQEPLIKGHVDMFLSKLCSLCGDGRAEVNILDWLTYCTFDLIGDLSFGEPFGCMENNMLHPWLQLVFANIYITHIILLCQRIPFFYLFLPIKTTYQLWRDFRRHVVLLREVVERRLSLSTPRDDFLDVMTTKQTSTLYMTKEEIFKNAILLTGGGAETTSSSLSGMMYMLTMRPDVKEKILEELRDTFPSEDDINMRSVAQLTYTGAFIEESMRYYPPGPNTMWRITPPAGNTILGDYIPGNTIVGIPHRVLYRSEAYWKDADGFRPERWLPDSQRPAEFDEDKREGFHPFSYGPRACIAMNLAYAEMRYILARFLWHFDIEATKESKKWMDDQKAYLVWDKPGLFVHLKPRAGVKVAA | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations . The C-terminal reductase (R) domain of sthA catalyzes the reductive release of the polyketide chain . Because sthA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase sthE . The short-chain dehydrogenase/reductase sthC then catalyzes reduction of dehydroprobetaenone I to probetaenone I . The cytochrome P450 monooxygenase sthF catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I . The FAD-linked oxidoreductase sthB is responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A . Finally, the cytochrome P450 monooxygenase sthD catalyzes the hydroxylation of C-15 to afford the final metabolite stemphyloxin II .
Catalytic Activity: dehydroprobetaenone I + H(+) + NADPH + O2 = epoxybetaenone + H2O + NADP(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59257
Sequence Length: 513
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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P15705 | MSLTADEYKQQGNAAFTAKDYDKAIELFTKAIEVSETPNHVLYSNRSACYTSLKKFSDALNDANECVKINPSWSKGYNRLGAAHLGLGDLDEAESNYKKALELDASNKAAKEGLDQVHRTQQARQAQPDLGLTQLFADPNLIENLKKNPKTSEMMKDPQLVAKLIGYKQNPQAIGQDLFTDPRLMTIMATLMGVDLNMDDINQSNSMPKEPETSKSTEQKKDAEPQSDSTTSKENSSKAPQKEESKESEPMEVDEDDSKIEADKEKAEGNKFYKARQFDEAIEHYNKAWELHKDITYLNNRAAAEYEKGEYETAISTLNDAVEQGREMRADYKVISKSFARIGNAYHKLGDLKKTIEYYQKSLTEHRTADILTKLRNAEKELKKAEAEAYVNPEKAEEARLEGKEYFTKSDWPNAVKAYTEMIKRAPEDARGYSNRAAALAKLMSFPEAIADCNKAIEKDPNFVRAYIRKATAQIAVKEYASALETLDAARTKDAEVNNGSSAREIDQLYYKASQQRFQPGTSNETPEETYQRAMKDPEVAAIMQDPVMQSILQQAQQNPAALQEHMKNPEVFKKIQTLIAAGIIRTGR | Function: May play a role in mediating the heat shock response of some HSP70 genes. It is required for optimal growth of yeast cells at both low and high temperature.
PTM: N-glycosylated.
Sequence Mass (Da): 66265
Sequence Length: 589
Subcellular Location: Cytoplasm
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Q7FA29 | MKRRHWSHPSCGLLLLVAVFCLLLVFRCSQLRHSGDGAAAAAPDGGAGRNDGDDVDERLVELAAVDPAAMAVLQAAKRLLEGNLARAPERHRDVALRGLREWVGKQERFDPGVMSELVELIKRPIDRYNGDGGGGGEGEGRRYASCAVVGNSGILLAAEHGELIDGHELVVRLNNAPAGDGRYARHVGARTGLAFLNSNVLSQCAVPRRGACFCRAYGEGVPILTYMCNAAHFVEHAVCNNASSSSSGAADATAAAPVIVTDPRLDALCARIVKYYSLRRFARETGRPAEEWARRHEEGMFHYSSGMQAVVAAAGVCDRVSVFGFGKDASARHHYHTLQRRELDLHDYEAEYEFYRDLESRPEAIPFLRQRNSGFRLPPVSFYR | Function: Possesses sialyltransferase-like activity in vitro. Transfers sialic acid to the glycoprotein asialofetuin. The transferred sialic acid is linked to galactose of Gal-beta-1,3-GalNAc through alpha-2,6-linkage.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 41999
Sequence Length: 384
Subcellular Location: Golgi apparatus membrane
EC: 2.4.99.-
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A0A0P0ZEA9 | MEGSINDARRTNYLVLLRTCYEIYGIYEPLLALFAVYSVAVVVYRLYLHPLARFPGPKLAAATGWYEFYHDVFRGGQYLYEIESMHRKYGPIIRINPHELVVNDPDFYNTVFVAANTRRTDKWSGLEGIGLRGSLAFTRDHDLHRIRRKRYEPFFSRLSVSRIEPIIVDEAKLLAKQLEASSKTGRVIELEHVMSAFTGDVITTLCSEKSPDMIRHPEFGKGWHTSLYNFPSCFRAGAFNSFLEYSTDHINTAKREMLSVDKLEQNNKSSVFRYVLSTDMPQAERDTERLAREAALLFGAGSVTTTRFFSVTIYYTLRNRQIRDRLSAELKDVMAGYPSTLPTWQELDRLPYLHAIVKEGLRYACPFVLSSSLAAWSSLSHKFSSRLSYGVMRHLSRISPDSALHYKQWTIPPGTPVGMSSYSLHTDPETFPEPFKFMPERWLGEYNPKMNRSWVPFTRGSRNCLGMNLAYAQIYWGLAVMFRPGGPRLELYETNESDIRPVLDFLGPLPKSGSRGLRVTVS | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the sesterterpene stellatic acid . The first step in the pathway is performed by the stellatatriene synthase that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and then converting GGDP into stellata-2,6,19-triene . The cytochrome P450 monooxygenase Stl-P450 then catalyzes three successive oxidation reactions on the C-20 methyl group to generate the carboxylic acid of stellatic acid .
Catalytic Activity: 3 O2 + 3 reduced [NADPH--hemoprotein reductase] + stellata-2,6,19-triene = 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase] + stellatate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59873
Sequence Length: 522
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q6ZH45 | MRVLPLALAAAIFSGVTAILVYLSGLSSYGGARVSDADLAALGALQSGFSKCVDANGLGLKAIPGEDYCRVVIQYPSDTDSKWKDPKTGEPEGLSFEFNLCEAVASWEQVRNSTTILTKEYIDALPNGWEEYAWRRINKGIHLNKCQNRTLCMEKLSLVLPETPPYVPRQFGRCAVVGNSGDLLKTKFGDEIDSYDVVIRENGAPIQNYTEYVGTKSTFRLLNRGSAKALDKVVELDETKKEALIVKTTIHDIMNQMIREIPITNPVYLMLGTSFGSSAKGTGLKALEFALSMCDSVDMYGFTVDPGYKEWTRYFSESRKGHTPLHGRAYYQMMECLGLVKIHSPMRGDPGRVVKWAPTKDTIEAARVASEKLLKRPGAGSEGPLSSCTMIKKREKGKTPKRSVVRHAALKHLEYMRGATRYPLERNAGGGYLCMINER | Function: May possess sialyltransferase-like activity in vitro.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48577
Sequence Length: 439
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
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A0A0P0ZEM1 | MEYKFSTVVDPGTYETHGLCEGYEVRYHKNAELEDIGCLRCQEHWRQSVGPLGAFKGTLGNPFNLLSLVIPECLPDRLSIVGFANELAFIHDDVTDIVQYGDAHNNDFKEAFNSMATTGSMENAASGKRALQAYIAREMVRIDKERAIPTIKAWAKFVDYGGRQETTRFTSEKEYTEYRIQDIGLWFWYGLLSFAMALDVPEHEREMCHEVCRTAYVQIMLVHDLASWEKEKLNAAALGKDVITNIIFVLMEEHGISEEEAKERCRETAKTLAADYLKIVEEYKARDDISLDSRKYIESWLYTISGNTVWSFICPRYNSSGSFSDHQLELMKNGVPKDPASGSTNGTSNGTSNGTSHVAVNGNGHVTNDDLSANGIKTDGELLSAITMEHLKNRNSFKLGDHDQEVKSLHGHGQALDPRVLQAPYEYITALPSKGLREQAIDALNVWFRVPTAKLEIIKSITTILHNASLMLDDVEDGSELRRGKPATHNIFGLGQTINSANYQLVRALQELQKLGDARSLLVFTEELHNLYVGQSMDLYWTSNLVCPSMHEYFQMIEHKTGGLFRLFGRLMAVHSTNPVQVDLTDFTNHLGRYFQTRDDYQNLVSAEYTKQKGFCEDFEEGKFSLPMIHLMQTMPDNLVLRNVWTQRRVNGTATHGQKQTILNLMKEAGTLKFTQDSLGVLYSDVEKSVAELESKFGIENFQLRLIMELLKTG | Function: Multifunctional diterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene stellatic acid . The first step in the pathway is performed by the stellatatriene synthase that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and then converting GGDP into stellata-2,6,19-triene . The cytochrome P450 monooxygenase Stl-P450 then catalyzes three successive oxidation reactions on the C-20 methyl group to generate the carboxylic acid of stellatic acid .
Catalytic Activity: dimethylallyl diphosphate + 4 isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + 4 diphosphate
Sequence Mass (Da): 80706
Sequence Length: 714
Domain: The characteristic DDXXD motif for binding a trinuclear Mg(2+) cluster is conserved in both the N-terminal terpene cyclase and C-terminal prenyl transferase domains.
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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Q09006 | MCDSDIKVKQLEKRASGQAFELILSPPSMDAAPDLSITSPKKKECSLEEIQKKLEAAEERRKLHEAEILKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTTKMETIKENREAQIAAKLERLREKDKKVEEIRKGKECKEPSEK | Function: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. It prevents assembly and promotes disassembly of microtubules (By similarity).
PTM: Different phosphorylated forms, from unphosphorylated to highly phosphorylated, are found in the mature egg. Progressive dephosphorylation from the mid-blastula to the tailbud stage.
Sequence Mass (Da): 16789
Sequence Length: 145
Subcellular Location: Cytoplasm
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Q09005 | KREHEKEVLQKAIEENNNFSKMAEEKLTTKMEAIKENREAQMAAKLERLREKDKKLEEIRKGKECKEPSED | Function: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. It prevents assembly and promotes disassembly of microtubules (By similarity).
PTM: From unphosphorylated forms to highly phosphorylated ones in the mature egg, followed by progressive dephosphorylation from the mid-blastula to the tailbud stage.
Sequence Mass (Da): 8474
Sequence Length: 71
Subcellular Location: Cytoplasm
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A0A1D8PK71 | MSFQNKNLYDLLGNDVEEDAAPSAPSREVVKKNTSSKKSDAAPASADPAKAKKKKSPTGNEAALKNKNFNKDVAPPQSTATKHSKKPFDRHSRTGKTDSKKKLQQGWGQSDKRELEGEVEGTEDAEAELEAEAEENDESANAIPKKSLQEYLAELELSKQELEGSKKLRQANEGAEQKWTAEEKIEKQQEVFFASTHTKKAKSKAQKEKVFLDIDANFGDEQPQTTRGGFRGGKRGGARGGSRGGAKRGGARGAAKPEVNDKNFPSL | Function: Ribosome preservation factor that protect a small pool of nontranslating, vacant ribosomes in cells under nutrient starvation conditions. Under nutrient-limiting conditions, cells reduce ribosome biogenesis and degrade ribosomes via autophagy (ribophagy) or proteasomal degradation. To avoid excessive degradation during starvation, STM1 binds to and protects 80S ribosomes from proteasomal degradation. Under nutrient-sufficient conditions, TORC1 phosphorylates and inhibits STM1 to prevent formation of dormant 80S ribosomes. Acts as an inhibitor of mRNA translation by promoting ribosome hibernation: clamps the two ribosomal subunits, thereby preventing their dissociation, and inhibits translation by excluding mRNA-binding. Acts via its association with eEF2, promoting ribosome stabilization and storage in an inactive state. May also repress translation by preventing association of eEF3 with ribosomes. Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs.
PTM: Phosphorylation by TORC1 upon nutrient replenishment inhibits STM1 and causes its release from dormant ribosomes.
Sequence Mass (Da): 29072
Sequence Length: 267
Subcellular Location: Cytoplasm
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P39015 | MSNPFDLLGNDVEDADVVVLPPKEIVKSNTSSKKADVPPPSADPSKARKNRPRPSGNEGAIRDKTAGRRNNRSKDVTDSATTKKSNTRRATDRHSRTGKTDTKKKVNQGWGDDKKELSAEKEAQADAAAEIAEDAAEAEDAGKPKTAQLSLQDYLNQQANNQFNKVPEAKKVELDAERIETAEKEAYVPATKVKNVKSKQLKTKEYLEFDATFVESNTRKNFGDRNNNSRNNFNNRRGGRGARKGNNTANATNSANTVQKNRNIDVSNLPSLA | Function: Ribosome preservation factor that protect a small pool of nontranslating, vacant ribosomes in cells under nutrient starvation conditions. Under nutrient-limiting conditions, cells reduce ribosome biogenesis and degrade ribosomes via autophagy (ribophagy) or proteasomal degradation. To avoid excessive degradation during starvation, STM1 binds to and protects 80S ribosomes from proteasomal degradation. Under nutrient-sufficient conditions, TORC1 phosphorylates and inhibits STM1 to prevent formation of dormant 80S ribosomes . Acts as an inhibitor of mRNA translation by promoting ribosome hibernation: clamps the two ribosomal subunits, thereby preventing their dissociation, and inhibits translation by excluding mRNA-binding . Acts via its association with eEF2 (EFT1), promoting ribosome stabilization and storage in an inactive state . May also repress translation by preventing association of eEF3 (YEF3 and HEF3) with ribosomes . Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs . Acts with CDC13 to control telomere length homeostasis . Involved in the control of the apoptosis-like cell death .
PTM: Phosphorylation by TORC1 upon nutrient replenishment inhibits STM1 and causes its release from dormant ribosomes.
Sequence Mass (Da): 29995
Sequence Length: 273
Subcellular Location: Cytoplasm
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Q9UBI4 | MLGRSGYRALPLGDFDRFQQSSFGFLGSQKGCLSPERGGVGTGADVPQSWPSCLCHGLISFLGFLLLLVTFPISGWFALKIVPTYERMIVFRLGRIRTPQGPGMVLLLPFIDSFQRVDLRTRAFNVPPCKLASKDGAVLSVGADVQFRIWDPVLSVMTVKDLNTATRMTAQNAMTKALLKRPLREIQMEKLKISDQLLLEINDVTRAWGLEVDRVELAVEAVLQPPQDSPAGPNLDSTLQQLALHFLGGSMNSMAGGAPSPGPADTVEMVSEVEPPAPQVGARSSPKQPLAEGLLTALQPFLSEALVSQVGACYQFNVVLPSGTQSAYFLDLTTGRGRVGHGVPDGIPDVVVEMAEADLRALLCRELRPLGAYMSGRLKVKGDLAMAMKLEAVLRALK | Function: May play a role in cholesterol transfer to late endosomes . May play a role in modulating membrane acid-sensing ion channels. Can specifically inhibit proton-gated current of ASIC1 isoform 1. Can increase inactivation speed of ASIC3. May be involved in regulation of proton sensing in dorsal root ganglions (By similarity). May play a role in protecting FBXW7 isoform 3 from degradation .
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 42968
Sequence Length: 398
Subcellular Location: Membrane
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Q9UJZ1 | MLARAARGTGALLLRGSLLASGRAPRRASSGLPRNTVVLFVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEASAVLAKAKAKAEAIRILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTKAPVPGTPDSLSSGSSRDVQGTDASLDEELDRVKMS | Function: Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation.
PTM: Hyperphosphorylated at Ser-17 in some patients with monoclonal gammopathy of undetermined significance (MGUS), multiple myeloma (MM) and Waldenstrom macroglobulinemia due to impaired dephosphorylation by PP2A.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38534
Sequence Length: 356
Subcellular Location: Cell membrane
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F1BVB6 | MSKMASSIFATFSLLSSLLPTSLASSDANYEDFLQCLDLYSQNSIPVYTRNTSSYTSILESTIKNLVFLSPTTPKPNFIVTPMQESHVQTSVICCRMHGLQMRIRSGGHDFEGLSYVSNVPFVVLDLIHLKTINVDIEENSAWVQTGATIGELYYRIAEKVGVHAFPAGLCPTVGVGGHISGAGYGVLMRKYGVSADHVIDARIVNVDGEILDRESMGEDLFWAIRGGGGASFGVILAWKIRLVPVPPTVTIFIVPKTLEEGATALLHKWQFIGDNVHEDLFIGLSMRSVIISPKGDKTILVSFIGLFLGGSDKLVQHMEQSFPELGVKPHDCIEMSWIKSTVVFGVFSNDASLSVLLDRKNPFPPKSYHKVKSDYVTEPLPISVLEGICHRFLKNGVNKAEIIMSPYGGRMNEISESEIAFPHRKGNLYKINYIAEWEEAGSMENHLSWIRELYRYMTPYVSKSPRSSYLNFKDIDLGQTKNGTATYSQAKAWGSKYFKNNFKRLMQVKTKVDPNNFFCNEQGIPPFSS | Cofactor: Binds 1 FAD per subunit in a bicovalent manner.
Function: Catalyzes the oxidation of different tetrahydroprotoberberines, such as (S)-canadine, (S)-scoulerine and (S)-corypalmine . Catalyzes the oxidation of (S)-coreximine and (S)-tetrahydropalmatine . Catalyzes the oxidation of different 1-benzylisoquinoline alkaloids, such as (S)-norreticuline, (S)-nororientaline, (S)-coclaurine and (S)-norisoorientaline . Exhibits strict specificity for the (S)-enantiomer of tetrahydroprotoberbirines and 1-benzylisoquinoline alkaloids .
PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage.
Catalytic Activity: (S)-canadine + H(+) + 2 O2 = berberine + 2 H2O2
Sequence Mass (Da): 58990
Sequence Length: 530
EC: 1.3.3.8
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Q9LT15 | MAGGAFVSEGGGGGRSYEGGVTAFVIMTCIVAAMGGLLFGYDLGISGGVTSMEEFLTKFFPQVESQMKKAKHDTAYCKFDNQMLQLFTSSLYLAALVASFMASVITRKHGRKVSMFIGGLAFLIGALFNAFAVNVSMLIIGRLLLGVGVGFANQSTPVYLSEMAPAKIRGALNIGFQMAITIGILVANLINYGTSKMAQHGWRVSLGLAAVPAVVMVIGSFILPDTPNSMLERGKNEEAKQMLKKIRGADNVDHEFQDLIDAVEAAKKVENPWKNIMESKYRPALIFCSAIPFFQQITGINVIMFYAPVLFKTLGFGDDAALMSAVITGVVNMLSTFVSIYAVDRYGRRLLFLEGGIQMFICQLLVGSFIGARFGTSGTGTLTPATADWILAFICVYVAGFAWSWGPLGWLVPSEICPLEIRPAGQAINVSVNMFFTFLIGQFFLTMLCHMKFGLFYFFASMVAIMTVFIYFLLPETKGVPIEEMGRVWKQHWFWKKYIPEDAIIGGHDDNNTN | Function: Hexose-H(+) symporter that catalyzes the high-affinity uptake of glucose, galactose and mannose . Proton-coupled symporter responsible for the uptake of glucose from the apoplast into the cells (Probable).
Catalytic Activity: D-glucose(out) + H(+)(out) = D-glucose(in) + H(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56200
Sequence Length: 514
Subcellular Location: Membrane
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O65413 | MPSVGIVIGDGKKEYPGKLTLYVTVTCIVAAMGGLIFGYDIGISGGVTTMDSFQQKFFPSVYEKQKKDHDSNQYCRFDSVSLTLFTSSLYLAALCSSLVASYVTRQFGRKISMLLGGVLFCAGALLNGFATAVWMLIVGRLLLGFGIGFTNQSVPLYLSEMAPYKYRGALNIGFQLSITIGILVANVLNFFFSKISWGWRLSLGGAVVPALIITVGSLILPDTPNSMIERGQFRLAEAKLRKIRGVDDIDDEINDLIIASEASKLVEHPWRNLLQRKYRPHLTMAILIPAFQQLTGINVIMFYAPVLFQTIGFGSDAALISAVVTGLVNVGATVVSIYGVDKWGRRFLFLEGGFQMLISQVAVAAAIGAKFGVDGTPGVLPKWYAIVVVLFICIYVAAFAWSWGPLGWLVPSEIFPLEIRSAAQSITVSVNMIFTFLIAQVFLMMLCHLKFGLFIFFAFFVVVMSIFVYLFLPETRGVPIEEMNRVWRSHWYWSKFVDAEKNLTKVVI | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56166
Sequence Length: 508
Subcellular Location: Membrane
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Q94AZ2 | MTGGGFATSANGVEFEAKITPIVIISCIMAATGGLMFGYDVGVSGGVTSMPDFLEKFFPVVYRKVVAGADKDSNYCKYDNQGLQLFTSSLYLAGLTATFFASYTTRTLGRRLTMLIAGVFFIIGVALNAGAQDLAMLIAGRILLGCGVGFANQAVPLFLSEIAPTRIRGGLNILFQLNVTIGILFANLVNYGTAKIKGGWGWRLSLGLAGIPALLLTVGALLVTETPNSLVERGRLDEGKAVLRRIRGTDNVEPEFADLLEASRLAKEVKHPFRNLLQRRNRPQLVIAVALQIFQQCTGINAIMFYAPVLFSTLGFGSDASLYSAVVTGAVNVLSTLVSIYSVDKVGRRVLLLEAGVQMFFSQVVIAIILGVKVTDTSTNLSKGFAILVVVMICTYVAAFAWSWGPLGWLIPSETFPLETRSAGQSVTVCVNLLFTFIIAQAFLSMLCHFKFGIFIFFSAWVLIMSVFVMFLLPETKNIPIEEMTERVWKKHWFWARFMDDHNDHEFVNGEKSNGKSNGFDPSTRL | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57419
Sequence Length: 526
Subcellular Location: Cell membrane
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Q8GW61 | MAGGALTDEGGLKRAHLYEHRITSYFIFACIVGSMGGSLFGYDLGVSGGVTSMDDFLKEFFPGIYKRKQMHLNETDYCKYDNQILTLFTSSLYFAGLISTFGASYVTRIYGRRGSILVGSVSFFLGGVINAAAKNILMLILGRIFLGIGIGFGNQAVPLYLSEMAPAKIRGTVNQLFQLTTCIGILVANLINYKTEQIHPWGWRLSLGLATVPAILMFLGGLVLPETPNSLVEQGKLEKAKAVLIKVRGTNNIEAEFQDLVEASDAARAVKNPFRNLLARRNRPQLVIGAIGLPAFQQLTGMNSILFYAPVMFQSLGFGGSASLISSTITNAALVVAAIMSMYSADKFGRRFLLLEASVEMFCYMVVVGVTLALKFGEGKELPKSLGLILVVLICLFVLAYGRSWGPMGWLVPSELFPLETRSAGQSVVVCVNLFFTALIAQCFLVSLCHLKYGIFLLFAGLILGMGSFVYFLLPETKQVPIEEVYLLWRQHWLWKKYVEDVDE | Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55386
Sequence Length: 504
Subcellular Location: Membrane
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P23586 | MPAGGFVVGDGQKAYPGKLTPFVLFTCVVAAMGGLIFGYDIGISGGVTSMPSFLKRFFPSVYRKQQEDASTNQYCQYDSPTLTMFTSSLYLAALISSLVASTVTRKFGRRLSMLFGGILFCAGALINGFAKHVWMLIVGRILLGFGIGFANQAVPLYLSEMAPYKYRGALNIGFQLSITIGILVAEVLNYFFAKIKGGWGWRLSLGGAVVPALIITIGSLVLPDTPNSMIERGQHEEAKTKLRRIRGVDDVSQEFDDLVAASKESQSIEHPWRNLLRRKYRPHLTMAVMIPFFQQLTGINVIMFYAPVLFNTIGFTTDASLMSAVVTGSVNVAATLVSIYGVDRWGRRFLFLEGGTQMLICQAVVAACIGAKFGVDGTPGELPKWYAIVVVTFICIYVAGFAWSWGPLGWLVPSEIFPLEIRSAAQSITVSVNMIFTFIIAQIFLTMLCHLKFGLFLVFAFFVVVMSIFVYIFLPETKGIPIEEMGQVWRSHWYWSRFVEDGEYGNALEMGKNSNQAGTKHV | Function: Major hexose transporter. Mediates an active uptake of hexoses, by sugar/hydrogen symport. Can transport glucose, 3-O-methylglucose, fructose, xylose, mannose, galactose, fucose, 2-deoxyglucose and arabinose. Confers sensitivity to galactose in seedlings.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57611
Sequence Length: 522
Subcellular Location: Cell membrane
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Q8Y678 | MHAEFRTDRGRIRHHNEDNGGVFENKDNQPIVIVADGMGGHRAGDVASEMAVRLLSDAWKETTALLTAEEIETWLRKTIQEVNKEIVLYAESEMDLNGMGTTLVAAIMAQSQVVIANVGDSRGYLLQNHVLRQLTEDHSLVHELLRTGEISKEDAMNHPRKNILLRALGVEGKVEVDTFVVPFQTSDTLLLCSDGLTNMVPETEMEEILKSKRTLSEKADVFITKANSYGGEDNITVLLVERDLTQKGRDAS | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that dephosphorylates EF-Tu.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28026
Sequence Length: 252
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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B3LFK1 | MPSTTLLFPQKHIRAIPGKIYAFFRELVSGVIISKPDLSHHYSCENATKEEGKDAADEEKTTTSLFPESNNIDRSLNGGCSVIPCSMDVSDLNTPISITLSPENRIKSEVNAKSLLGSRPEQDTGAPIKMSTGVTSSPLSPSGSTPEHSTKVLNNGEEEFICHYCDATFRIRGYLTRHIKKHAIEKAYHCPFFNSATPPDLRCHNSGGFSRRDTYKTHLKARHVLYPKGVKPQDRNKSSGHCAQCGEYFSTIENFVENHIESGDCKALPQGYTKKNEKRSGKLRKIKTSNGHSRFISTSQSVVEPKVLFNKDAVEAMTIVANNSSGNDIISKYGNNKLMLNSENFKVDIPKRKRKYIKKKQQQVSGSTVTTPEVATQNNQEVAPDEISSATIFSPFDTHLLEPVPSSSSESSAEVMFHGKQMKNFLIDINSFTNQQQQAQDNPSFLPLDIEQSSYDLSEDAMSYPIISTQSNRDCTQYDNTKISQILQSQLNPEYLSENHMRETQQYLNFYNDNFGSQF | Function: Transcription factor involved in the regulation of gene expression in response to extracellular amino acid levels. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system, becomes proteolytically activated and relocates to the nucleus, where it induces the expression of SPS-sensor-regulated genes, including the amino-acid permeases AGP1, BAP2, BAP3 and GNP1. Binding to promoters is facilitated by DAL81. Involved in the repression of genes subject to nitrogen catabolite repression and genes involved in stress response. Negatively regulated by inner nuclear membrane proteins ASI1, ASI2 and ASI3, which prevent unprocessed precursor forms that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes. May be involved in pre-tRNA splicing (By similarity).
PTM: Phosphorylated by casein kinase I. Phosphorylation is not dependent on the extracellular amino acid levels, but is a prerequisite for proteolytic processing (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58088
Sequence Length: 519
Domain: The N-terminal inhibitory domain contains conserved sequence elements important for cytoplasmic retention (Region I) and proteolytic processing (Region II) of the protein. Region I is also required for ASI1/2/3-mediated negative regulation of transcription (By similarity).
Subcellular Location: Cell membrane
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A0A384XLH1 | MIPNRWRDLARRDIFEPLGLNGSYFIPNAHNRAHVAVASKYSDEVDIDFLDVMACSGGQMSSLSDYIKLMQTFLDPTLPQSLLPAHIMREWMTPVFGFNDDETEVGLLWEIVKIQDSYCRPVRVYEKNGVLGASRSVFAIHREMAFGVALLNTGTATVTGNIALEIFRIMQPYLDKLQERKVKERFAGHWRLPLQTNATSGSMVDISVSDGSLWITRLVLNGTDVLSLTEAMPAFGGARSRRVALWSMRRDEFRMVLGAGAATSCMSSWTAMDSGFSRGYPMDLVYFKGGRLHIPSAGVVLVRA | Function: Beta-lactamase-like protein; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl CoA by step-wise elimination of ammonia from phenylalanine by the phenylalanine ammonia-lyase str11, oxygenation by str8 and retro-Claisen reaction to form benzoic acid, which is activated to its CoA thiolester benzoyl CoA by the dedicated CoA ligase str10 . Benzoyl CoA forms the starter unit for the highly reducing polyketide synthase stpks1 that produces the polyketide prestrobilutin A . The FAD-dependent oxygenase str9 then catalyzes the key oxidative rearrangement responsible for the creation of the beta-methoxyacrylate toxophore . Str9 performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by Meinwald rearrangement to furnish the aldehyde intermediate (Probable). Rapid enolization of the aldehyde intermediate would give the beta-methoxyacrylate skeleton and methylations catalyzed by str2 and str3 complete the synthesis and lead to the production of strobilurin A (Probable). The short-chain dehydrogenase stl2 and the dehydrogenase str4 play a role in the shunt pathway leading to the production of bolineol . The cluster encodes no obvious halogenase gene that could be involved in production of strobilurin B, nor any obvious dimethylallyl-transferase that could be involved in the production of strobilurin G (Probable). It is possible that unknown proteins encoded in, or near, the cluster (such as str1 or stl1) may form new classes of halogenases or dimethylally-transferases, or that the responsible genes are located elsewhere on the genome (Probable). Similarly, proteins encoded by str5/str6 hydrolases appear to have no chemical role in the biosynthesis of strobilurin A (Probable). Finally, no obvious self-resistance gene is found within the cluster (Probable).
Sequence Mass (Da): 33923
Sequence Length: 304
Pathway: Mycotoxin biosynthesis.
EC: 3.5.-.-
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A0A3B1EFQ1 | MPLPTRKIGQSLVSEIGFGSMGIARLGPSGFYGVVESDDERFKVLDAAHAAGCTFWDSAHLYGDSEELIGKWLKRTGKRNDIFLATKFGITPQGVRGDPDFVKEQCATSLERLGVDCIDLFYQHRVDPKTPIEITVGAMAELVKEGKVKYLGLSECSAKALRRAHAVHPIAALQIEYSPFVLDIEDPKIALLETARELGVTIVAYSPLGRGLLTGQYKSPDDFEPNDFRRTIPKFSADNFPKILDVVAQLKKIGEKHNATPGQVTLAWILAQGPEFIVIPGTKKIKYLEENVGAASIKLTEEEVAAVRKLAEESEIPGDRNARMGAMLIDSPELPQ | Function: Aldo-keto reductase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl CoA by step-wise elimination of ammonia from phenylalanine by the phenylalanine ammonia-lyase str11, oxygenation by str8 and retro-Claisen reaction to form benzoic acid, which is activated to its CoA thiolester benzoyl CoA by the dedicated CoA ligase str10 . Benzoyl CoA forms the starter unit for the highly reducing polyketide synthase stpks1 that produces the polyketide prestrobilutin A . The FAD-dependent oxygenase str9 then catalyzes the key oxidative rearrangement responsible for the creation of the beta-methoxyacrylate toxophore . Str9 performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by Meinwald rearrangement to furnish the aldehyde intermediate (Probable). Rapid enolization of the aldehyde intermediate would give the beta-methoxyacrylate skeleton and methylations catalyzed by str2 and str3 complete the synthesis and lead to the production of strobilurin A (Probable). The short-chain dehydrogenase stl2 and the dehydrogenase str4 play a role in the shunt pathway leading to the production of bolineol . The cluster encodes no obvious halogenase gene that could be involved in production of strobilurin B, nor any obvious dimethylallyl-transferase that could be involved in the production of strobilurin G (Probable). It is possible that unknown proteins encoded in, or near, the cluster (such as str1 or stl1) may form new classes of halogenases or dimethylally-transferases, or that the responsible genes are located elsewhere on the genome (Probable). Similarly, proteins encoded by str5/str6 hydrolases appear to have no chemical role in the biosynthesis of strobilurin A (Probable). Finally, no obvious self-resistance gene is found within the cluster (Probable).
Sequence Mass (Da): 36832
Sequence Length: 336
Pathway: Mycotoxin biosynthesis.
EC: 1.1.1.-
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A0A384XR80 | MSRLLCPSSSTSVVRRARPTFVLGNLSIKQAQGTGASSALARRRRSTFAATADGLHVIPLEQKYPFPWLRDACRCPDCVHPSTRQKLFCTSDIPVDIQPATNGVEEVGEGVKIRWSNGHESLYDWDFLKEHSSSVSRSEANKDLPRVGWTRASIAKERDLYLEYEELKTKEGLRKAIDHTCRFGLLFIRNVPNVETSTASCSLRTLAHYFGDIRTTFYGELWDVKNVSNSRNIAYTNLGLGLHMDLLYFQHPPQFQFLHCLRNRVQGGSSIFSDALHAAETLRIQDAASYSVLTDVQVPFFYVNDGHHLYHTHPTIEVSASGDVNQINYSPPFQAPLLLDTPPAFFTALHQFSNLVNSDENTYEYTLEEGDAVLFDNRRVLHARRAFEEIPGQGVRVGEANRWLKGCYIEGDTMWDRGRMLR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl CoA by step-wise elimination of ammonia from phenylalanine by the phenylalanine ammonia-lyase str11, oxygenation by str8 and retro-Claisen reaction to form benzoic acid, which is activated to its CoA thiolester benzoyl CoA by the dedicated CoA ligase str10 . Benzoyl CoA forms the starter unit for the highly reducing polyketide synthase stpks1 that produces the polyketide prestrobilutin A . The FAD-dependent oxygenase str9 then catalyzes the key oxidative rearrangement responsible for the creation of the beta-methoxyacrylate toxophore . Str9 performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by Meinwald rearrangement to furnish the aldehyde intermediate (Probable). Rapid enolization of the aldehyde intermediate would give the beta-methoxyacrylate skeleton and methylations catalyzed by str2 and str3 complete the synthesis and lead to the production of strobilurin A (Probable). The short-chain dehydrogenase stl2 and the dehydrogenase str4 play a role in the shunt pathway leading to the production of bolineol . The cluster encodes no obvious halogenase gene that could be involved in production of strobilurin B, nor any obvious dimethylallyl-transferase that could be involved in the production of strobilurin G (Probable). It is possible that unknown proteins encoded in, or near, the cluster (such as str1 or stl1) may form new classes of halogenases or dimethylally-transferases, or that the responsible genes are located elsewhere on the genome (Probable). Similarly, proteins encoded by str5/str6 hydrolases appear to have no chemical role in the biosynthesis of strobilurin A (Probable). Finally, no obvious self-resistance gene is found within the cluster (Probable).
Sequence Mass (Da): 47791
Sequence Length: 422
Pathway: Mycotoxin biosynthesis.
EC: 1.14.-.-
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A0A3B1EFQ2 | MAVDRKIRIAVVGGGPGGVIAALALSKSPNVEIDLYEAATAFGDIGLSLGMPWRPWRILRLLGLQGYLAALLPPDQIPKEDVTVPTIHYRKSDQAVGEDIFTCTSLSGYTRFRRSHFHAALLPHLPSNCKTYTSKRLVSYAEPSNASDPIVITFADGTTAECDVLVGADGIKSPTRASMYNYAADEAEKAGRSAEANDLRSKIRAKFSGVEVYRSVISAEQLRAAAPDHHAFRCPTQFLGKEKVRMPTYPIQSENSQFLNCALYICDYSREGEDYPEPWVTDVEAKDLRSSLPDWEPEAQAAVSCMGEVVSRWAICTLSPLPFFQRSRVVLLGDAAVRVTTPFSTFSSDHCQTLACYDELPRCRLRPGDDAYILSEILTHPAVTRDNVQKALEIYSEVRVPMSTHVLESSRRTGMDCALHDEVAAADLKSLGERMQQEMVWAWEWNPEDEKKKALDLVEERLV | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl CoA by step-wise elimination of ammonia from phenylalanine by the phenylalanine ammonia-lyase str11, oxygenation by str8 and retro-Claisen reaction to form benzoic acid, which is activated to its CoA thiolester benzoyl CoA by the dedicated CoA ligase str10 . Benzoyl CoA forms the starter unit for the highly reducing polyketide synthase stpks1 that produces the polyketide prestrobilutin A . The FAD-dependent oxygenase str9 then catalyzes the key oxidative rearrangement responsible for the creation of the beta-methoxyacrylate toxophore . Str9 performs epoxidation of the 2,3 olefin of prestrobilutin A, followed by Meinwald rearrangement to furnish the aldehyde intermediate (Probable). Rapid enolization of the aldehyde intermediate would give the beta-methoxyacrylate skeleton and methylations catalyzed by str2 and str3 complete the synthesis and lead to the production of strobilurin A (Probable). The short-chain dehydrogenase stl2 and the dehydrogenase str4 play a role in the shunt pathway leading to the production of bolineol . The cluster encodes no obvious halogenase gene that could be involved in production of strobilurin B, nor any obvious dimethylallyl-transferase that could be involved in the production of strobilurin G (Probable). It is possible that unknown proteins encoded in, or near, the cluster (such as str1 or stl1) may form new classes of halogenases or dimethylally-transferases, or that the responsible genes are located elsewhere on the genome (Probable). Similarly, proteins encoded by str5/str6 hydrolases appear to have no chemical role in the biosynthesis of strobilurin A (Probable). Finally, no obvious self-resistance gene is found within the cluster (Probable).
Sequence Mass (Da): 51392
Sequence Length: 463
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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Q0V8E7 | MSTQAAGNQTSSGATDSEDSYDSWYIDEPQGGQELQPEGLVPSCQPNVPPSLYHTCLAVLSILVLFLLAMLVRRRQLWPRCGHGRPGLPSPVDFLTGDRPRTVPAAVFMVLFSSLCLLLPTEDPLPFLSLASPPGRDGEAETSRGPWKILALLYYPALYYPLAACATVRHGAAHLLGSLLSWAHLGVQVWQRAECPESPKIYKYYSLLASLPLLLGLGFLSLWYPVQLVRSFGHGAATGSKGLQSSYSEEYLRTLLCQKKLKSSSHTCKRGFASQAWMYFRHSVYIPQRGFRLPLKLVLSVTLTGTAIYQVALLLLVGVVPTIQKVRAGITTDVSYLLAGFGIVLSEDRQEVVELVKHHLWALEVCYISALVLSCLLTFLMLVHSLVTHRTNLRALHRGGALDIGPLTQSPRPSRQAIFCWMSFTAYQTAFTCLGLLVQQILFFLGTLTLAFLVFMPMLHGRNLLLLHYLKSSWPFWLTLALAVTLQNAAAHWAFLDTHHGRPGLTNRRALYAATFLLFPVNVLVGTMVAAWRVLLSALYNAVHLGRMDLSLLPLRAATLDPGYHTYCNFLRMEASQSHPAATAFCALLLRTQRPKPRATPQDGLRLGEEEEGIQLLQTKDLVAKGAGPRARQGRARWGLAYTLLHNPALQAFRKTALPGARPNGAQP | Function: Functions as retinol transporter. Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1 . Retinol uptake is enhanced by LRAT, an enzyme that converts retinol to all-trans retinyl esters, the storage forms of vitamin A. Contributes to the activation of a signaling cascade that depends on retinol transport and LRAT-dependent generation of retinol metabolites that then trigger activation of JAK2 and its target STAT5, and ultimately increase the expression of SOCS3 and inhibit cellular responses to insulin. Important for the homeostasis of vitamin A and its derivatives, such as retinoic acid. STRA6-mediated transport is particularly important in the eye, and under conditions of dietary vitamin A deficiency. Does not transport retinoic acid (By similarity).
PTM: Phosphorylated on tyrosine residues in response to RBP4 binding. Phosphorylation requires the presence of LRAT, suggesting it may be triggered by the uptake of retinol that is then metabolized within the cell to retinoids that function as signaling molecules.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73762
Sequence Length: 668
Domain: Contrary to predictions, contains nine transmembrane helices, with an extracellular N-terminus and a cytoplasmic C-terminus . Besides, contains one long helix that dips into the membrane and then runs more or less parallel to the membrane surface (By similarity).
Subcellular Location: Cell membrane
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