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stringlengths 6
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stringlengths 11
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stringlengths 108
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P38278 | MHSRKSKSITGKRKQVGSNVTRVIKPQKTRRIIRRFHHLINKRQSICKFLCLKENLDDSNEEKNDKIIRLSIKGNVRLGKYYEDGKSQSFNDAMESQLLRLHSLIKNESKSKDTSDLAVMYTLLGYIMNQINKLGGLETYQIASQNGQLKERGGDTSKLLEKWIRSSFENCPGAVALEIGSLSSGNRISRCALFRNVVRIDLEEHEGVIKQDFMERPLPRNENDKFDLISCSLVLNFVKNHRDRGAMCHRMVKFLKPQGYIFIVLPQACVTHSRYCDKTLLQNLLGSIGLIMLNSHQSNKLYYCLYQLQVVPPQPSSFSKRIKVNDGPGLNNFGITL | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine 2142 in 25S rRNA. N(1)-methyladenine(2142) in 25S rRNA is present in helix 65, a region that accounts for most of the intersubunit surface of the large subunit.
Catalytic Activity: adenosine(2142) in 25S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(2142) in 25S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38550
Sequence Length: 337
Subcellular Location: Nucleus
EC: 2.1.1.286
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Q5A846 | MFESDLSFYSALLILCCPISIVFFKKFPIKGYTGANKVSLFLQCLIAILNLNILYSFINSLTITLGHDGSSANTLTIDPITTTQQQGHVDYTPIKVSGYTFKNQVATKNLQCDSIVYDQDLDLQVSQAVDLNKPEDLKFFRDKLNELRSLNNIYDLFFQDNEDEVEESILERKWYKFCGSAVWLDKYGVYFMVNRIAYSKKGTRNNPTISVLAGQVFDKNWIELTGKKFPFSGLEFPTILPHYIDEGKEAEKVILGAEDPRVILHEYTNENGIRIQEPLIAFNALSTEVDWKRAMHIYRPLHDPHRIIRLSIENYAPREKEKNWAPFIDGNNLNFVYNFPLRILRCNINNGDCQKVSGPDFNDKSHENAGKLRGGTNLVEIPSQSLPKHLRSRKYWFGIARSHITDCGCVGELYRPHLILISRNKKSDQYELNYVSDLIDFNVNPEPWTPGKTTCSDGKSVLIPNSVAFIKDDYMSVTFSEADKTNKLINAKGWLTYITKMLEFTQERLKDESSDPVLESRLLSKCSTFLAQQYCALSKDTMGWDKLSR | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for addition of the second beta-mannose residue to acid-stable fraction of cell wall phosphopeptidomannan, and in elongation of beta-mannose chains on the phosphopeptidomannan acid-labile fraction.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 62926
Sequence Length: 549
Subcellular Location: Membrane
EC: 2.4.1.-
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Q5ABT8 | MTKSYMPLFRSPRQFKKIYFILIPLILAVIILHVFFDGFNKISEYSPTFISNRILNHQDQQQKSEKSSDVISSYFPSLAIYPKNFDNRVEFVNEPKNSKWIQYFGDSKTVLSNYITNQTYTNHSIGLYSSSTVRPPASSCKDILYERSFEITKYRTLHDDLYKLATTLLYQLENDPAFQDLSPFFNDRLPHIIMRGELHKHIYKFAGTSVWLEQHGVHLMLSRVIYSQQGKKNDPQLSLLYAQVYDENWNELNDIELIVPVINPNGERVYDSVKYPQFLAIPFYHNSEYIKSRWYGPEDTRLILTKNKFGDDEPVIIFNSYHRQIKDMSTEDDNNVHTKFEFYRSMFVGWLFQYQLGKLNTDGIQDSKFNNVTFNKVKELRIEGKERTSIEKNWTPFIDPDERNQISYYGNHNLGDNYVYIVYQWNHLKILKCELDNFIDSSHSTCTMFFKDVETTQEVGPVRGGTELWPIKIDNNNNNNNLNEDDLSTKQEPQQQRQLWIGFLRAHVKDCGCGGSMYRPNFLILEKLNSKFKLTYLSGSINFNVSVYGWANYDVVCAGHEANALIPNGISMFDQDDDYLTLSMSVADQDNTLVHIHGVKKLIYSLDHDWNGILKENKQIECVVNNANDFCKAYADEHYKLGDSEAAIKEVKQKAKEEAEKAKAEKEKAEKEKAEKEKAEKEKEEKEKEEKEEKEKAEKEKEEKEKAEKELAEKELAEQKDEDAKDEDKNEDEDDKEKNDESGLTEKSEVEENGENTNEGGEDDGDGDGEEEKEDDDDIEV | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for the elongation of beta-mannose chains on the acid-labile fraction of cell wall phosphopeptidomannan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 90959
Sequence Length: 781
Subcellular Location: Membrane
EC: 2.4.1.-
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F2QZ45 | MKLDTQQISHLLSRQMYHLAPRKKLLIWGGSLGFVLLLLIVASSHQRIRSTILHRTPISTLPVISQEVITADYHPTLLTGFIPTDSDDSDCADFSPSGVIYSTDKLVLHDSLKDIRDSLLKTQYKDLVTLEDEEKMNIDDILKRWYTLSGSSVWIPGMKAHLVVSRVMYLGTNGRSDPLVSFVRVQLFDPDFNELKDIALKFSDKPDGTVIFPYILPVDIPREGSRWLGPEDAKIAVNPETPDDPIVIFNMQNSVNRAMYGFYPFRPENKQVLFSIKDEEPRKKEKNWTPFFVPGSPTTVNFVYDLQKLTILKCSIITGICEKEFVSGDDGQNHGIGIFRGGSNLVPFPTSFTDKDVWVGFPKTHMESCGCSSHIYRPYLMVLVRKGDFYYKAFVSTPLDFGIDVRSWESAESTSCQTAKNVLAVNSISNWDLLDDGLDKDYMTITLSEADVVNSVLRVRGIAKFVDNLTMDDGSTTLSTSNKIDECATTGSKQYCQRYGELH | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Responsible for addition of a hexose to the beta-mannose chain (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 56665
Sequence Length: 503
Subcellular Location: Membrane
EC: 2.4.1.-
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Q5ALW2 | MVQKQYRFAPKSIFTFVFLCFVAIVVIISTSSLVQVEESLDPIEVSDEIKKHDRKVVIFPSNFQSANNKLADFLTEAFGQRLNKGDIVYKNRDTYELPQTVYTWNTIDLFQSIGEKDNLKCEKIPLNFEISKIYNKNADLYKILRDFKNENSFYYKEVSVFFPDLGKQLRERTIEKHWFQLIGSSVWLEQYGVHLMISRVIYTKTGNKVQPVISLSYVQAFDRNWTELKNVTLVVPDSGKAKFKTVSYPSFIPIPVYHNVNQQRGKFYGVEDPRIMLVKNKEGYEEPLIVYNSFNRSPPNANYLEEIKNLVKLDTYRSIFMAWIWRTQLGKSNVGSSLPDLATTDDHKYVKVKELSLPNKKRPKTEKNWTPFVIYEDQKKQGYDSHLYFIYSFQDLSILKCSLWDAGNCIWEYRMNNKKTKISELRGGTELMNVNQLLDKYNFAGLETVKDQFKGKEVWISFARAALSKCGCGSKMYRPNFTVLVKQGGRFQLSFVSSYMDFGVPILPWAKGKGLCNGKNLLIPNGISNWVLAKDEGGGFQDYMTLSLSRSDSTVDIIHMKGILKSILSEYLLQTNRDVLNNNAIHCALLESESYCKSYAENYRAHLKRWQN | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for beta-1,2-mannose transfer on phospholipomannan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 70896
Sequence Length: 612
Subcellular Location: Membrane
EC: 2.4.1.-
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O94480 | MGKKARFKEARRLQKRNLNNAIGSSSINSQNSLTNDKIGKGKNKGPTERYVLPFEKNNRFLLLGEGNFSFAFSLLLHHVSSEGFVLATSYDSKEDLKQKYPDAAEYISKIEINGGKVMHEIDATKLHLHKKLKTQKFDTIFWNFPHSGKGIKDQDRNILDNQKMLLAFFKASKFLLSEKGVIVITLAETKPYTLWNLKGLAKDAGYTSLMTEKFDSSFYPEYSHRRTIGWIDGISERSPWKGELRDSRHYCFVVNGSNIKPYNQRKEKRKRSELSDDSSDSS | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of a uridine in 25S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine in 25S rRNA = H(+) + N(3)-methyluridine in 25S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32345
Sequence Length: 282
Subcellular Location: Nucleus
EC: 2.1.1.-
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P40493 | MARKLKGKIGSKGLKGALLRHKAKVKLVRNIESKQKHELRKKNSSANNKTVKRNQEFQKLNQGKVMPFEKDETLMLCGEGDFSFARSIVEQNYIESDNLIITSYDNSVNELKLKYPHTFEENYQYLKDLNIPIFFQIDVTKLVKSFKISKNNTWFKIINRLSDHRWGNKPLQNIVFNFPHNGKGIKDQERNIREHQDLIFNFFQNSLQLFNLINTKIQNDTLRYTQGYDLNEDTPQAKKLTAEGYGNIILSLFDGEPYDSWQIKLLAKKNGLTLSRSSKFQWENFPGYHHRRTNSEQDTTKPAKERDARFYIFSKYVSNSSKHNRKSKKDTDSDSD | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of uridine 2634 (m3U2634) in 25S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2634) in 25S rRNA = H(+) + N(3)-methyluridine(2634) in 25S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39402
Sequence Length: 336
Subcellular Location: Nucleus
EC: 2.1.1.313
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Q5ABU8 | MGNYKPSIKQYVVTVKAIKSSQFGRLGICAVVLLFVLGYPFYFISNNPFDTSIRYQYVDPYNDTTRKYTTIEKQHTDIGGNGTTILYPKNLQLDQTALSQLLNTTETTNPFVQYIGNSSSIAFSQLNQTLVNHSIQVFDPFSNSDNCSDLMTETQLTISQNIIIKESFEIMVKRLMHQLDTEPAFKELAPFFQNKLSLHLRMRSYHKHFYKFARTSVWLKDYGVHLMISRVIYSQKGKKGDPQISLLYTQLYDTNWQELTNTDLLVSMQDITGEYKLEKLQFPRFLPMPFYYNPKLTKGRWYGPEDARIMLVKNQLDMEEPVVIYNSYHRQIANHTTTGKTDGSVELNFEFYRSMFVGWPFRYQLGKSNTDGFVDDRFDNVKFTRVAELKIHNQTRASIEKNWTPFVDPSERDPEDKSLYIVYQWDKLRILKCDISNLVTDDGFIHYSACRFKQDTKHDEVEKVGPIRGGTELIPTIINNKQLWVGFLRAHIDKCGCGKAMYRPNMVVLQKTDMGTFQVAYLSSYISFNIPVPGWKTHEIQCGKRDPNVLIPNGISNWEVATIDGIERDVLTMTLSAADEDNILMDIHGLKTVIKNLITNQKHGNEFNSDSVQMKCVVAYSIEFCRAYGEEQARLGLTGGWLPSHN | Function: Beta-mannosyltransferase involved in cell wall biosynthesis. Required for beta-1,2-mannose transfer on phospholipomannan. Required for pro-inflammatory response in macrophages through phospholipomannan-induced TNF-alpha production.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 74499
Sequence Length: 646
Subcellular Location: Membrane
EC: 2.4.1.-
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Q12291 | MLLMRRFAFLTSSVYFKYIPIYSQYHYSSQFPINMNPKKVAQLPVHNKSTLPPQEIIDLFKITFLEELYPKDQDNEKSPLTEQIQAVKSDLYNRDYNAAFNNDSKRIAYCCRWSPSRATSYASVFAHFPELLKIIRCEIDDKDSNVLCIGGGAGGELVALASIFTLSRDFSSKFASALKIDNEVNKKPRNLNIQLVDIADWSTVVEKLTATIKSKWLYGDSEAESFNVNFTHKDCLQMTEPQDIKIYQGLDLITLLFTTNELFTQKKVESIKFLQRLNENCAPGCHLLILESAGSYSHITINNKKFPIQFLIDTILVGNRKDKGTTGPWSLVSENDSIWYRMDPKLDYSIPLENMRFFYRLYVKN | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of uridine 2843 (m3U2843) in 25S rRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2843) in 25S rRNA = H(+) + N(3)-methyluridine(2843) in 25S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42041
Sequence Length: 365
Subcellular Location: Cytoplasm
EC: 2.1.1.312
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Q19000 | MLSALLIRNIRNASKLASVAGPNSDRIVNVKWSDGKTGVFPLIWLRDTSPDPSTYTISPAMTARKLTMLEFDVEQNARKLWIDEDANCLKIEWESGVLSEFPSEWLKIRNPSDQEARRRRRKVYLFPEQTWGKAEIEGKLKKFSHEEFMKNEQVVHDFLQAVCIDGIAVLKGAPQGVRGAVEAIGDRIGMIKRTHFGLVFEVSLKADASNMAYASNGGLPFHTDFPSLSHPPQLQMLHMLQSAEEGGHSLFVDGFHVAEQLRVEKPEIFKILTTQSMEYIEEGYDVHEINGKTIRFDYDMCARHKVIRLNDDGKVNKIQFGNAMRSWFYDCEPSKVQDVYRAMKTFTEYCYQPRNMLKFRLEDGDTVLWANQRLLHTRDGFRNAPEKARTLTGCYFDWDIVKSRVRFLRDKLSLEQNQPSA | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Catalytic Activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate
Sequence Mass (Da): 48436
Sequence Length: 421
Pathway: Amine and polyamine biosynthesis; carnitine biosynthesis.
EC: 1.14.11.1
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O75936 | MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIFDVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISRHLEGAYADWDVVMSRLRILRQRVENGN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Catalytic Activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate
Sequence Mass (Da): 44715
Sequence Length: 387
Pathway: Amine and polyamine biosynthesis; carnitine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.14.11.1
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P80193 | NAIADYRTFPLISPLASAASFASGVSVTWADGRVSPFHNLWLRDNCPCGDCVYEVTREQVFLVADVPEDIQVQAVTIGDDGRLVVQWDDGHASAYHPGWLRAHAYDAQSLAEREAARPHKHRWMQGLSLPVYDHGAVMQDDDTLLEWLLAVRDVGLTQLHGVPTEPGALIPLAKRISFIRESNFGVLFDVRSKADADSNAYTAFNLPLHTDLPTRELQPGLQFLHCLVNDATGGNSTFVDGFAIAEALRIEAPAAYRLLCETPVEFRNKDRHSDYRCTAPVIALDSSGEVREIRLANFLRAPFQMDAQRMPDYYLAYRRFIQMTREPRFCFTRRLEAGQLWCFDNRRVLHARDAFDPASGDRHFQGCYVDRDELLSRILVLQR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Catalytic Activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate
Sequence Mass (Da): 43322
Sequence Length: 383
Pathway: Amine and polyamine biosynthesis; carnitine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.14.11.1
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Q9QZU7 | MHCAILKAEAVDGARLMQIFWHDGAESLYPAVWLRDNCQCSDCYLHSAKARKLLLEALDVNIRMDDLTFDQKKVYITWPNGHYSEFEANWLKKRCFSQEARAGLQGELFLPECQYWGSELQLPTLNFEDVLNDDDHAYKWLSSLKKVGIVRLTGAADKRGEIIKLGKRIGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKEKNPQAFSILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTVFDVPIERVQPFYAALKEFVDLMNSKEYKYTFKMNPGDVITFDNWRLLHGRRSYEAGTEISRHLEGAYADWDVVMSRLRILRQRVMNGN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Catalytic Activity: 2-oxoglutarate + 4-(trimethylamino)butanoate + O2 = carnitine + CO2 + succinate
Sequence Mass (Da): 44546
Sequence Length: 387
Pathway: Amine and polyamine biosynthesis; carnitine biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.14.11.1
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P24282 | MEPIFIIGIILGLVILLFLSGSAAKPLKWIGITAVKFVAGALLLVCVNMFGGSLGIHVPINLVTTAISGILGIPGIAALVVIKQFII | Function: Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB-processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8964
Sequence Length: 87
Subcellular Location: Forespore outer membrane
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O81851 | MAVQAHHMNIFSQFISPNRDCVKFQENMNHGEFEFTGGEVPLITGESFAVEPLAAKANFNKAESGLSYNFTVPPLSTKRQRDFQFSDSNAPVKRRSVAFDSSSPSLINVELVSQIQNQQQSEIDRFVAQQTEKLRIEIEARQQTQTRMLASAVQNVIAKKLKEKDDEIVRIRNLNWVLQERVKSLYVENQIWRDIAQTNEANANTLRTNLDQVLAQLETFPTASAVVEDDAESSCGSCCGDGGGEAVTAVGGGCKRCGEREASVLVLPCRHLCLCTVCGGSALLRTCPVCDMVMNASVHVNMSS | Function: E3 ubiquitin-protein ligase involved in the regulation of pathogen and abiotic stress responses by facilitating degradation of MYB108/BOI. Attenuates cell death by preventing caspase activation. Has no effect on the stability of the DELLA proteins. Not regulated by MYB108/BOI.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 33509
Sequence Length: 304
Domain: The N-terminal domain (1-150) prevents cell death by suppressing caspase-like protease activation.
Pathway: Protein degradation; proteasomal ubiquitin-dependent pathway.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q6DC66 | MEMLRRSSVFAAEVMEVFDRSPTDKELVSQSKVLCRDYIHSRLHRAGIGWSKPEHGSGGTLAEVSSVLLWLGDELEYLRPNVYRNVARQLNITIASENIVSDAFLAVAAEIFSTEYSRKGLEKHKGVTWGKIVSLYAVAGALAVDCVRNGHPAMVHTIVDCMGEFVRKSLASWLKKRGGWADITKCVVSTDPSFHSHWLVTAACACGHYLKAVVFYLLREK | Function: May play a role in apoptosis. Does not appear to show pro-apoptotic activity when expressed ectopically in early embryos.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24599
Sequence Length: 221
Subcellular Location: Membrane
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Q7T381 | MNVFARSSVLAAEMIDVFDRTHTEKELVFQSKELCRDFIHSRITREGLSWSKVELDLPEPRGVLVDVSVVLLKLGDELECMRPYVYRNIAKQLNISVSVEAVVSDAFLSVATEVIAMGITWGKVVAIYAVAAGLAVDCVRLGHPVMVHTIVDSLGEFVRRSLVPWLKKRGGWVDILKCVVNMDSRAHVHWLSTAVLTWREFIKTMYVYLTK | Function: May play a role in apoptosis. Does not appear to show pro-apoptotic activity when expressed ectopically in early embryos.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23834
Sequence Length: 211
Subcellular Location: Membrane
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O35425 | MEVLRRSSVFAAEIMDAFDRSPTDKELVAQAKALGREYVHARLLRAGLSWSAPERASPAPGGRLAEVCTVLLRLGDELEQIRPSVYRNVARQLHIPLQSEPVVTDAFLAVAGHIFSAGITWGKVVSLYSVAAGLAVDCVRQAQPAMVHALVDCLGEFVRKTLATWLRRRGGWTDVLKCVVSTDPGFRSHWLVATLCSFGRFLKAAFFLLLPER | Function: Apoptosis regulator that functions through different apoptotic signaling pathways . Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner . In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response . Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD-proteasome degradation system, resulting in cytochrome c release . In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner. Plays a role in granulosa cell apoptosis by CASP3 activation (By similarity). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation . In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression.May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (By similarity).
PTM: Ubiquitinated by AMFR/gp78 E3 ubiquitin ligase complex; mediates degradation by ubiquitin-proteasome pathway in a VCP/p97-dependent manner; prevents from proapoptotic activity; promotes degradation of newly synthesized proteins that are not ITPR1 associated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23456
Sequence Length: 213
Domain: BH4 domain mediates interaction with ITPR1.
Subcellular Location: Mitochondrion membrane
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P47229 | MTALTESSTSKFVKINEKGFSDFNIHYNEAGNGETVIMLHGGGPGAGGWSNYYRNVGPFVDAGYRVILKDSPGFNKSDAVVMDEQRGLVNARAVKGLMDALDIDRAHLVGNSMGGATALNFALEYPDRIGKLILMGPGGLGPSMFAPMPMEGIKLLFKLYAEPSYETLKQMLQVFLYDQSLITEELLQGRWEAIQRQPEHLKNFLISAQKAPLSTWDVTARLGEIKAKTFITWGRDDRFVPLDHGLKLLWNIDDARLHVFSKCGHWAQWEHADEFNRLVIDFLRHA | Function: Catalyzes an unusual C-C bond hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) to produce benzoic acid and 2-hydroxy-2,4-pentadienoic acid (HPD).
Catalytic Activity: 2,6-dioxo-6-phenylhexa-3-enoate + H2O = 2-oxopent-4-enoate + benzoate + H(+)
Sequence Mass (Da): 32030
Sequence Length: 286
Pathway: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl: step 4/4.
EC: 3.7.1.8
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O05151 | MQSPINSFKKALAEGRTQIGFWLALGDAYSAEVCAGAGFDWLLIDGEHAPQDLRSVLAQLQVIGAYRDCHAAVRVPSADTTVIKQYLDLGAQSLLVPMVDTADEAAAVVRACRYPPGGIRGVGGARASRWGRYPRYLHEADEQVCVVVQAETALALSNLEAIAEVDGIDGVFIGTADLAASLGFPGNPAHPEVQDAILDALQRVRAAGKAPGVLTPVEDLAQKYLAHGAVFVAVGIDTHLLAKQTSALAARFAQVAYS | Function: Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-oxovalerate to pyruvate and acetaldehyde.
Catalytic Activity: (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
Sequence Mass (Da): 27159
Sequence Length: 258
Pathway: Xenobiotic degradation; biphenyl degradation.
EC: 4.1.3.39
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Q8R164 | MATATVRPAAQRLRLLLSPLKSRICVPQAEPVATFGTAVTSAKVAVNGVHLHYQRVGEGEHAILLLPGMLGSGKTDFAPQLQSLNKKRFTLVAWDPRGYGYSRPPDRDFPRDFFERDAKDAVDLMKALQFKQVSLLGWSDGGITALIAAAKYPSYIRKMVIWGANAYVTEEDSRIYQGIRDVSKWSEKARKPLEALYGYDYLAKTCEDWVDGISQFKQLPEGNICRHLLPLVQCPTLIVHGEKDPLVPRFHADFLLQHVKGSRLHLMPEGKHNLHLRFADEFNRLVEDFLQ | Function: Serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. Activates valacyclovir to acyclovir. May play a role in detoxification processes. It is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol (By similarity).
Sequence Mass (Da): 32851
Sequence Length: 291
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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B4E8N5 | MTHPTELPLSPLSALQFYATAPYPCSYLDGRIARSQVATPSHLINSDIYTELVKAGFRRSGVFTYRPYCDGCRACVPVRVPVGEFAPTRTQRRMWKRHRALVATVSPLHYDEEHYALYMRYQSARHAGGGMDRDSRDQYEQFLLQSRINSRLVEFRDLDAPGGEPGKLRMVSMIDILGDGLSSVYTFFEPDDRHTSYGTYNILWQIEQAKSLGLPYVYLGYWIRESPKMAYKANFHPLEGLIDGRWKTLDPERVDLPPVDAALARAPLPGGHSGSG | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 31250
Sequence Length: 276
Subcellular Location: Cytoplasm
EC: 2.3.2.29
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Q9LY74 | MASLMLNGAITFPKGLGSPGSNLHARSIPRPTLLSVTRTSTPRLSVATRCSSSSVSSSRPSAQPRFIQHKKEAYWFYRFLSIVYDHVINPGHWTEDMRDDALEPADLSHPDMRVVDVGGGTGFTTLGIVKTVKAKNVTILDQSPHQLAKAKQKEPLKECKIVEGDAEDLPFPTDYADRYVSAGSIEYWPDPQRGIREAYRVLKIGGKACLIGPVYPTFWLSRFFSDVWMLFPKEEEYIEWFKNAGFKDVQLKRIGPKWYRGVRRHGLIMGCSVTGVKPASGDSPLQLGPKEEDVEKPVNNPFSFLGRFLLGTLAAAWFVLIPIYMWIKDQIVPKDQPI | Function: Involved in a key methylation step in both tocopherols (vitamin E) and plastoquinone synthesis. Catalyzes the conversion of 2-methyl-6-phytyl-1,4-hydroquinone (MPBQ) to 2,3-dimethyl-6-phytyl-1,4-hydroquinone (DMPQ, a substrate for tocopherol cyclase), and 2-methyl-6-solanyl-1,4-benzoquinone (MSBQ) to plastoquinone.
Catalytic Activity: 2-methyl-6-phytyl-1,4-benzene-1,4-diol + S-adenosyl-L-methionine = 2,3-dimethyl-6-phytylbenzene-1,4-diol + H(+) + S-adenosyl-L-homocysteine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37927
Sequence Length: 338
Pathway: Cofactor biosynthesis; tocopherol biosynthesis.
Subcellular Location: Plastid
EC: 2.1.1.295
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P74388 | MPEYLLLPAGLISLSLAIAAGLYLLTARGYQSSDSVANAYDQWTEDGILEYYWGDHIHLGHYGDPPVAKDFIQSKIDFVHAMAQWGGLDTLPPGTTVLDVGCGIGGSSRILAKDYGFNVTGITISPQQVKRATELTPPDVTAKFAVDDAMALSFPDGSFDVVWSVEAGPHMPDKAVFAKELLRVVKPGGILVVADWNQRDDRQVPLNFWEKPVMRQLLDQWSHPAFASIEGFAENLEATGLVEGQVTTADWTVPTLPAWLDTIWQGIIRPQGWLQYGIRGFIKSVREVPTILLMRLAFGVGLCRFGMFKAVRKNATQA | Function: Involved in a key methylation step in both tocopherol (vitamin E) and plastoquinone synthesis. Catalyzes the conversion of 2-methyl-6-phytyl-1,4-hydroquinol (MPBQ) to 2,3-dimethyl-6-phytyl-1,4-hydroquinol (DMPQ, a substrate for tocopherol cyclase), and 2-methyl-6-solanyl-1,4-benzoquinol (MSBQ) to plastoquinol.
Catalytic Activity: 2-methyl-6-phytyl-1,4-benzene-1,4-diol + S-adenosyl-L-methionine = 2,3-dimethyl-6-phytylbenzene-1,4-diol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34947
Sequence Length: 318
Pathway: Cofactor biosynthesis; tocopherol biosynthesis.
EC: 2.1.1.295
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O74510 | MSGSKCCSSSNTIKVSIYLFLHTLTYGLLNYHLNPRLLASTGVVESDIPYWMSYLSIIMHVGQSLLLQKFNLGYGWLLLTKYPVYVLLSTYYLTPLSQIAWAFIIDAISLLVARCFSRANPIKCSNQVNTQYSVSFLFTIMASVLISVLNYISQKIFLNGLILGNSHNVVTSLVAPPLPLQYLAHVPIGYVIQRVVFSERPIPQSLFLMIFLTLWNCFIPYSILFSMNWSAMFQVVGAYLSQIWIITFICWALSL | Function: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28899
Sequence Length: 255
Subcellular Location: Endoplasmic reticulum membrane
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O60158 | MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSAFPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEGEPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPSSSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVNKGMNGVANQVNKGVTGVASQVRKPVGKLEKKFENLEKSIGDTLKSSIRSSPKSKKRSREDFEENEDYNAMVPVKRSRITKLESEVYYEKRKVRALGGIAIGLGVGAILPFLF | Function: Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47827
Sequence Length: 432
Subcellular Location: Cytoplasm
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A8KBY2 | MSKNCPECGSSRVVEDDLYSQKQWVCEDCGSVVSEGLLTTTLSEESHSRAVPFFTSTAAFKKPCRNLVSGFSRLRALCRIFRLSSSMEDASANLFERAYNHPNFLHISLSKKQILAGCCMFHICRQNSWPVFMGTIGYLLDADNYQMGTIYQELTKSLNLQTTQVCITRMLESFCYDFKLAPDEVEEVFSVAQQRLVDQTSALLELAADTWILTGRRPFPLFLAAVYVAWQSLNPLARMKYSLMKFCKIAKAPEQLWCKSKDTINKRLNELLEVLCKLGRELPWVRPTDIQMNTVTTLVEDILKHRKALLILAVKHYEKQLEETQTSQYSESELSDSKSSVQTQCKSPPDEEDEGCELPPDHWGKRHLFLPPCVRTQKRQKINEAPLEVTGDEDISDSEIESYIRSEEEIKLFAKARKKICKY | Function: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates expression of target genes in response to oxidative stress. Overexpression protects cells against apoptosis in response to oxidative stress.
PTM: In response to oxidative stress, a Cys-residue is reversibly oxidized to cysteine sulfenic acid. This impairs formation of a ternary complex with TBP and DNA and down-regulates expression of target genes in response to oxidative stress.
Sequence Mass (Da): 48439
Sequence Length: 423
Subcellular Location: Nucleus
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Q9HAW0 | MPGRGRCPDCGSTELVEDSHYSQSQLVCSDCGCVVTEGVLTTTFSDEGNLREVTYSRSTGENEQVSRSQQRGLRRVRDLCRVLQLPPTFEDTAVAYYQQAYRHSGIRAARLQKKEVLVGCCVLITCRQHNWPLTMGAICTLLYADLDVFSSTYMQIVKLLGLDVPSLCLAELVKTYCSSFKLFQASPSVPAKYVEDKEKMLSRTMQLVELANETWLVTGRHPLPVITAATFLAWQSLQPADRLSCSLARFCKLANVDLPYPASSRLQELLAVLLRMAEQLAWLRVLRLDKRSVVKHIGDLLQHRQSLVRSAFRDGTAEVETREKEPPGWGQGQGEGEVGNNSLGLPQGKRPASPALLLPPCMLKSPKRICPVPPVSTVTGDENISDSEIEQYLRTPQEVRDFQRAQAARQAATSVPNPP | Function: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites . Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress . Down-regulates expression of target genes in response to oxidative stress . Overexpression protects cells against apoptosis in response to oxidative stress .
PTM: In response to oxidative stress, Cys-361 is reversibly oxidized to cysteine sulfenic acid. Oxidation of Cys-361 impairs formation of a ternary complex with TBP and DNA and down-regulates expression of target genes in response to oxidative stress.
Sequence Mass (Da): 46533
Sequence Length: 419
Subcellular Location: Nucleus
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Q4V8D6 | MPNGSRCPDCGSSELVEDSHYSQSQLVCSDCGCVVTEGVLTTTFSDEGNLREVTYSRSTGENEQVSRSQQRDLRRVRDLCRILKLPLTFEETAVSYYQKAYQLSGIRAARLQKKEVVVGCCVLITCRQHNWPLTMGAICTLLYADLDVFSSTYMQIVKLLGLDVPSLCLADLVKSYCSSFKLFQASPSMPAKYVEDKDKMLSRTLLLVELANETWLVTGRHPLPIITAATFLAWQSLRPSDRLTCSLARFCKLANVDLPYPAASRLQELLAVLLQMASQLAWLQVLRLDKRSVVKHIGDLLQHRHMLVRMAFQDGTAEVETKQQQPQGRGQQEEVGDSTFDLPKRKRPASPALLLPPCMLKPPKRTHTMPPDSVVTGDEDISDSEIEQYLRTPQEVRDFERAQAASRAAMSVPNPP | Function: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates expression of target genes in response to oxidative stress. Overexpression protects cells against apoptosis in response to oxidative stress.
PTM: In response to oxidative stress, Cys-358 is reversibly oxidized to cysteine sulfenic acid. Oxidation of Cys-358 impairs formation of a ternary complex with TBP and DNA and down-regulates expression of target genes in response to oxidative stress.
Sequence Mass (Da): 46596
Sequence Length: 416
Subcellular Location: Nucleus
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A4QNR3 | MSGAKQCPDCGSSDIVEDAHYSQDQVVCADCGCILSEGLITTTAAEESHLQAVRFADSTGENDSMTVSKLRGIVRVRNICRVLRLPDGFSDTAVSYYEQAYKHPLYHSVSIEKKEIIVGCCVYITCRQHQWPITMATICSLVYAKKELFASIFLSIVQVLKLDVPSVSLQNLVMSHCRSFKLFKDSCEVPSHYAEKLDTVSERTVQTVELAYETWLVTGRHPIPIITAAAYISWQSLLPARRLSCSLSRFCKLSDVDLPPPSAIRLRELQGTLIKLSVYLPWLKVLSLNKKTVVQHLGDLLRHRVFLLRKALAVTEAELSRGTLADTEAQLSRGTLADTEAQLSRGTLADTEAQLSRGTLADTEAQLSRGTLADTEAQLSRGTLADTEAQLSRGTLADTEAQLSRGTLADTEAQLSRGTLADTVAQLSRGTLADTEAQLSRGTKALSSNDQPNSTFVFLPPCVSNPRKRSRSIPFPRGHLDITGDEDISDSEIEQYLRTPAEMKEFEQALNRDDELPNA | Function: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates expression of target genes in response to oxidative stress. Overexpression protects cells against apoptosis in response to oxidative stress.
PTM: In response to oxidative stress, a Cys-residue is reversibly oxidized to cysteine sulfenic acid. This impairs formation of a ternary complex with TBP and DNA and down-regulates expression of target genes in response to oxidative stress.
Sequence Mass (Da): 57126
Sequence Length: 519
Subcellular Location: Nucleus
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Q9FHE4 | MAVEARHMNLFSSQYITNRECVKSQTNMNNGQQIAGGGFPVTIGDRNLQYIDPINSFNKSESELTAISKRQRDSTFDSDALIASQKRRAIAFSPASLIDAELVSQIQQQNSEIDRFVAQQTETLRIELEARQRTQTRMLASAVQNAILKKLKAKDEEIIRMGKLNWVLQERVKNLYVENQIWRDLAQTNEATANNLRSNLEQVLAQVDDLDAFRRPLVEEADDAESSCGSCDGGDVTAVVNGGCKRCGELTASVLVLPCRHLCLCTVCGSSALLRTCPVCDMVMTASVHVNMSS | Function: E3 ubiquitin-protein ligase involved in regulation of abiotic stress responses. Not involved in ubiquitination of MYB108/BOS1. Has no effect on the stability of the DELLA proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 32549
Sequence Length: 294
Domain: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Pathway: Protein degradation; proteasomal ubiquitin-dependent pathway.
EC: 2.3.2.27
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F4IDI6 | MAVDAHHLFLSPPQLFSNRELTMNNNTMEPTSGGFCNNNQTGYGVVSPFSVPNHTSTTTTATPPLLHVYGGSDTIPTTAGYYADGATNLDCEFFPLPTRKRSRDSSRSNYHHLLLQNPRSSSCVNAATTTTTTTLFSFLGQDIDISSHMNQQQHEIDRFVSLHLYQMERVKYEIEEKRKRQARTIMEAIEQGLVKRLRVKEEERERIGKVNHALEERVKSLSIENQIWRDLAQTNEATANHLRTNLEHVLAQVKDVSRGAGLEKNMNEEDDAESCCGSSCGGGGEETVRRRVGLEREAQDKAERRRRRMCRNCGEEESCVLLLPCRHLCLCGVCGSSVHTCPICTSPKNASVHVNMSS | Function: Probable E3 ubiquitin-protein ligase. Has no effect on the stability of the DELLA proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 40085
Sequence Length: 358
Domain: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Pathway: Protein degradation; proteasomal ubiquitin-dependent pathway.
EC: 2.3.2.27
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Q9LDD1 | MAVEAHHLNPLFSSNREMIHPVEASGVVYNTQMRYGTVPTFNPTVECQTSLFNPIYNISPVDRLVHQSMKPTIQSVDSSLTFNSDNNVDFLRPVSSRKRSREESVVLNPSAYMQIQKNPTDPLMFLGQDLSSNVQQHHFDIDRLISNHVERMRMEIEEKRKTQGRRIVEAVEQGLMKTLRAKDDEINHIGKLNLFLEEKVKSLCVENQIWRDVAQSNEATVNALRSNLQQVLAAVERNRWEEPPTVADDAQSCCGSNDEGDSEEERWKLAGEAQDTKKMCRVGMSMCRSCGKGEASVLLLPCRHMCLCSVCGSSLNTCPICKSPKTASLHVNLSS | Function: Probable E3 ubiquitin-protein ligase. Has no effect on the stability of the DELLA proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 37709
Sequence Length: 335
Domain: The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Pathway: Protein degradation; proteasomal ubiquitin-dependent pathway.
EC: 2.3.2.27
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Q9XF92 | MGFPVGYTEVFLPKLFVQTLSILGFIRTIVFSIFRFLGLSDFLEMDQTWPDYTSYPTRIPETRSPFSALLIREILPVIKFEELTNSGEDLPENCAVCLYEFEGEQEIRWLRNCRHIFHRSCLDRWMDHDQKTCPLCRTPFVPDEMQEEFNQRLWAASGVHDFHCPVTELL | Function: May be involved in the brassinosteroids (BRs) signaling pathway and regulate the growth and development of rosette leaves . Seems to prevent over development of leaves and inflorescence stems .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20060
Sequence Length: 170
Subcellular Location: Membrane
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Q8WY22 | MGARASGGPLARAGLLLLLLLLLLLGLLAPGAQGARGRGGAEKNSYRRTVNTFSQSVSSLFGEDNVRAAQKFLARLTERFVLGVDMFVETLWKVWTELLDVLGLDVSNLSQYFSPASVSSSPARALLLVGVVLLAYWFLSLTLGFTFSVLHVVFGRFFWIVRVVLFSMSCVYILHKYEGEPENAVLPLCFVVAVYFMTGPMGFYWRSSPSGPSNPSNPSVEEKLEHLEKQVRLLNIRLNRVLESLDRSKDK | Function: Involved in tumorigenesis and may function by stabilizing p53/TP53.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27836
Sequence Length: 251
Subcellular Location: Mitochondrion outer membrane
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P48582 | MKPYLFDLKLKDTEKLDWKKGLSSYLKKSYGSSQWRTFYDEKATSELDHLRNNANGELAPSSLSEQNLKYYSFLEHLYFRLGSKGSRLKMDFTWYDAEYSSAQKGLKYTQHTLAFEKSCTLFNIAVIFTQIARENINEDYKNSIANLTKAFSCFEYLSENFLNSPSVDLQSENTRFLANICHAEAQELFVLKLLNDQISSKQYTLISKLSRATCNLFQKCHDFMKEIDDDVAIYGEPKWKTTVTCKLHFYKSLSAYYHGLHLEEENRVGEAIAFLDFSMQQLISSLPFKTWLVEFIDFDGFKETLEKKQKELIKDNDFIYHESVPAVVQVDSIKALDAIKSPTWEKILEPYMQDVANKCDSLYRGIIPLDVYEKESIYSEEKATLLRKQVEETETANLEYSSFIEFTNLPRLLSDLEKQFSDGNIFSNTDTQGQLMRDQIQTWCKFIQTNEFRDIEEQMNKIVFKRKQILEILSALPNDQKENVTKLKSSLVAASNSDEKLFACVKPHIVEINLLNDNGKIWKKFDEFNRNTPPQPSLLDIDDTKNDKILELLKQVKGHAEDLRTLKEERSRNLSELRDEINNDDITKLLIINKGKSDVELKDLFEVELEKFEPLSTRIEATIYKQSSMIDDIKAKLDEIFHLSNFKDKSSGEEKFLEDRKNFFDKLQEAVKSFSIFASDLPKGIEFYDSLFNMSRDLAERVRVAKQTEDSTANSPAPPLPPLDSKASVVGGPPLLPQKSAAFQSLSRQGLNLGDQFQNLKISAGSDLPQGPGIPPRTYEASPYAATPTMAAPPVPPKQSQEDMYDLRRRKAVENEERELQENPTSFYNRPSVFDENMYSKYSS | Function: Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. Acts as an adapter that recruits the DOA4 deubiquitinase to the endosomes, leading to deubiquitination of cargo proteins prior to the lumenal sequestration. Its association to the endosomes depends on SNF7 and its dissociation requires VPS4. Interacts functionally with the Pkc1p-mitogen-activated protein kinase pathway.
Sequence Mass (Da): 97276
Sequence Length: 844
Domain: The coiled-coil domain is essential for MVB sorting.
Subcellular Location: Cytoplasm
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P12428 | MQESGGSSGQGGPSLCLEWKQLNYYVPDQEQSNYSFWNECRKKRELRILQDASGHMKTGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDVVLNGMAMERHQMTRISSFLPQFEINVKTFTAYEHLYFMSHFKMHRRTTKAEKRQRVADLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYSVIKTLRHLCTRRRIAKHSLNQVYGEDSFETPSGESSASGSGSKSIEMEVVAESHESLLQTMRELPALGVLSNSPNGTHKKAAICSIHQPTSDIFELFTHIILMDGGRIVYQGRTEQAAKFFTDLGYELPLNCNPADFYLKTLADKEGKENAGAVLRAKYEHETDGLYSGSWLLARSYSGDYLKHVQNFKKIRWIYQVYLLMVRFMTEDLRNIRSGLIAFGFFMITAVTLSLMYSGIGGLTQRTVQDVGGSIFMLSNEMIFTFSYGVTYIFPAALPIIRREVGEGTYSLSAYYVALVLSFVPVAFFKGYVFLSVIYASIYYTRGFLLYLSMGFLMSLSAVAAVGYGVFLSSLFESDKMASECAAPFDLIFLIFGGTYMNVDTVPGLKYLSLFFYSNEALMYKFWIDIDNIDCPVNEDHPCIKTGVEVLQQGSYRNADYTYWLDCFSLVVVAVIFHIVSFGLVRRYIHRSGYY | Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family which transports various molecules including bioamines, neurotransmitters and metabolic intermediates . In the eye and probably in association with w/white, required for the transport of the eye red pigment precursor, guanine, into pigment cell granules . In Malpighian tubules, involved in guanine uptake . Probably in association with w/white, involved in aging-induced intestinal stem cell proliferation in the midgut by regulating tetrahydrofolate transport .
Catalytic Activity: ATP + guanine(out) + H2O = ADP + guanine(in) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75943
Sequence Length: 675
Subcellular Location: Membrane
EC: 7.6.2.-
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Q5VW32 | MTHWFHRNPLKATAPVSFNYYGVVTGPSASKICNDLRSSRARLLELFTDLSCNPEMMKNAADSYFSLLQGFINSLDESTQESKLRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLPKLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLEPAYSAKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETKGPGPTVKPSGHLFFRKLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKANYGLVEPIPFEFPPTSVQWTPETLAAFDLTKRPKDDSTKPKPEEEVKPVKEPDIKPQKDTGCYIS | Function: Nuclear envelope-associated factor that is involved in the nuclear envelope ruptures during interphase (NERDI) repair, where it is locally recruited by CHMP5 and reduces cytoskeletal stress through its action on SYN2 to help reseal the ruptured membrane.
PTM: Farnesylation is required for nuclear envelope localization.
Location Topology: Lipid-anchor
Sequence Mass (Da): 46476
Sequence Length: 411
Subcellular Location: Nucleus membrane
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A4IIL4 | MTHWFHRNPLKATAPVSFNFYGVASTQAASKICSDLRSTRARLLELFSDITCNHEMMKNATDAYFSLLLGFIDSLDGGTQDNKLRYIQNFKWTDTLQGNAPSAQQDAVFELVSMGFNVALWYTKYASRLAGKEDITEEEAKEVHRSLKIAAGVFKHLKENHIPKLITPVEKGRDLETRVIDAYTVQCQAEAQEVTIARAIELKHNPGLIAALAYETANYYQKVDHTLATLDPVYIAKWRSYTQLKMCFYMAYSYCYHGQTLLSADKCGEAIRSLQEAEKFYGKAEALCKEYGETKGPGTTAKPSGHLFFRKMGTLVRNTLEKCQRENGFIYFQKVPPEAPQLELKANYGLVEPVPFEFPAMTSQWSPETHTGFDLTKRPKDDSAKPKKEEEVKPMKEPDIKPQKDSGCQIS | Function: Nuclear envelope-associated factor that is involved in the nuclear envelope ruptures during interphase (NERDI) repair.
PTM: Farnesylation is required for nuclear envelope localization.
Location Topology: Lipid-anchor
Sequence Mass (Da): 46510
Sequence Length: 411
Subcellular Location: Nucleus membrane
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F4I7Y4 | MGCCQSSFLKPSSLHDKKITSDDLSGRRGKGAKRGNRHRHANINEGRGWHFSDVPDFSEFSASVLRDATNNFNKNAVVSVCSDQEPNLVYQGCIRSDKDKRLIAVKKFSKTTWPDPKQFATEARAIGSLRHVRLVNLIGYCCEGDERLLVSEYMPNESLTKHLFHWEKQTMEWAMRLRVALYVAEALEYCRQSGLKLYHDLNTCRVLFDENGSPRLSCFGWMKNSKDGKNFSTNLAYTPPEYLRSGTLIPESVVFSFGTFLLDLLSGKHIPPSHAVGTIQKQNLNVLMDSHLEGNYPEEDAAMVFDLASKCLHNNPNERPEIGDIISVITTLQQKLDVPSYTMLGISKLEKLEMEHPKSLIYDACHQMDLAALHQILEAMEYKEDEVTCELSFQQWAQQIKDVCNTRQQGDSAFRNKHFESAIDKYTQFIEIGIMISPTVYARRSMCYLFCDQPDAALRDAMQAQCVYSDWPTAFYLQAVALSKLNMVEDSATMLKEALILEDKRGS | Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1.
PTM: Phosphorylated by BRI1, ASK7/BIN2 and ASK9/BIL2.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 57611
Sequence Length: 507
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q7XJT7 | MGCCYSLSSTVDPVQDHTTDASSEPRNGGGEDPPLTKFSFSALKTATNHFSPENIVSDQTSDVVFKGRLQNGGFVAIKRFNNMAWSDPKLFLEEAQRVGKLRHKRLVNLIGYCCDGDKRFLVADFMANDTLAKRLFQRKYQTMDWSIRLRVAYFVAEALDYCNTAGFASYNNLSAYKVLFDEDGDACLSCFGLMKEINNDQITTGSVNPENVIYRFGTVLVNLLSGKQIPPSHAPEMIHRKNVFKLMDPYLKGKFSIDEANVVYKLASQCLKYEGQESPNTKEIVATLETLQTRTEAPSYEVVEMTNQEKDASSSSNLSPLGEACLRMDLASIHSILVLAGYDDDKDIIELSFEEWIQEVKELQDVRRNGDRAFVEQDFKTAIACYSQFVEERSLVYPSVYARRSLSYLFCDEPEKALLDGMHAQGVFPDWPTAFYLQSVALAKLDMNTDSADTLKEAALLEVKK | Function: Probable inactive protein kinase that activates the YODA MAP kinase cascade, which regulates the asymmetric first division and embryo polarity, by promoting the elongation of the zygote and the development of its basal daughter cell into the extra-embryonic suspensor. Acts as an adapter at the plasma membrane, possibly by recruiting and binding an activator.
PTM: Diacylation-mediated membrane association is essential for BSK12 function.
Location Topology: Lipid-anchor
Sequence Mass (Da): 52281
Sequence Length: 465
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cell membrane
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Q336V9 | MGCCGSSLRVGSHAPEKPPRRARPPPPPPQPHHPRRPSFTLNAHQAAASSSAASAAPAPAFAEFSLAELREATGGFAAANIVSESGEKAPNLVYRGRLQGAGGGGRAIAVKKFGKLAWPDPKQFAEEARGVGKLRHRRMANLIGYCCDGDERLLVAEFMPNDTLAKHLFHWENKAIEWAMRLRVAYNIAEALEYCSNEERPLYHDLNAYRVLFDENGDPRLSCFGLMKNSRDGKSYSTNLAYTPPEYLRNGRVTLESVVFSFGTILIDLLSGKRIPPTLALDMIRSRSIQAIMETNLEGKYSIEEATTLVDLASKCLQYEPRDRPDIKKLVSILQPLQTKSEVPSYVMLGVPKPEEVPKAPPAPQHPLSPMGEACSRMDLTAIHQILVSTHYRDDEGTNELSFQEWTQQMRDMLDARKRGDFAFRDKNFKQAIDCYTQFVDVGTMVSPTVYARRSLCHLMCDQPDAALRDAMQAQCVYPDWPTAFYMQAVALSKLNMQSDSLDMLNEASQLEEKRQKSIKGP | Function: Probable serine/threonine kinase that functions as a positive regulator of plant immunity. May be involved in the regulation of pattern-triggered immunity (PTI). Does not seem to be involved in responses to brassinosteroid (BR) signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 58177
Sequence Length: 522
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q944A7 | MGCCQSLFSGDNPLGKDGVQPQPLSQNNHGGATTADNGGSGGASGVGGGGGGGGIPSFSEFSFADLKAATNNFSSDNIVSESGEKAPNLVYKGRLQNRRWIAVKKFTKMAWPEPKQFAEEAWGVGKLRHNRLANLIGYCCDGDERLLVAEFMPNDTLAKHLFHWENQTIEWAMRLRVGYYIAEALDYCSTEGRPLYHDLNAYRVLFDEDGDPRLSCFGLMKNSRDGKSYSTNLAYTPPEYLRNGRVTPESVTYSFGTVLLDLLSGKHIPPSHALDMIRGKNIILLMDSHLEGKFSTEEATVVVELASQCLQYEPRERPNTKDLVATLAPLQTKSDVPSYVMLGIKKQEEAPSTPQRPLSPLGEACSRMDLTAIHQILVMTHYRDDEGTNELSFQEWTQQMKDMLDARKRGDQSFREKDFKTAIDCYSQFIDVGTMVSPTVFGRRSLCYLLCDQPDAALRDAMQAQCVYPDWPTAFYMQSVALAKLNMNTDAADMLNEAAQLEEKRQRGGRGS | Function: Serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Mediates signal transduction from BRI1 by functioning as substrate of BRI1 . Functions as a positive regulator of plant immunity. May be involved in the regulation of pattern-triggered immunity (PTI) downstream of the flagellin receptor FLS2. Possesses kinase activity in vitro. Kinase activity is required for its function in innate immunity .
PTM: Phosphorylated at Ser-230 by BRI1 upon brassinolide (BL) treatment. Phosphorylation at Ser-230 weakens the interaction between BSK1 and BRI1 . Phosphorylated by ASK7/BIN2 and ASK9/BIL2 .
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 56818
Sequence Length: 512
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9LS26 | MGCLHSKTANLPSSDDPSAPNKPESVNGDQVDQEIQNFKEFELNELRKATNGFSPSCIVSEGGEKAPNVVYRGKLEGNHLVAIKRFSRQSWPDAQQFVVEATGVGKLRNKRIVSLIGCCAEGDERLLVAEYMPNDTLSKHLFHWEKQPLPWDMRVRIADYIAEALDYCNIENRKIYHDLNAYRILFDEEGDPRLSTFGLMKNSRDGKSYSTNLAYTPPEFLRTGRVIPESVIFSYGTILLDLLSGKHIPPSHALDIIRGKNALLLMDSSLEGQYANDDATKLVDLASKCLQSEAKDRPDTKFLLSAVAPLQKQEEVASHVLMGLPKNTVILPTMLSPLGKACAKMDLATFHDILLKTGYRDEEGAENELSFQEWTQQVQEMLNTKKFGDIAFRDKDFKNSIEYYSKLVGMMPVPSATVFARRAFSYLMTDQQELALRDAMQAQVCIPEWPTAFYLQALALSKLGMETDAQDMLNDGAAYDAKRQNSWRC | Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Mediates signal transduction from BRI1 by functioning as substrate of BRI1.
PTM: Phosphorylated by BRI1 upon brassinolide (BL) treatment.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54973
Sequence Length: 489
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q8W4L3 | MGGQCSSLSCCRNTSHKTAVLEAPDVDNGESSEITDVPNFREYTLEQLKAATSGFAVEYIVSEHGEKAPNVVYKGKLENQKKIAVKRFTRMAWPDSRQFLEEARSVGQLRSERMANLLGCCCEGDERLLVAEFMPNETLAKHLFHWETQPMKWTMRLRVVLYLAQALEYCTSKGRTLYHDLNAYRVLFDEECNPRLSTFGLMKNSRDGKSYSTNLAFTPPEYLRTGRITPESVIYSFGTLLLDLLSGKHIPPSHALDLIRDRNLQTLTDSCLDGQFSDSDGTELVRLASRCLQYEARERPNTKSLVTALTPLQKETEVLSHVLMGLPHSGSVSPLSPLGEACSRRDLTAMLEILEKLGYKDDEGVTNELSFHMWTDQMQESLNSKKKGDVAFRQKDFREAIECYTQFIDGGMISPTVCARRSLCYLMSDMPKEALDDAIQAQVISPVWHVASYLQSASLGILGMEKESQIALKEGSNLEAKMNGVPRVK | Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Mediates signal transduction from BRI1 by functioning as substrate of BRI1 . Functions redundantly with BSK4, BSK6, BSK7 and BSK8 .
PTM: Phosphorylated by BRI1 upon brassinolide (BL) treatment . Phosphorylated by ASK7/BIN2 and ASK9/BIL2 .
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54914
Sequence Length: 489
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q4WUK5 | MSGPNRTYSFGEGDDSLAHPSSRTHAMHSQYDDVSPISDGARMNPMNGQGMDHGLASVLEDGRQGWGRSPEPSPSLLTGSSATPGMDNLGPGAVGGGISGIALSVANSHDRLSGVEALMGTDGQEANIPAERGLSTTGSDNPYVPEPPEHRYSYGSNIALGAAAAPAGQLTPGQSVSHLSSTNPSQRNLYDIPYQDVGGLNAGPYQRHSAYSSNDLPVDINPDEIVDDGDDGFVPAPNSGSGARKSQAIPAAAGGAAAGGVLGNLGGLFGGKSAADTSYGPVPGAGLEAGEKGRWVKPKPGGGNKKRGWIVGAILAFIIIGAIVGGAVGGTIGHRGNEEPSSASSASSSSTQTATEDTSVNGDLDKNSAEIKALMNNKNLHKVFPGIDYTPWGVQYPLCLKYPPSQNNVTRDMAVLTQLTNNVRLYGTDCNQTEMVLHAIDKLEIKDMKIWLGVWIDSNETTSRRQIDQLYKIIDDAKDISIFNGAIVGNEALYRAGSDKTSAQTTLINYMQEVKDHFKKKNIDLPVATSDLGDNWDATLVQAADVVMANVHPFFGGIPVDQAAAWTWRFWQDHNVALTKGTNKKQIISEVGWPSGGGNDCGQGANCPNDTAGAVAGVDELNKFMEDWVCQALDNGTDYFWFEAFDEPWKIVYNTGKENWEDKWGLMDSARNLKPGLKIPDCGGKTAT | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan (By similarity).
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 72696
Sequence Length: 688
Subcellular Location: Cell membrane
EC: 3.2.1.39
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A2QN74 | MAGVNRSFSYSRGDDALLRDDEREISPLRSAEDGLYSTSYGDVSPLSAGVQAQNRPFDRGLVSVPEGQTLERHMTSTPGMDNLGPASVGGGISGIALGVANSHNRQSGVDAFRETDVPVRNLPAERDFNTTGSDNPYIPAPPDGDIYPSSEAVRYRDSYSSHTGLGAGAPFAEHSTPGTTPSQRSFFDSPYQGVDAGPYQRHSAYSSHDYPLVINPDDIADDGDDGFPVHPKGAADYRSNANVPGTGVAGAAAAGGFLGKFRALFKREEPSPFYDSDIGGGLGGAEKAQGGRHIIGGGSRKRGWIVGLILAAVIVAAIVGGAVGGILGHQEHDGDTSSSSSSSSSSGTGSGGSDKGDGLLDKDSDEIKALMNNKNLHKVFPGVDYTPWGVQYPLCLQYPPSQNNVTRDLAVLTQLTNTIRLYGTDCNQTEMVLEAIDRLQLTNMKLWLGVWIDTNTTTTDRQISQLYKIVENANDTSIFKGAIVGNEALYRAGSDVASAETNLIGYINDVKDHFKDKNIDLPVGTSDLGDNWNAQLVSAADFVMSNIHPFFGGVEIDDAASWTWTFWQTHDTPLTAGTNKQQIISEVGWPTGGGNDCGSDNKCQNDKQGAVAGIDELNQFLSEWVCQALDNGTEYFWFEAFDEPWKVQYNTPGQEWEDKWGLMDSARNLKPGVKIPDCGGKTIT | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan (By similarity).
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 73248
Sequence Length: 684
Subcellular Location: Cell membrane
EC: 3.2.1.39
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Q5B430 | MGDRSEQYGDIPPISSQHRMHGYGNNGEPAAMPGDGQQNWGSGPGIAHTHSMRTASTATPGMDNLGPSAVGGGISGIALGVANTHDRQSGIDAFRDADATLGYIPAERGYHTTGADNPYVPSPPSVGPGPDESSEGLRSHETFGSSAALSAAGAPAGNWTPPSGSRHSFLDGSYQGVASGPYQRHSAYSSQDYPADINPDDILDDGDDGFAAAPSNKPNAAGGAATGGAAGGLLGEFFGAKKAADASYDPVPGAGLPSVEKYAKPRPSGASRKRGWIIGGILAFIVIGAIVGGAVGGTLGNRRSETASESSEVSADDDTETNGDLDKNSDEIKSLMAMEGLHKVFPGMDYTPWGVQHPECDKWPPSQNNVTRDMAVLSRLTNTVRLYGTDCNQTEMVLHAIDRLELTDMKLWLGVWIDTNTTTNERQLSQLYDILDKRSDHSVFKGAIIGNEALYRAGSTKEEARKNIIDYMRQVRKHFNDHNIDIKVATSDLGDNWDETLADATDVVMSNVHPFFGGVEVSKAAGWTWSFWNSHNAPLTQGTNKGNIIAEVGWPSGGGNDCGDGANCKDDTSGAVAGVKQMNQFMADWVCPALENGTDYFWFEAFDEPWKVKFNKGDEQWEDKWGLMDPGRNLKPGIEIPDCGGKTAA | Function: Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan.
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 68963
Sequence Length: 649
Subcellular Location: Cell membrane
EC: 3.2.1.39
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B0Y9Q9 | MRGAILATAAALAGTAMADVAHMRRHGHDSFHQRRSPLAEADATCGCTTEVVTVWGPPTLIPVASPTPSTVTSEAVTTLHSTSTTTVTVIASASTPAASPSPATDKVPLPTPAITNFPSTGVYTIPATTVTVFDTTTVCGATTTELPAGTHTYGGVTTVVETATTVVCPYATVEPSGTTVTSVIKTTTYVCPSAGTYTIAPTTTTVPTSTVIVYPTPAVITPGTYTQPEQTVTVTRTDYTYVCPFTGQDEPTSAPAAPSTTAVPATTTAAPETTTAAPDTTTAVPSTSSAAPSSSSTAPASTGAVSGQMGMTYTPYTKGGDCKDKSSVLSEVAALKSKGFTHVRVYSTDCNSLEYIGEAARTSGLQMIIGVFISSTGVSGAQDQVTAISKWAQWDLVSLIVVGNEAIQNGYCDASTLAGFISSAKSAFQAAGYTGKVTTTEPINVWQAHGSTLCGVCDIVGANIHPFFNADVSADQAGKFVAQEIKVLESICPGKDVLNLETGWPHAGNANGKAVPGTSEQAIAIKSIADEVGSKSVFFSYFDDLWKEPGQFGVERYWGCFDTFN | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 58148
Sequence Length: 565
Pathway: Glycan metabolism; cellulose degradation.
Subcellular Location: Secreted
EC: 3.2.1.21
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Q5BD29 | MRGAILATAAAFAGTAVADMHMRRHAHEGLHHRALHASSAVPEEECGCTTEVITYWGEPTTIPLSVPTSTVTSETTETVHSTSYSTVTVTATSSAAPVETPSETPSPTPEVTLPTAGVTSYSETGTYTIPATTITVTDTTTVCGATTTELPSGTHTYGGVTTIVETATTITCPYATVKPTGSTVTSVIETTTYVCPSAGTYTIAPTTTFVPTSTVVVYPTPETVTPGTYTNPGTTITVTRTEDVYVCPYTNGNVPTSVPALPTTSAASTTTAVPSSSTTTSSATSVPTGASGNKMGMTFTPYNNDGSCMAKNDVLEQVGLIKGKGFSHVRVYGTDCHTLEYVGAACSTHGLKMILGVNVEGSTGFDGARSQFKDITNWGQWDLVSLIVVGNEVVTSNIASAAQLASFVSEGASAFSAAGYTGQVTTAEPIDVWLSNGATLCPVVDILGANLHPFFNPEFTAAEAGTLVSNQIKDLKQVCTGKDVINLETGWPNAGSANGKAIPGQSQQTTAIKSLVEKVGDVSVFFSYADDGWKSKFATSDKYNVEQHWGCIDQF | Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Mass (Da): 57672
Sequence Length: 555
Pathway: Glycan metabolism; cellulose degradation.
Subcellular Location: Secreted
EC: 3.2.1.21
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P08630 | MMGTKHRNSHVNGSIKSSSSLRSSSKSFQAKMDLMSERLYDVVKSGSMVKRAQNKKRFTPVNYKHRWFELTKRTFSYFDVENVERRRERGRIHLKGVRLVEEATVSGEGGDPFAPDGYPFQVGYCEISASANSHQLENGNGGGSGVGIEGQQSGRAVPQYTLYVIANSEKERSEWIRAIRQVCEDSNTPKSYRYHPGLWSGKKWSCCKGLSRTTFGCRAAAHWREANNNPSNGSSPAQNSTRSISPNSSTTNSQFSLQHNSSGSLGGGVGGGLGGGGSLGLGGGGGGGGSCTPTSLQPQSSLTTFKQSPTLLNGNGTLLDANMPGGIPTPGTPNSKAKDNSHFVKLVVALYPFKAIEGGDLSLEKNAEYEVIDDSQEHWWKVKDALGNVGYIPSNYVKPKALLGLERYEWYVGDMSRQRAESLLKQGDKEGCFVVRKSSTKGLYTLSLHTKVPQSHVKHYHIKQNARCEYYLSEKHCCETIPDLINYHRHNSGGLACRLKSSPCDRPVPPTAGLSHDKWEIHPMELMLMEELGSGQFGVVRRGKWRGSIDTAVKMMKEGTMSEDDFIEEAKVMTKLQHPNLVQLYGVCSKHRPIYIVTEYMKHGSLLNYLRRHEKTLIGNMGLLLDMCIQVSKGMTYLERHNYIHRDLAARNCLVGSENVVKVADFGLARYVLDDQYTSSGGTKFPIKWAPPEVLNYTRFSSKSDVWAYGVLMWEIFTCGKMPYGRLKNTEVVERVQRGIILEKPKSCAKEIYDVMKLCWSHGPEERPAFRVLMDQLALVAQTLTD | Cofactor: Binds 1 zinc ion per subunit.
Function: Required for proper ring canal development. Also required for the development of male genitalia and for adult survival.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 87392
Sequence Length: 786
EC: 2.7.10.2
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Q8JH64 | MASIILESIFLKRSQQKKKTSPLNFKKRLFLLTESKLSYYEYDFERGRRGSKKGSVDIEKITCVETVVPENNPPPERQVPKKGEDYNMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKSVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCKILESRNGSLKAGRSHRKTKKPLPPTPEEDTMVMKPLPPEPAPSAAGEMKKVVALYNYVPMNVQDLQLQKGEDYLILEESHLPWWKARDKNGREGYIPSNYVTATSNSLEIYEWYSKNITRSQAEQLLKQEGKEGGFIVRDSTSKTGKYTVSVYAKSAVDPQGMIRHYVVCCTPQNQYYLAEKHLFNTIPELITYHQHNSAGLISRLKYPVSRHQKSAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYNVAIKMIREGSMSEDEFIDEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNFLRETQRRFQPAELLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGIVKVSDFGLSRYVLDDEYTSSMGSKFPVRWSPPEVLLYSKFSSKSDVWSFGVLMWEVYSLGKMPYERFNNSETTEHVIQGLRLYRPQQASERVYAIMYSCWHEKAEERPTFSALLGSIVDITDEEP | Cofactor: Binds 1 zinc ion per subunit.
Function: Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling . Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation (By similarity). After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members (By similarity). PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK (By similarity). BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways (By similarity). Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway (By similarity). The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense (By similarity). Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells (By similarity). Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation (By similarity). BTK also plays a critical role in transcription regulation (By similarity). Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes . BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B (By similarity). Acts as an activator of NLRP3 inflammasome assembly by mediating phosphorylation of NLRP3 (By similarity). Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR (By similarity). GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression (By similarity). ARID3A and NFAT are other transcriptional target of BTK (By similarity). BTK is required for the formation of functional ARID3A DNA-binding complexes (By similarity). There is however no evidence that BTK itself binds directly to DNA (By similarity). BTK has a dual role in the regulation of apoptosis (By similarity).
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
PTM: Following B-cell receptor (BCR) engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-549 by LYN and SYK. Phosphorylation at Tyr-549 is followed by autophosphorylation of Tyr-220 which may create a docking site for a SH2 containing protein (By similarity). Phosphorylation at Ser-179 by PRKCB, leads in translocation of BTK back to the cytoplasmic fraction (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75879
Sequence Length: 657
Domain: The PH domain mediates the binding to inositol polyphosphate and phosphoinositides, leading to its targeting to the plasma membrane (By similarity). It is extended in the BTK kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain.
Subcellular Location: Cytoplasm
EC: 2.7.10.2
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Q06187 | MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPAAAPVSTSELKKVVALYDYMPMNANDLQLRKGDEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGDPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSQQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNILDVMDEES | Cofactor: Binds 1 zinc ion per subunit.
Function: Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling . Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation . After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members . PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK . BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways . Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway . The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense . Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells . Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation . BTK also plays a critical role in transcription regulation . Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes . BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B . Acts as an activator of NLRP3 inflammasome assembly by mediating phosphorylation of NLRP3 . Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR . GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression . ARID3A and NFAT are other transcriptional target of BTK . BTK is required for the formation of functional ARID3A DNA-binding complexes . There is however no evidence that BTK itself binds directly to DNA . BTK has a dual role in the regulation of apoptosis .
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
PTM: Following B-cell receptor (BCR) engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-551 by LYN and SYK. Phosphorylation at Tyr-551 is followed by autophosphorylation of Tyr-223 which may create a docking site for a SH2 containing protein. Phosphorylation at Ser-180 by PRKCB, leads in translocation of BTK back to the cytoplasmic fraction. Phosphorylation at Ser-21 and Ser-115 creates a binding site for PIN1 at these Ser-Pro motifs, and promotes it's recruitment.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76281
Sequence Length: 659
Domain: The PH domain mediates the binding to inositol polyphosphate and phosphoinositides, leading to its targeting to the plasma membrane. It is extended in the BTK kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain.
Subcellular Location: Cytoplasm
EC: 2.7.10.2
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Q05619 | MSYKLLIINPGSTSTKIGVYEGEKELFEETLRHTNEEIKRYDTIYDQFEFRKEVILNVLKEKNFDIKTLSAIVGRGGMLRPVEGGTYAVNDAMVEDLKVGVQGPHASNLGGIIAKSIGDELNIPSFIVDPVVTDELADVARLSGVPELPRKSKFHALNQKAVAKRYGKESGQGYENLNLVVVHMGGGVSVGAHNHGKVVDVNNALDGDGPFSPERAGSVPIGDLVKMCFSGKYSEAEVYGKAVGKGGFVGYLNTNDVKGVIDKMEEGDKECESIYKAFVYQISKAIGEMSVVLEGKVDQIIFTGGIAYSPTLVPDLKAKVEWIAPVTVYPGEDELLALAQGAIRVLDGEEQAKVY | Function: Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate.
Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 38434
Sequence Length: 355
Pathway: Lipid metabolism; butanoate metabolism.
Subcellular Location: Cytoplasm
EC: 2.7.2.7
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Q9RVA9 | MSMIAHVINPGISGVKLACAVIEPGQNPAFPSHLQVSLTREELPLEAAPDELGLDALAERILEQTAAWPAPDAVVGRGGLMGRVPAGTYHVTPELARYVLENVSGSQPADDPNPGIGAPLALRVAQARGVPAYIVDPQSVDELLPEAHMTGVPGVRREARFHALNARAVARRAAYEVGKQFREARVVVAHLGVTTSVTAFDQGRAIDTTGTAPDGGPMGARQSGPLPTRAVIRLLQTQSESELLRLLTRGSGFFALTGTADLSEIERRQEQGEDSVVQTAIAAFVHQVCKAIGEQTAALPGRPDAVALTGGIARWDAVVDRIERRLAWVAPFIVLPGELELEALAEGAGRVLLGLEGVREWTPEGVTLRPAAPLVQVETVEEV | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 40533
Sequence Length: 383
Subcellular Location: Cytoplasm
EC: 2.7.2.7
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B2KEH0 | MEHNILVINPGSTSDDIGYYKGPKTVFEESARYSQEELDSFAGKELSEQIPLRRKFLLDVLKKHEINLNEIDAVIGRGGLLKHIEGGIYTINEAMLADLKRGYNGHHPSNLGGILAREIAESLGKPCFIADPVVVDEMEPLARYTGFKEIKRKSIFHALNQKRVAITAAKELGKKYKECNFIVMHGGGGVSVGAHKKGKVIDVSDGFEGAGPMTPQRSGVLPSLELVEMCFSGQYTIQELRKKMRGRGGMIAHTGTSDIADLYNYISSGKKKPGSTINCSREAAQEAFDAMIYQISKEIGAMATVLKGDVDAIILTGGLAYNEYLVNMIKERTGFITDKFFVYPGGDEKAALKEAAARALENPEIIKQYK | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 40599
Sequence Length: 370
Subcellular Location: Cytoplasm
EC: 2.7.2.7
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Q9RPS7 | METVLVINPGSTSTKLALFANHDCLAEETLRHSVQELAPFENVVSQTSFRKQMIAEFLETHNIIQLAAVVGRGGLLKPIPGGTYLVDQQMLEDLRTERFNTHASNLGAILANEFAEKYHVPAFIVDPVVVDELQPLARISGLKGIQRRSVGHALNQKAVARKIAEDLGKTYEQSNFIVVHLGGGISLGAHQKGRMVDVVNGLDGEGPYTPERSGALPLVEFAQWILEQELTISQVKKLIAGNSGLKSYLGETDLRHIQAQIAAGDQTANYYLKGMCYQIAKSIGEMAVVLEGTIDAIILTGGAAYSQTVVQEISQKVTWIAPIKVYPGEMEMAALYEGVNRVLTGEEQALNYSEAKIEQE | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 39256
Sequence Length: 360
Subcellular Location: Cytoplasm
EC: 2.7.2.7
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P54621 | MQEQKFRILTINPGSTSTKIGVFENERAIVEKTIRHEGRCFGNIKR | Catalytic Activity: ATP + butanoate = ADP + butanoyl phosphate
Sequence Mass (Da): 5334
Sequence Length: 46
Subcellular Location: Cytoplasm
EC: 2.7.2.7
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I1RV18 | MSWKAIAKAAQAEVLDAIPTKWKLDPAKYRTLTDVTSVPRECGILSDAQLSITDLTALEVVKRIESRELTAVQALEAFGARTAIAHQLVNCLMDWFYEDGLRQAEELDKSFKATGKLKGPLHGVPVALKDFHFVAGRPTTTGYVSRRDFRPEHDSALVKTLRDAGAVFYCKTTMPQSGMAIETVSNLWGRTLNPYNTALSAGGSSGGDAVLVALKGTPITPSTDLGGSIRVPAAFNGLYAIRPTSDRIPKGGMDNINSGQISIKLSCGPICHSMEDLESFTKLINAYPENQNDPTSVPVPWKTVKPIEGKLTIGLMKWDKVVMPHPPVIRALEHTKRTLEKAGHEVVEFDVPFDCWDAIQTTFDTYYQSGHSGTLSTLEATGEPLIPAFEDLIKVFGSKEISAAESQQLNVKARIFREKFRDAWDATTKLTSTGRPVDALICPTAPAVGYPHDFNVYWGYTSLFNLLDYPSVILPVANFKVNPQDDPVASNYKPLETNPYDKPNHELYKPELFSSQPSTIQVVGRPFQDEELIKVSSVMDDLLRAM | Function: Amidase; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid intermediate (Probable). The predicted function of the NADH:flavin oxidoreductase FG08077, the cytochrome P450 monooxygenase FG08079, the decarboxylase FG08083, and the putative acetyltransferase FG08082 are consistent with this pathway, however, the respective activities of the butelonide biosynthesis cluster enzymes have still to be experimentally determined (Probable).
Sequence Mass (Da): 60107
Sequence Length: 546
Pathway: Mycotoxin biosynthesis.
EC: 3.5.1.-
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I1RV19 | MAMFTVLPLIWLAPLGLISLFFYYIIPYFWNYRHLRSIPGPLFARLSNWWLVYACREKSRWKYVNDAHTRYGPVVRIQPNHVSIANEEVINAIYGHGNGMLKSSFYDASVITTYSIFTSRDRAEHSRKRKVVSHSFAPQSMRNFEPFIQQHLNVFLQKWDAMAANEAKFDGYADVESRVWLNYLVLDIIGDLAFGAPFGVLAKGSEVVDFETEKGPSSLPVITSLSTRSEIAATVGALPELKPYLKWSPDPFFRTGFNGMINLRTLGTSRITDRLNNPPGDEREKDLLERVREGRDHKGQPFGKGELIAEALTVLIAGTDTTSSTMAALLYHVVRTPGVLKKLQAELDEAIPADVSIPSFEMVKNLKYLGFVVNEALRHHSTISLGLPRLVPENGNGVTIAGYHFAPGTVLSIPIYTVHHLKEVWGPDADEFKPERWEDVTQRQKQAFIPFSHGPRACLGRNLAEMELKVITATWARRYDLIMRDDTMEILEGLARKPEAVNVGIRRRM | Function: Cytochrome P450 monooxygenase FG08079; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid intermediate (Probable). The predicted function of the NADH:flavin oxidoreductase FG08077, the cytochrome P450 monooxygenase FG08079, the decarboxylase FG08083, and the putative acetyltransferase FG08082 are consistent with this pathway, however, the respective activities of the butelonide biosynthesis cluster enzymes have still to be experimentally determined (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57604
Sequence Length: 509
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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I1RV21 | MTASSRPAEYRDVRTANLNTITFDNLFDKDEAELKRLIESCEKDGFFYLDLKSAASQKFWNDLYTIDSTTKDWFKQPIEKKLQTPTVSLAHGFKAVGNQSGSIESKKDGFEALKIGKSELDGRWALPDVVSDNLPLFDQFASSCHFISKLLLDCLSDGLNLKGDARFETHHRDDCRSKSTLYFLHYPPGAQDPNKVGQNMHTDIGTLTILYAPQWGLQVFSPADGAWEYVEPRPNQIIVNVGDTLRFLSGKRFKSALHRVLPLGGIQIEDRYSISYFLRASDSTEFKDSDEDESNAKQWYTKKYAMYEMPHVIQKQQTTLSGGMAQELQATF | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid intermediate (Probable). The predicted function of the NADH:flavin oxidoreductase FG08077, the cytochrome P450 monooxygenase FG08079, the decarboxylase FG08083, and the putative acetyltransferase FG08082 are consistent with this pathway, however, the respective activities of the butelonide biosynthesis cluster enzymes have still to be experimentally determined (Probable).
Sequence Mass (Da): 37686
Sequence Length: 332
Pathway: Mycotoxin biosynthesis.
EC: 1.14.-.-
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I1RV22 | MINITKPQNWTRGDYLVSTDPALLQVDAINAALSSDMVWWAGDLPADALWDALRSSICFGLYRKRSSEMNGTGPTVEYKIEEWEQVGLVRMITDGVTFGYLTDVYILPEHQGGGRGRWMLQILNEALQGWPHLRRVMLLTTDKMHLFGKNLGMKDYREFDGMKGVSIAMVEGPGAQH | Function: Putative acetyltransferase; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid intermediate (Probable). The predicted function of the NADH:flavin oxidoreductase FG08077, the cytochrome P450 monooxygenase FG08079, the decarboxylase FG08083, and the putative acetyltransferase FG08082 are consistent with this pathway, however, the respective activities of the butelonide biosynthesis cluster enzymes have still to be experimentally determined (Probable).
Sequence Mass (Da): 19949
Sequence Length: 177
Pathway: Mycotoxin biosynthesis.
EC: 2.3.1.-
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I1RV23 | MDNGLSRRHEISELLQLVDSTTTRAFHTSNGSPKSDCRNDSKPLKRYEELFGSFPAEGLGTSGFKDAIDLISRNSVDNASPGFLGKLVSAPSAPGIASDLFLSILNNNGHVQRAGPALTAIEKHTSLELARLFDLQGPHAGGVTVPGGAAGNLMAMLVARNIVAPESKQRGLTPGEYAIFVSDAAHYSVSNSANVIGLGNDSIIRVPALDDGTMDADALQRAVDQAGKDGKKPLLIAATSGSTVNGAFDPLDKIGEIAHRVGAWFHVDACWGGGVVFSDKLKHLMKGSHLADSIAFNPHKLLGVPLVCAFLLVNDLRTLWLANKLNAGYLFHDDAPKKNGVSSEQSANTNGSEKESWRHSKLLDTAPDVMKINDLASLTIQCSRRHDATKMFLHWLYYGTAGIAREVEQAVDSAKHLACLVRDHPRFELIWDPEQVFAQVCFYWKSASTPEKSGETLAEINSRNTRALFQGIEEMGWKVDFAPGKAKGEFLRIACNRLTTRQTVEKIVSELVELGESLGL | Function: Glutamate decarboxylase-like protein; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat . Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid intermediate (Probable). The predicted function of the NADH:flavin oxidoreductase FG08077, the cytochrome P450 monooxygenase FG08079, the decarboxylase FG08083, and the putative acetyltransferase FG08082 are consistent with this pathway, however, the respective activities of the butelonide biosynthesis cluster enzymes have still to be experimentally determined (Probable).
Sequence Mass (Da): 56206
Sequence Length: 520
Pathway: Mycotoxin biosynthesis.
EC: 4.1.1.-
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I1RV24 | MPPQQEQDTDSDAIRSYNEESKSETPGCIPDAMLSSDETSNDVASDISPPPDGGWNAWLCTLCGHFLFMNTWGFINSFGIFQTYYTTFLDRDPSDISWIGSIQVFLSFFVGAFVGRYIDSGHLRLVLSCGTILVLIGIFTASLSTQYWQLILSQGICCGLGNGFLVTPAVSVTSTYFAKRRSLAIGISTCGSVTGALVFNSMARQLLPTAGFGWTMRAIGFVQAATLLFVVVAMKTRLPPTKSGRLVEWVAFKQLDYTFFTIGMFFNFWAVFFGYYYIAPYSRDIITPTLTYTQSLNLLLILNGVGVFGRMIANHYADTFGPLELLIPTCLVAAVATFSWIAVDTPTHAYVWTVFYGIIGGSILSLFPAGISCLTTDLSTRGAYIGMNFTVISFATLTGNPIAGAIITAMQGRYYGAQAFMGSSFIVGTAFIVAAKMNHVK | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48062
Sequence Length: 441
Subcellular Location: Membrane
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Q5HJP2 | MTNNKVALVTGGAQGIGFKIAERLVEDGFKVAVVDFNEEGAKAAALKLSSDGTKAIAIKADVSNRDDVFNAVRQTAAQFGDFHVMVNNAGLGPTTPIDTITEEQFKTVYGVNVAGVLWGIQAAHEQFKKFNHGGKIINATSQAGVEGNPGLSLYCSTKFAVRGLTQVAAQDLASEGITVNAFAPGIVQTPMMESIAVATAEEAGKPEAWGWEQFTSQIALGRVSQPEDVSNVVSFLAGKDSDYITGQTIIVDGGMRFR | Function: Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH.
Catalytic Activity: (S)-acetoin + NAD(+) = diacetyl + H(+) + NADH
Sequence Mass (Da): 27216
Sequence Length: 258
EC: 1.1.1.304
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Q8CQD2 | MSKTAIITGAAGGLGKGIAERLANDGFNIVLQDINEALLLETEKEFKEKGYQAVAYKSDVSKKKEQEELVQFAVTEFGQLDVMVNNAGVDAVTPILEIGEEELSKLFNINVFGTLFGIQAAANQFIKQKSKGKIINACSIAGHESYEVLGTYSATKHSVRSFTQTAAKELADKGITVNAYCPGVAKTEMWDRIDEEMVKLDDSLEIGDAFEAFSSEIKLGRYQEPSDVANLVSFLASNDSDYITGQSILTDGGLVYR | Function: Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH.
Catalytic Activity: (S)-acetoin + NAD(+) = diacetyl + H(+) + NADH
Sequence Mass (Da): 27917
Sequence Length: 257
EC: 1.1.1.304
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P56685 | SIVPIRCRSNRDCRRFCGFRGGRCTYARQCLCGY | Function: Active against both Gram-positive and Gram-negative bacteria.
PTM: Contains three disulfide bonds.
Sequence Mass (Da): 3975
Sequence Length: 34
Subcellular Location: Secreted
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Q8S307 | MTSDGATSTSAAAAAAAAAAARRKPSWRERENNRRRERRRRAVAAKIYTGLRAQGDYNLPKHCDNNEVLKALCVEAGWVVEEDGTTYRKGCKPLPGEIAGTSSRVTPYSSQNQSPLSSAFQSPIPSYQVSPSSSSFPSPSRGEPNNNMSSTFFPFLRNGGIPSSLPSLRISNSCPVTPPVSSPTSKNPKPLPNWESIAKQSMAIAKQSMASFNYPFYAVSAPASPTHRHQFHTPATIPECDESDSSTVDSGHWISFQKFAQQQPFSASMVPTSPTFNLVKPAPQQMSPNTAAFQEIGQSSEFKFENSQVKPWEGERIHDVGMEDLELTLGNGKARG | Function: Transcriptional repressor that binds to the brassinosteroid (BR) response element (BRRE) 5'-CGTG(T/C)G-3' in gene promoter. Regulates positively the brassinosteroid-signaling pathway . Mediates downstream growth responses and negative feedback regulation of brassinosteroid biosynthesis. Promotes growth. Modulates ovule initiation and development by monitoring the expression of genes related to ovule development (e.g. HLL, ANT, and AP2). Regulates negatively the abscisic acid (ABA) signaling pathway during the post-germination stage .
PTM: Phosphorylated by BIN2 and MKK5 in response to brassinosteroid (BR). Dephosphorylation level is consistent with ovule and seed number.
Sequence Mass (Da): 36486
Sequence Length: 336
Subcellular Location: Nucleus
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B8B7S5 | MTSGAAAAGRTPTWKERENNKRRERRRRAIAAKIFTGLRALGNYNLPKHCDNNEVLKALCREAGWVVEDDGTTYRKGCKPPPSSAGGASVGMSPCSSTQLLSAPSSSFPSPVPSYHASPASSSFPSPSRIDNPSASCLLPFLRGLPNLPPLRVSSSAPVTPPLSSPTASRPPKIRKPDWDVDPFRHPFFAVSAPASPTRGRRLEHPDTIPECDESDVSTVDSGRWISFQMATTAPTSPTYNLVNPGASTSNSMEIEGTAGRGGAEFEFDKGRVTPWEGERIHEVAAEELELTLGVGAK | Function: Positive brassinosteroid-signaling protein. Mediates downstream brassinosteroid-regulated growth response and feedback inhibition of brassinosteroid biosynthetic genes. May act as transcriptional repressor by binding the brassinosteroid-response element (5'-CGTGCG-3') in the promoter of GRAS32 (AC Q9LWU9), another positive regulator of brassinosteroid signaling (By similarity).
PTM: Dephosphorylation after treatment with epibrassinolide.
Sequence Mass (Da): 31909
Sequence Length: 298
Subcellular Location: Nucleus
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Q9LN63 | MTSDGATSTSAAAAAAAMATRRKPSWRERENNRRRERRRRAVAAKIYTGLRAQGNYNLPKHCDNNEVLKALCSEAGWVVEEDGTTYRKGHKPLPGDMAGSSSRATPYSSHNQSPLSSTFDSPILSYQVSPSSSSFPSPSRVGDPHNISTIFPFLRNGGIPSSLPPLRISNSAPVTPPVSSPTSRNPKPLPTWESFTKQSMSMAAKQSMTSLNYPFYAVSAPASPTHHRQFHAPATIPECDESDSSTVDSGHWISFQKFAQQQPFSASMVPTSPTFNLVKPAPQQLSPNTAAIQEIGQSSEFKFENSQVKPWEGERIHDVAMEDLELTLGNGKAHS | Function: Positive regulator of brassinosteroid (BR) signaling. Transcription factor that activates target gene expression by binding specifically to the DNA sequence 5'-CANNTG-3'(E box) through its N-terminal domain. Can bind individually to the promoter as a homodimer or synergistically as a heterodimer with BIM1, BIM2 or BIM3. The C-terminal domain is probably involved in transcriptional activation . Recruits the transcription elongation factor IWS1 to control BR-regulated gene expression . Forms a trimeric complex with IWS1 and ASHH2/SDG8 to regulate BR-regulated gene expression . Promotes quiescent center (QC) self-renewal by cell divisions in the primary root. Binds to the E-boxes of the BRAVO promoter to repress its expression .
PTM: Phosphorylated by ASK7/BIN2. Phosphorylation increases protein degradation and/or interferes with the nuclear localization.
Sequence Mass (Da): 36486
Sequence Length: 335
Domain: The central part (140-272) is important for interaction with MYB30.
Subcellular Location: Nucleus
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O44220 | MWKFAIHSQQPFCWQQLCNRRHLYVGNVQQQTHLELLDAAPTRSDDEWLQAKPYEKVPGPGTWQVLSYFLPGGKQYNTNLIQMNRRMREWYGDIYRFPGLMGKQDVIFTYNPNDFELTYRNEGVWPIRIGLESFTYYRKVHRPEVFGSIGGLVSEQGKDWAHIRNKVNPVQMRVQNVRQNLPQIDQISREFVDKLDTLRDPVTHILNDNFHEQLKMWAFESISFVALNTRMGLLSDRPDPNAARLAEHMTDFFNYSFKYDVQPSIWPYYKTPGFKKFLQTYDKITEITTAYIDEAIKRFEIEKDSGNECVLQQLLSLNKKVAVVMAMYMLMAGIDTTSSAFVTILYHLARNPHKQRQLHRERRRILPDSDEPLTPENTKNMPYLRACIKECMRITSITPGNFRIATKDLVLSGYRVPRGEGVLMGVLELSNSEKYFGQSGQFMPERWLKADTDPDVKACPAARSRNPFVYLAFGFGPRTCIGKRIAELEMETLLTRLLRRYQVSWLAEMPLQYESNIILSPHGIYVQVRAAC | Function: Probably involved in steroid hormones biosynthesis.
Sequence Mass (Da): 62031
Sequence Length: 532
Subcellular Location: Mitochondrion
EC: 1.14.-.-
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Q6IDS6 | MSDRILCKFFVHGSCLKGENCEFSHDSKDPPNNVCTFYQKRICLYGSRCRYDHVRAASNLPLSSDSESLDRSISTTPSRHLQQQGDNNDGDKSSNVYCIHPREYPICSFAAAGDCPRGNQCPHMHGDLCNTCGKKCLHPFRPEEREEHTKECEKKQKHIEALKQSQDIECSVCLDRILSKATPGERKFGLLTECDHPFCIQCIRNWRSSAPVSGMDVNSTLRACPICRKLSYFVVPSVVWYSSPEEKKEIIDIYKAKLRSIDCKHFNFGNGNCPFGASCFYKHAYSDGHLEEVVLRHLGSQEGETVITDSIRLSEFLGGLQIF | Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 36562
Sequence Length: 323
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q94AD9 | MRTPMSDTQHVQSSLVSIRSSDKIEDAFRKMKVNETGVEELNPYPDRPGERDCQFYLRTGLCGYGSSCRYNHPTHLPQDVAYYKEELPERIGQPDCEYFLKTGACKYGPTCKYHHPKDRNGAQPVMFNVIGLPMRLGEKPCPYYLRTGTCRFGVACKFHHPQPDNGHSTAYGMSSFPAADLRYASGLTMMSTYGTLPRPQVPQSYVPILVSPSQGFLPPQGWAPYMAASNSMYNVKNQPYYSGSSASMAMAVALNRGLSESSDQPECRFFMNTGTCKYGDDCKYSHPGVRISQPPPSLINPFVLPARPGQPACGNFRSYGFCKFGPNCKFDHPMLPYPGLTMATSLPTPFASPVTTHQRISPTPNRSDSKSLSNGKPDVKKESSETEKPDNGEVQDLSEDASSP | Function: Possesses RNA-binding and ribonuclease activities in vitro.
Sequence Mass (Da): 44704
Sequence Length: 404
Subcellular Location: Nucleus
EC: 3.1.-.-
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P75925 | MSFTNTPERYGVISAAFHWLSAIIVYGMFALGLWMVTLSYYDGWYHKAPELHKSIGILLMMGLVIRVLWRVISPPPGPLPSYSPMTRLAARAGHLALYLLLFAIGISGYLISTADGKPISVFGWFDVPATLADAGAQADFAGALHFWLAWSVVVLSVMHGFMALKHHFIDKDDTLKRMLGKSSSDYGV | Cofactor: Binds 2 heme b (iron-protoporphyrin IX) groups per molecule.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20736
Sequence Length: 188
Subcellular Location: Cell inner membrane
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Q8RN05 | MFEEKNALRGTEIHRRERFDPGPELRALMAEGRMSVMESEESPGGRTGWLATGYEETRQVLGSDKFSAKLLFGGTAAGRIWPGFLNQYDPPEHTRLRRMVASAFTVRRMRDFRPRIEAVVKATLDDIEATGGPVDFVPRFAWPIATTVICDFLGIPRDDQAELSRVLHASRSERSGKRRVAAGNKYWTYMGQVAAKTRRDPGDDMFGAVVREHGDDITDAELLGVAAFVMGASGDQVARFLSAGAWLMVEHPEQFAVLRDDPDSVPDWLNEVARYLTSDEKTTPRIALEDVRIGDQLVKKGDAVTCSLLASNRHRFPDPEDRFDITREKPSHVTFGHGIHHCLGRPLAEMVFRTAIPALAHRFPTLRLAEPDREIKLGPPPFDVEALLLDW | Function: Involved in the coupling of aromatic side chains of the heptapeptide of vancomycin.
Sequence Mass (Da): 43829
Sequence Length: 391
Pathway: Antibiotic biosynthesis; vancomycin biosynthesis.
EC: 1.14.-.-
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P30992 | MASMNFSPPEYPDYGTATLDPNIFVDESLNTPKLSVPDMIALVIFVMVFLVGVPGNFLVVWVTGFEVRRTINAIWFLNLAVADLLSCLALPILFSSIVQQGYWPFGNAACRILPSLILLNMYASILLLTTISADRFVLVFNPIWCQNYRGPQLAWAACSVAWAVALLLTVPSFIFRGVHTEYFPFWMTCGVDYSGVGVLVERGVAILRLLMGFLGPLVILSICYTFLLIRTWSRKATRSTKTLKVVVAVVVSFFVLWLPYQVTGMMMALFYKHSESFRRVSRLDSLCVAVAYINCCINPIIYVLAAQGFHSRFLKSLPARLRQVLAEESVGRDSKSITLSTVDTPAQKSQGV | Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a . The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production (By similarity).
PTM: Sulfation plays a critical role in the association of C5aR with C5a, but no significant role in the ability of the receptor to transduce a signal and mobilize calcium in response to a small peptide agonist.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39213
Sequence Length: 352
Subcellular Location: Cell membrane
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P21730 | MDSFNYTTPDYGHYDDKDTLDLNTPVDKTSNTLRVPDILALVIFAVVFLVGVLGNALVVWVTAFEAKRTINAIWFLNLAVADFLSCLALPILFTSIVQHHHWPFGGAACSILPSLILLNMYASILLLATISADRFLLVFKPIWCQNFRGAGLAWIACAVAWGLALLLTIPSFLYRVVREEYFPPKVLCGVDYSHDKRRERAVAIVRLVLGFLWPLLTLTICYTFILLRTWSRRATRSTKTLKVVVAVVASFFIFWLPYQVTGIMMSFLEPSSPTFLLLKKLDSLCVSFAYINCCINPIIYVVAGQGFQGRLRKSLPSLLRNVLTEESVVRESKSFTRSTVDTMAQKTQAV | Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a . The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events . Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production .
PTM: Sulfation plays a critical role in the association of C5aR with C5a, but no significant role in the ability of the receptor to transduce a signal and mobilize calcium in response to a small a small peptide agonist . Sulfation at Tyr-14 is important for CHIPS binding .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39336
Sequence Length: 350
Subcellular Location: Cell membrane
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Q6UNA4 | MDDMCSILTEEELSLYNITDCEFVKPGGLGPVLGPRHLSALVFYGLVFLLGVPGNALVVWVTGFRMPRSVTSLWFLNLALADLLCCLSLPLLMVPLAMDQHWPFGPVACKLLKGLLYLIMFCSVLLLVLISLDRFLLVSWPVWCQNWRRPRKAGWVCVGVWLLALLGSIPQFVYVKEVQLSTSKSECLGLYTVASAWANTTARFLVGFVLPFITIVTCHWVVYSRARRGSGVGPGRVSEARSRRTLRVIVAVSLSFFLCWFPLHILDFLVLSTPRHSSHSANIQLAHTLALCLAYCNSCLNPLLYVCLGRGFKQNINRSLRNMFNFATEESVTRQSMFKSTSERTQEMNM | Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39323
Sequence Length: 350
Subcellular Location: Cell membrane
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Q9TUE1 | APMENSTYDYTNYDSLGTLDPSTPVDNTVRRLRPTTIVALVIYMAVFLVGVPGNALVVWVTALEAKRTVNAIWFLNLAVADLLSCLALPILFVSIIQEGHWPFGRAACSVLPSLILLNMYASILLLATISADRFLLVFNPIWCQNTRGAGLAWLACCVAWGLALLLTIPSFLYRKVLQDDYPPKTTCGVDYGHEGVRAERAVAIVRLVVGFLLPLFTLSVCYTFLLLRTWSRNGTRSTKTLKVVVAVVVSFFIFWLPYQVMGMILALLHPSSATFRWAIRLDPLCIALAYVNCCINPIIYVVAGKGFQGQLRKSLPSLLRNVLAEESVIQGSKSFSRSTVDTVADKCQAV | Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a . The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production (By similarity).
PTM: Sulfation plays a critical role in the association of C5aR with C5a, but no significant role in the ability of the receptor to transduce a signal and mobilize calcium in response to a small peptide agonist.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38586
Sequence Length: 350
Subcellular Location: Cell membrane
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A0A0S1TPC7 | MQVLILLSLAFLASCVVAYSRRRPGGRGAGDLPPGPPRLPIIGNMLQLGQNPHKSLAHLAKTYGPLMSLKLGNQFVVVVSSPEMAREVLQRHGLVFSRPFTPIAVQILGHGEVSMNMLPATSPIWKKIRKIAREKLFSNQALHATRAVRRERLRKLADYVGRCSGAMNVGEATFTTMSNLMFATLFSVEITQYADSDSDSGVNKKFREHVNAITRYMGVPNIADFFPIFAPFDPQGLRRKLTYHLGSLLELVQSLIEQRLRARNAATYRKKDDFLEMLLDLSEGDEYDLSVNEIKHLCVDLIIAGSDTSAATTEWAMVELLLHPDKLAKLKAELKSVVGDKSIIEESDISKLPYLQATVKEVLRYHPAAPLLAPHLAEEETQLNGYIIPKNTKIFINDWTISRDPSIWKNPEMFEPERFLNNDIDFCGQHFELIPFGSGRRICPGLPLASRMLHCMVATLCHNFDWELEKGTESKQLQREDVFGLALQKKIPLRAIPIKV | Function: Monooxygenase involved in the biosynthesis of carnosate, a potent antioxidant labdane-related diterpene natural product . Catalyzes the oxidation of 11-hydroxyferruginol to produce carnosate . Mediates the conversion of miltiradien into miltiradien-20-al (By similarity). Also involved in the production of pisiferic acid and derivative products from ferruginol (By similarity).
Catalytic Activity: 11-hydroxyferruginol + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = carnosate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56161
Sequence Length: 500
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.14.61
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Q6YTF5 | METRELWVLAAALAVSLLYYLAALMRYAGGGCSRSSRPPLPPGPTPLPLIGNLLSLRGVLHHRLASLARVHGPVMALRLGLTTAVVVSSRDAAAEAFTKHDRRLAARVVPDSNRAHGFSDRSIIWLPSSDPRWKALRGIQATHLFSPRGLAAVRSVRESKVRDIVAYFRSRAGEEVVFGEAIYSGVLNLVSSSFFSVNMAGVGSEEAHGLRELVEDLVEAIAKPNVSDLFPFLRQLDLQGLRRRTEERMARAFGILDGIIDRRLANRTHGDRHGDFLDALLDLVSEGKMARDHVTIMLFEVFGAGSDTMSVSLEWAMAELLRNPRAMRKARAELEDAAAVVEESDAARLPYLQAVVKEAMRLHPVGPILLPHRAVEDGVEIGGYAVPRGAMVIFNAWAIMRDPAAWERPDEFVPERFMETTTAIDFRGKEYEYLPFGSGRRLCPGLPLAERVVPFVLASLLRAFEWRLPDGVSAEDLDVSERFNTANVLAVPLKVVPVIVN | Function: Enzyme of the diterpenoid metabolism involved in the biosynthesis of the oryzalexin class of phytoalexins. Hydroxylates ent-sandaracopimaradien.
Catalytic Activity: ent-sandaracopimaradien-3beta-ol + O2 + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oryzalexin E + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55244
Sequence Length: 501
Subcellular Location: Membrane
EC: 1.14.14.122
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Q6YTF1 | MENSQMWLLWGALSVALFFYFSTLRRRYAGGKPLPPGPTPLPLIGNLHLVGGGTFHHKLRDLARVHGPVMTLKLGLATNVVISSREAAIEAYTKYDRHLAARATPDTFRACGFADRSMVFIPSSDPQWKALRGIHASHVFTPRVLAAVRPIRERKVGDLIAYLRAHAGEEVLVGHAMYTGILNMVSFSYFSVDIVDMGSQMARELREVVDDIILVVGKPNVSDFYPFLRPLDLQGLRRWTTKRFNRVFSIMGDIIDRRLAHIRDNKPRHDDFLDSILELMAAGKIDRVNVLNMLFEAFVAGADTMALTLEWVMAELLKNPSVMAKARAELRDVLGDKEIVEEADAARLPYLQAVLKEAMRLHPVGALLLPHFAMEDGVEVGGYAVPKGSTVLFNAWAIMRDAAAWERPDEFVPERFVERTPQLDFRGKDVEFMPFGSGRRLCPGLPLAERVVPFILASMLHTFEWELPGGMTAEELDVSEKFKTANVLAVPLKAVPVLIK | Function: Enzyme of the diterpenoid metabolism involved in the biosynthesis of both phytocassane and the oryzalexin class of phytoalexins. Can hydroxylate syn-pimaradiene, ent-pimaradiene, ent-sandaracopimaradiene, ent-isokaurene, ent-kaurene, and ent-cassadiene, but no activity with syn-stemodene, syn-stemarene, syn-labdatriene, C11-alpha-hydroxy-ent-cassadiene or syn-pimadien-19-oic acid as substrates. Hydroxylates 3-alpha-hydroxy-ent-sandaracopimaradiene at C-7-beta, resulting in a 3-alpha,7-beta-diol corresponding to oryzalexins D.
Catalytic Activity: ent-cassa-12,15-diene + O2 + reduced [NADPH--hemoprotein reductase] = ent-11beta-hydroxycassa-12,15-diene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55933
Sequence Length: 500
Subcellular Location: Membrane
EC: 1.14.14.112
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Q9LZ31 | MFPLISFSPTSLDFTFFAIIISGFVFIITRWNSNSKKRLNLPPGPPGWPVVGNLFQFARSGKPFFEYAEDLKKTYGPIFTLRMGTRTMIILSDATLVHEALIQRGALFASRPAENPTRTIFSCNKFTVNAAKYGPVWRSLRRNMVQNMLSSTRLKEFGKLRQSAMDKLIERIKSEARDNDGLIWVLKNARFAAFCILLEMCFGIEMDEETIEKMDEILKTVLMTVDPRIDDYLPILAPFFSKERKRALEVRREQVDYVVGVIERRRRAIQNPGSDKTASSFSYLDTLFDLKIEGRKTTPSNEELVTLCSEFLNGGTDTTGTAIEWGIAQLIANPEIQSRLYDEIKSTVGDDRRVDEKDVDKMVFLQAFVKELLRKHPPTYFSLTHAVMETTTLAGYDIPAGVNVEVYLPGISEDPRIWNNPKKFDPDRFMLGKEDADITGISGVKMIPFGVGRRICPGLAMATIHVHLMLARMVQEFEWCAHPPGSEIDFAGKLEFTVVMKNPLRAMVKPRI | Function: Catalyzes the epoxidation of physiological unsaturated fatty acids in vitro. Can use laurate, oleate, linoleate, linolenate and vernolate as substrate.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58138
Sequence Length: 512
Subcellular Location: Membrane
EC: 1.14.-.-
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O22203 | MSWFLIAVATIAAVVSYKLIQRLRYKFPPGPSPKPIVGNLYDIKPVRFRCYYEWAQSYGPIISVWIGSILNVVVSSAELAKEVLKEHDQKLADRHRNRSTEAFSRNGQDLIWADYGPHYVKVRKVCTLELFTPKRLESLRPIREDEVTAMVESVFRDCNLPENRAKGLQLRKYLGAVAFNNITRLAFGKRFMNAEGVVDEQGLEFKAIVSNGLKLGASLSIAEHIPWLRWMFPADEKAFAEHGARRDRLTRAIMEEHTLARQKSSGAKQHFVDALLTLKDQYDLSEDTIIGLLWDMITAGMDTTAITAEWAMAEMIKNPRVQQKVQEEFDRVVGLDRILTEADFSRLPYLQCVVKESFRLHPPTPLMLPHRSNADVKIGGYDIPKGSNVHVNVWAVARDPAVWKNPFEFRPERFLEEDVDMKGHDFRLLPFGAGRRVCPGAQLGINLVTSMMSHLLHHFVWTPPQGTKPEEIDMSENPGLVTYMRTPVQAVATPRLPSDLYKRVPYDM | Function: Cytochrome P450 which catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. Can use p-coumarate, p-coumaraldehyde, p-coumaroyl methyl ester, 5-O-(4-coumaroyl) D-quinate and 5-O-(4-coumaroyl) shikimate as substrates, but not p-coumaryl alcohol, p-coumaroyl CoA, 1-O-p-coumaroyl-beta-D-glucose, p-hydroxy-cinnamyl alcohol, cinnamate, caffeate or ferulate. Has a weak activity on tri(p-coumaroyl)spermidine, but none on triferuloylspermidine. Hydroxylates preferentially the 5-O-isomer, but can also convert the 4-O- and 3-O-isomers with a lower efficiency. Involved in the biosynthesis of the coumarins scopoletin and scopolin. Essential for the biosynthesis of lignin.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57927
Sequence Length: 508
Subcellular Location: Membrane
EC: 1.14.-.-
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Q9CA61 | MIIYLISLLPIIVATLMLYQRWWRSNIPPGPKPKFLLGNLHQMKPLWTHSFSEWSETYGPIISVWIGSQLTVVVSSSDLARQVLRDKDHQLSNRHRIARMTQTGTDLVWSDYSPHYVKLRKLCTLELFSLKSIENFRSLREMEARSMVVSILKDLMSNSGDDQERKPVIVRKYLAAVVLNTISRLMIGKEFGSEEGKEFKAIVEKEHLLSGSGTILDHVWWLKWVSSWFFSDKEFLAHKDRRTKWFRGAIMVEEDIEIEDHRGFVRKLLVLKEQKELSEETVGGLVWNMLTAGADTTAVVIEWAMAEMIKCPTVQEKAQQELDSVVGSERLMTESDIPILPYLQCVVKEALRLHPSTPLMLPHKASETVWVGGYKVPKGATVYVNVQAIGRDPANWINPYEFRPERFLQEETDVKGRDFRVLPFGSGRRMCPAAQLSMNLMTLVMGNLLHCFSWSSPVPGERIDMSENPGLLCNMRTPLQALALPRAAARAIPLPLD | Function: Acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. Catalyzes also the meta-hydroxylation of the three triferuloylspermidine phenolic rings. Unable to use 5-O-(4-coumaroyl) D-quinate or 5-O-(4-coumaroyl) shikimate as substrates.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56741
Sequence Length: 497
Subcellular Location: Membrane
EC: 1.14.-.-
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Q0JF01 | MMEINSEATVTLVSVVTLPILLALLTRKSSSKKRRPPGPWNLPLVGGLLHLLRSQPQVALRDLAGKYGPVMFLRTGQVDTVVISSPAAAQEVLRDKDVTFASRPSLLVSEIFCYGNLDIGFAPYGAYWRMLRKLCTVELLSTKMVRQLAPIRDGETLALVRNIEAAAGGKKPFTLATLLISCTNTFTAKAAFGQACGGELQEQFLTALDEALKFSNGFCFGDLFPSLRFIDAMTGLRSRLERLRLQLDTVFDKIVAQCESNPGDSLVNVLLRIKDQGELDFPFSSTHVKAIILDMFTGGTETTSSTTEWLMSELMRNPEVMAKVQAEVRGVFDNKSPQDHEGLLENLSYMKLVIKETLRLNPVLPLLLPHLCRETCEIGGYEIVEGTRVLINSWAMARSPEYWDDAEKFIPERFEDGTADFKGSRFEYLPFGTGRRRCPGDIFAMATLELIVARLLYYFDWSLPDGMQPGDIDMELVVGATARRKNHLQLVASPYKPISMQS | Function: Involved in momilactone phytoalexins biosynthesis; acts as a multifunctional diterpene oxidase. Participates in the biosynthetic steps between 9-beta-pimara-7,15-diene and 3-beta-hydroxy-9-beta-pimara-7,15-dien-19,6-beta-olide. Catalyzes also consecutive oxidations at C19 of syn-stemod-13(17)-ene.
Catalytic Activity: 9beta-pimara-7,15-diene + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = 9beta-pimara-7,15-dien-19-oate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55892
Sequence Length: 502
Subcellular Location: Membrane
EC: 1.14.14.111
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Q6DBW9 | MEKTLWTWTLLAVFSLLVVKGMSDGLDLADALGDDDDDEPTTKPPKADPGAGGAGGAAVKPTLKPVKPTVKEPAKPKPKQTGLDDFDLADALNPDNDIKGKGKDSGKGDKEVGGGSRDDGTPNSRGSQFSDDDLLDVGNDNSYKPDKGKGGKGGSSSNVGDLDPADDNNYDTMAETGTIAGIVSAVAMALVGAVSSYISYQKKKLCFSIQQSLNADMVKADAPDAVVAQEPQVQQTLLQPPNAEPPTEENAV | Function: May function as a homophilic adhesion molecule.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26102
Sequence Length: 252
Subcellular Location: Cell membrane
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Q8TCZ2 | MVAWRSAFLVCLAFSLATLVQRGSGDFDDFNLEDAVKETSSVKQPWDHTTTTTTNRPGTTRAPAKPPGSGLDLADALDDQDDGRRKPGIGGRERWNHVTTTTKRPVTTRAPANTLGNDFDLADALDDRNDRDDGRRKPIAGGGGFSDKDLEDIVGGGEYKPDKGKGDGRYGSNDDPGSGMVAEPGTIAGVASALAMALIGAVSSYISYQQKKFCFSIQQGLNADYVKGENLEAVVCEEPQVKYSTLHTQSAEPPPPPEPARI | Function: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity).
PTM: O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 27986
Sequence Length: 262
Subcellular Location: Cell membrane
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Q8BIF0 | MVARLTAFLVCLVFSLATLVQRGYGDTDGFNLEDALKETSSVKQRWDHFSTTTRRPVTTRAPANPAERWDHVATTTTRRPGTTRAPSNPMELDGFDLEDALDDRNDLDGPKKPSAGEAGGWSDKDLEDIVEGGGYKPDKNKGGGGYGSNDDPGSGISTETGTIAGVASALAMALIGAVSSYISYQQKKFCFSIQQGLNADYVKGENLEAVVCEEPQVTYSKQETQSAEPPPPEPPRI | Function: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1. Homophilic adhesion molecule, but these interactions may not be required for cell aggregation.
PTM: O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25463
Sequence Length: 237
Subcellular Location: Cell membrane
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Q5RE35 | MVAWRSAFLVCLAFSLATLVQRGSGDFDDFNLKDAVKETSSVKQRWNHVTTTTKRPVTTRAPANTLGNDFDLADALDDRNDRDDGRRKPIAGGGGFSDKDLEDIVGGGEYKPDKGKGDGRYGSNDDPGSGMVAETGTIAGVASALAMALIGAVSSYISYQQKKFCFSIQHAAEGQEGLNADYVKGENLEAVVCEEPQVKYSALHTQSAEPPPSEPARI | Function: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity).
PTM: O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 23294
Sequence Length: 218
Subcellular Location: Cell membrane
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Q8R1R5 | MVARLTTLLVCLVFSLATLVQRGYGDFDDFNLEDALKETSSVKQSHFSTTTRRTGTTRAPANPAERWDHMTTTTTKRPGTTRAPSNPLELDGFDLEDALDDRNDLDGPKKPSTGEGGGLSDKDLEDILGGGGYKPDKNKGGGGGYGSQDDPGSGAVTDPGTIAGLVSALAAALLGAVSGYLSYQHRKFCFSVQRGLDAAYVKGENLEAVVCEEPRVEAAMCEAPPVTDSTQHSQPTEPLAPERPRI | Function: Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity).
PTM: O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26074
Sequence Length: 246
Subcellular Location: Cell membrane
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E9KBR8 | MISESLLLVFLIVFISASLLKLLFVRENKPKAHLKNPPSPPAIPIIGHLHLLKPLIHHSFRDLSLRYGPLLSLRIGSVKFIVASTPSLAQEFLKTNELTYSSRKMNMAINMVTYHNATFAFAPYDTYWKFMKKLSTTELLGNKTLGHFLPIRTREVHDIIQFLFHKSKAQESVNLTEALLSLSNNVISQMMLSIKSSGTDSQAEQARTLVREVTQIFGEFNVSDFLGFCKNLDLQGFRKRALDIHKRYDALLEKIISDREELRRKSKVDGCEDGDDEKVKDFLDILLDVAEQKECEVQLTRNHVKSLILDYFTAATDTTAISVEWTIAELFNNPKVLKKAQEEVDRVTGNTQLVCEADIPNLPYIHAIIKETMRLHPPIPMIMRKGIEDCVVNGNMIPKGSIVCVNIWAMGRDPNIWKNPLEFKPERFLEGEGSAIDTKGHHFELLPFGSGRRGCPGMPLAMRELPTIIGALIQCFEWKMLGSQGEILDHGRSLISMDERPGLTAPRANDLIGIPVARLNPTPFRQM | Function: Functions as flavone synthase II (FNSII) that catalyzes the direct conversion of flavanones to flavones . In vitro, can convert liquiritigenin, naringenin and eriodictyol to 7,4'-dihydroxyflavone, apigenin and luteolin, respectively .
Catalytic Activity: a flavanone + O2 + reduced [NADPH--hemoprotein reductase] = a flavone + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59580
Sequence Length: 527
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.19.76
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A0A517FNB9 | MEGLLLLLPTAIIALYLYISLIRRSRKKHNLPPGSDGWPFLGETFSYLKPHSAISIGRFMEDHISRYGKIYRSNLFGEPTIVSADAELNRFVLQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRMISLNFMSAARLRTRLMPEVERQTLLVLRSWREGSTFSAQEEAKKFTFNLMAKHIMSMDPGEPETEMLRREYITFMKGVVSAPLNFPGTPYWKALKSRSSILAVIERKMEERIGRRDRGDGGVEDDDLLGWAMNQSNLLKEQILDLLLSLLFAGHETSSMALALAIYFLESCPEAVRDLRDEHLAISMSGKEGECGLSWDQYKQMEFTHCVINESLRLGNVVRFVHRKAIQDVQYKGYDIPCGWKVLPVFAAVHLDSTLYSDPHRFNPWRWQSSSSKTTAANFMPYGGGLRLCTGSELAKLEMAVFLHHLVLNYQWKLAEPEQAFAYPFLDFPKGLQIKVRAIT | Function: Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation.
Catalytic Activity: cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54036
Sequence Length: 473
Pathway: Steroid metabolism; cholesterol metabolism.
Subcellular Location: Membrane
EC: 1.14.14.-
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C7S340 | LPTLSHEAFGDIYLFEGELPNTLTTSNNNQLSLSKQHAKDGEQSLKWQYQPQATLTLNNIVNYQDDKNTATPLTFMMWIYNEKPQSSPLTLAFKQNNKIALSFNAELNFTGWRGIAVPFRDMQGSATGQLDQLVITAPNQAGTLFFDQIIMSVPLDNRWAVPDYQTPYVNNAVNTMVSKNWSALLMYDQMFQAHYPTLNFDTEFRDDQTEMASIYQRFEYYQGIRSDKKITPDMLDKHLALWEKLVLTQHADGSITGKALDHPNRQHFMKVEGVFSEGTQKALLDANMLRDVGKTLLQTAIYLRSDSLSATDRKKLEERYLLGTRYVLEQGFTRGSGYQIITHVGYQTRELFDAWFIGRHVLAKNNLLAPTQQAMMWYNATGRIFEKNNEIVDANVDILNTQLQWMIKSLLMLPDYQQRQQALAQLQSWLNKTILSSKGVAGGFKSDGSIFHHSQHYPAYAKDAFGGLAPSVYALSDSPFRLSTSAHERLKDVLLKMRIYTKETQIPVVLSGRHPTGLHKIGIAPFKWMALAGTPDGKQKLDTTLSAAYAKLDNKTHFEGINAESEPVGAWAMNYASMAIQRRASTQSPQQSWLAIARGFSRYLVGNESYENNNRYGRYLQYGQLEIIPADLTQSGFSHAGWDWNRYPGTTTIHLPYNELEAKLNQLPAAGIEEMLLSTESYSGANTLNNNSMFAMKLHGHSKYQQQSLRANKSYFLFDNRVIALGSGIENDDKQHTTETTLFQFAVPKLQSVIINGKKVNQLDTQLTLNNADTLIDPTGNLYKLTKGQTVKFSYQKQHSLDDRNSKPTEQLFATAVISHGKAPSNENYEYAIAIEAQNNKAPEYTVLQHNDQLHAVKDKITQEEGYAFFEATKLKSADATLLSSDAPVMVMAKIQNQQLTLSIVNPDLNLYQGREKDQFDDKGNQIEVSVYSRHWLTAESQSTNSTITVKGIWKLTTPQPGVIIKHHNNNTLITTTTIQATPTVINLVK | Function: Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion, and preferentially degrades the tetra- and hexasaccharide derivatives of chondroitin sulfate and dermatan sulfate produced by the chondroitin sulfate ABC endolyase, to yield the respective disaccharides. To a lesser extent, is also able to split off disaccharide residues directly from polymeric chondroitin 4- and 6-sulfate, dermatan sulfate, chondroitin, and hyaluronan. Is not active against keratan sulfate, heparan sulfate, and heparin.
Catalytic Activity: Exolytic removal of Delta(4)-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.
Sequence Mass (Da): 111744
Sequence Length: 990
EC: 4.2.2.21
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Q9ESJ1 | MAAATATAGTAACSSSSSSRGGSTDAAATSGVQPPPPPPATAPPEPLRKPRMDPRRRQAALSFLTNISLDGRPPLQDHEWGGGEEGGGTKPGARARLSLLAAGCNAFSAPGTAAAPWTAGSGSSPCPLPPSLVPRVLGEPSQPPRSAPAVTGAQLQLPDGPGGAGQEELEEDDAFTNVQVPSASFLGSGTPGSTSGSRGRLNSFTQGILPIAFSRQNSQNYCALEQSGQGGSTSALEQLQRSRRRLISQRSSLETLEDIEENAPLRRCRTLSGSPRPKNFKKIHFIKNMRQHDTKNGRDLKLDGGRQSAGAMSLKEIIGLEGVELGADGKTVSYTQFLLPTNAFGNRRNTIDSTASFSQFRSLSHRSLSMGRAGSTQGSLDAGSDLGDFMDYDPNLLDDPQWPCGKHKRVLTFPSYMTTVIDYVKPSDLKKDMNETFKEKFPHIKLTLSKIRSLKREMRKLAQEDCGFEEPTVAMAFVYFEKLALRGKLNKQNRKLCAGACVLLAAKVGSDLRKHEVKHLIDKLEEKFRLNRRELIAFEFPVLVALEFALHLPEHEVMPHYRRLIQSS | Function: Cyclin-dependent kinase binding protein. Enhances cyclin-dependent kinase tyrosine phosphorylation by nonreceptor tyrosine kinases, such as that of CDK5 by activated ABL1, which leads to increased CDK5 activity and is critical for neuronal development, and that of CDK2 by WEE1, which leads to decreased CDK2 activity and growth inhibition. Positively affects neuronal outgrowth. Plays a role as a regulator for p53/p73-induced cell death (By similarity).
PTM: Phosphorylated on Ser-274 by CCNE1/CDK3. Phosphorylated on serine/threonine residues by CDK5 and on tyrosine residues by ABL1. Also phosphorylated in vitro by CCNA1/CDK2, CCNE1/CDK2, CCNA1/CDK3 and CCNE1/CDK3.
Sequence Mass (Da): 61429
Sequence Length: 568
Subcellular Location: Nucleus
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P84783 | VRTPVTVQTKVDNIKXY | Function: Hydrolysis of carbamoyl and sulfocarbamoyl esters of paralytic shellfish toxins. Ester hydrolysis is unaffected by the presence or absence of a hydroxyl moiety at the N-1 postion of the substrate toxin but is significantly affected by the stereochemistry of sulfate esters at C-11 of the substrate toxin.
PTM: Glycosylated.
Sequence Mass (Da): 1973
Sequence Length: 17
EC: 3.-.-.-
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P38505 | MAEALFKEIDVNGDGAVSYEEVKAFVSKKRAIKNEQLLQLIFKSIDADGNGEIDQNEFAKFYGSIQGQDLSDDKIGLKVLYKLMDVDGDGKLTKEEVTSFFKKHGIEKVAEQVMKADANGDGYITLEEFLEFSL | Function: Calcium-binding protein which probably acts as a calcium sensor and modulator, contributing to cellular Ca(2+)-mediated signaling . Activates endogenous kinase(s) in a Ca(2+)-dependent manner . Plays a role in regulating actin cytoskeleton dynamics . Regulates the association of actin filaments in a bundle but not actin polymerization and/or nucleation processes . Required for host cell phagocytosis and macropinocytosis .
Sequence Mass (Da): 14953
Sequence Length: 134
Domain: The N-terminal domain (EF-hands 1 and 2) is required for localization to the phagocytic cup, G-actin binding and activation of kinases.
Subcellular Location: Cytoplasm
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Q9NZU7 | MGGGDGAAFKRPGDGARLQRVLGLGSRREPRSLPAGGPAPRRTAPPPPGHASAGPAAMSSHIAKSESKTSLLKAAAAAASGGSRAPRHGPARDPGLPSRRLPGSCPATPQSSGDPSSRRPLCRPAPREEGARGSQRVLPQAHCRPREALPAAASRPSPSSPLPPARGRDGEERGLSPALGLRGSLRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR | Function: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling . Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels . Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but has an opposite effect on channel function . Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels . Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina (By similarity).
PTM: Phosphorylated. The phosphorylation regulates the activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 39838
Sequence Length: 370
Domain: EF-1 binds magnesium constitutively under physiological conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2 binds neither calcium nor magnesium.
Subcellular Location: Cytoplasm
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O88751 | MSSHIAKSESKTSLLKAAAASGGSRAPRHSSARDPGLRGRRLPGPCPDSPATCGDPSSRRPLCRPVPRDEGARGSRRGLPQAHCRPRETLPPARGRDGEERGLAPALSLRGSLRSRGRGDPAPAGTPEADPFLHQLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR | Function: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling (By similarity). Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels . Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but has an opposite effect on channel function. Suppresses the calcium-dependent inactivation of CACNA1D. Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina (By similarity).
PTM: Phosphorylated. The phosphorylation regulates the activity (By similarity).
Sequence Mass (Da): 33017
Sequence Length: 298
Domain: EF-1 binds magnesium constitutively under physiological conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2 binds neither calcium nor magnesium.
Subcellular Location: Cytoplasm
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Q9NPB3 | MGNCAKRPWRRGPKDPLQWLGSPPRGSCPSPSSSPKEQGDPAPGVQGYSVLNSLVGPACIFLRPSIAATQLDRELRPEEIEELQVAFQEFDRDRDGYIGCRELGACMRTLGYMPTEMELIEISQQISGGKVDFEDFVELMGPKLLAETADMIGVRELRDAFREFDTNGDGRISVGELRAALKALLGERLSQREVDEILQDVDLNGDGLVDFEEFVRMMSR | Function: Required for sound encoding at inner hair cells (IHCs) synapses, likely via inhibition of the inactivation of voltage-gated calcium channel of type 1.3 (Cav1.3) in the IHCs . Required for the normal transfer of light signals through the retina (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 24482
Sequence Length: 220
Subcellular Location: Cytoplasm
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Subsets and Splits