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Q7BU69 | MQTSNITNHERNDSSWMSTVKSTTEVSWNKLSFCDILLKIITFGIYSPHETLAEKHSEKKLMDSFSPSLSQDKMDGEFAHANIDGISIRLCLNKGICSVFYLDGDKIQSTQLSSKEYNNLLSSLPPKQFNLGKVHTITAPVSGNFKTHKPAPEVIETAINCCTSIIPNDDYFHVKDTDFNSVWHDIYRDIRASDSNSTKIYFNNIEIPLKLIADLINELGINEFIDSKKELQMLSYNQVNKIINSNFPQQDLCFQTEKLLFTSLFQDPAFISALTSAFWQSLHITSSSVEHIYAQIMSENIENRLNFMPEQRVINNCGHIIKINAVVPKNDTAISASGGRAYEVSSSILPSHITCNGVGINKIETSYLVHAGTLPSSEGLRNAIPPESRQVSFAIISPDV | Function: Alpha-tubulin-specific protease that is required for entry into epithelial cells and for subsequent intra- and intercellular spreading. Contributes to bacterial entry into epithelial cells by inducing microtubule (MT) destabilization and the formation of membrane ruffles. The membrane ruffling evoked by VirA results from the activation of host rac1, which is associated with the destruction of MT networks. Creates a tunnel inside the host cell cytoplasm by breaking down the microtubule infrastructure. This facilitates the bacterium's movement through the cytoplasm and also helps other bacteria move faster during the invasion of the eukaryotic cell. Is absolutely required for virulence.
Sequence Mass (Da): 44735
Sequence Length: 400
Subcellular Location: Secreted
EC: 3.4.22.-
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G9N4B0 | MADQQQNPQESELLLTSAGYVSTFPAPGLRRTVRHITGHNAEGKGVFIQTDCGDHHRIIGNEQALANIIYSTKETPVEMNGDVDLKYAKENEPPLHIHNGSVCRMIDFAPNVISPMHRAVSLDYGIVIEGEFKLILDSGESRIMRQGDVSVQRASAHQWHNITGNGTLPGRMMWVLLDCKPIVINDIDFMECSQ | Function: Cupin-domain-containing oxidoreductase; part of the gene cluster that mediates the biosynthesis of virensols and trichoxide, fungal natural products that contain or are derived from a salicylaldehyde core . The pathway begins with the synthesis of the reduced chain in virensol C by the highly reducing polyketide synthase virA via condensation of one acetate and 8 malonate units . VirA has interesting programming rules since the first 2 ketides are fully reduced, the 3 following ketides undergo beta-dehydration, and the last 3 ketides are only reduced to beta-hydroxys to yield the trihydroxy portion . The production of aldehyde virensol C by virA alone is surprising, since virA does not contain a reductase (R) domain that is typically associated with reductive product release in HRPKS . The cupin-domain enzyme virC is involved in enhancing virA product turnover . The short-chain dehydrogenase virB then oxidizes the C-7 alcohol of virensol C to a ketone, yielding virensol D . Virensol D is further transformed to salicylaldehyde 5-deoxyaurocitrin by the short-chain dehydrogenase virD . VirD catalyzes the dehydrogenation of C-3 to form the beta-ketone aldehyde, which is followed by the generation of the nucleophilic C-2 that is required for the intramolecular aldol condensation between C-2 and C-7, itself followed by dehydration and aromatization which leads to salicylaldehyde 5-deoxyaurocitrin . While the dehydrogenation of virensol D is definitely catalyzed by virD, the aldol condensation and dehydration may be uncatalyzed or assisted by virD . The short chain dehydrogenase virG then converts salicylaldehyde 5-deoxyaurocitrin into virensol B which is further hydroxylated by the cytochrome P450 monooxygenase virE to yield the hydroquinone virensol A . VirI then may oxidize virensol A to form the quinone, while virH performs the epoxidation . Finally, the two remaining short-chain dehydrogenases, virK and virL, are probably responsible for reducing the ketones to the corresponding alcohols to furnish the epoxycyclohexanol structure in trichoxide .
Sequence Mass (Da): 21577
Sequence Length: 194
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q6G2A8 | MKYTKTQLALISMPIASGALTIFLVPHMLSFVINDLKTNQIYWYVRSEPLLTLMLVAAVSLFYTLSQKLHLRKAITFVSTAFFCITALYYIGSEIKRLNPYVGQQGITWGYALKFMDPMVVFGVILGFVLLAIQVIITSPRTSNVKRAKKGIFGDAAWMNLKEAARIFPSNGQIVIGERYRVDQDNVRNIPFAPGNKTTWGKGGTAPLLTFNLDFGSTHMIFFAGSGGYKTTSTVVPTCLTYTGPIVCLDPSTEIAPMVKFARKKMGNRNVIILDPNSLLTKNFNVLDWLLDENIPRTRREANIVSFSKLLLSEKKSENSSAEYFSTQAHNLLTALLAHVIFSDKYEDSERNLKTLRAILSQSETAVVNQLRMIQETTPSPFIREMVGIFTEMADQTFSGVYTTASKDTQWLSLSNYADLVCGNDFASSDIANGKTDVFLNLPASILNSYPAIGRVIIGAFLNAMVTADGNYKKRVLFVLDEVDLLGYMNILEEARDRGRKYGTSLMLFYQSSGQLVNHFGEAGARSWFESCSFVSYAAIKDLQTAKDISERCGQMTIEVTGTSKSRGLSLTKGSQNINYQQRALILPHEIIQEMRQDEQIILMQGHPPLRCGRAIYFRRKEMLAATEKNRFAPQAKKS | Function: The type IV secretion system VirB/VirD4 is a major virulence determinant for subversion of human endothelial cell (HEC) function. VirB-dependent changes of HEC include massive cytoskeletal rearrangements, a pro-inflammatory activation by nuclear factor NF-kappa-B, inhibition of early and late events of apoptosis, leading to an increased cell survival, and, at high infection doses, a cytostatic or cytotoxic effect, which interfers with a potent VirB-independent mitogenic activity. These changes of HEC require the T4S coupling protein VirD4 and at least one of the effector proteins BepA-G.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71447
Sequence Length: 639
Subcellular Location: Cell membrane
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Q08520 | MTSPTNSTMLTYTTNNYYDDDYYEYSTITDYYNTINNDITSSSVIKAFDNNCTFLEDTKYHIIVIHIILFLLGSIGNIFVVSLIAFKRNKSITDIYILNLSMSDCIFVFQIPFIVYSKLDQWIFGNILCKIMSVLYYVGFFSNMFIITLMSIDRYFAIVHPIKRQPYRTKRIGILMCCSAWLLSLILSSPVSKLYENIPHMSKDIYQCTLTNENDSIIAFIKRLMQIEITILGFLIPIIIFVYCYYRIFTTVVRLRNRRKYKSIKIVLMIVVCSLICWIPLYIVLMIATIVSLYTSNIFRHLCLYLNLAYAITFSETISLARCCINPIIYTLIGEHVRSRISSICSCIYRDNRIRKKLFSRKSSSSSNII | Function: Putative chemokine receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43171
Sequence Length: 370
Subcellular Location: Host cell membrane
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Q07175 | MAVSARPARAPRGSDKVKKDKAAQTSGPRQGSRMGKLLGFEWTDVSSWERLVTLLNRPTDPAGLAVFRFLFGLMMVLDIPQERGLSSLDRRYLDGLEVCRFPLLDALQPLPLDWMYLIYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFVDAHHYWSVDGLLRARKRNAHVPLWNYAVLRGQIFIVYFIAGIKKLDADWVEGYSMEYLSRHWLFSPFKLVLSEEMTSLLVVHWCGLLLDLSAGFLLFFDASRPIGFVFVSYFHCMNSQLFSIGMFPYVMLASSPLFCSPEWPRKLVAHCPKKLQELLPLRTAPQPSTSCMYKRSRARGSQKPGLRHKLSTAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTPWLQPLLMDLSPWRTKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLQEGEKMQLPAGEYHKVYTVSSSPSCYMYIYVNTTEVALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNAPFHERLVRFLLRKLFIFRRSFLMTCISLRNLAFGRPSLEQLAQEVTYANLRPFEPAGEPSPVNTDSSNPNPPEPDSHPVHSEF | Function: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. Catalyzes gamma-carboxylation of various proteins, such as blood coagulation factors (F2, F7, F9 and F10), osteocalcin (BGLAP) or matrix Gla protein (MGP).
PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+) + H2O = CO2 + L-glutamyl-[protein] + O2 + phylloquinol
Sequence Mass (Da): 87557
Sequence Length: 758
Subcellular Location: Endoplasmic reticulum membrane
EC: 4.1.1.90
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P38435 | MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF | Function: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide . Catalyzes gamma-carboxylation of various proteins, such as blood coagulation factors (F2, F7, F9 and F10), osteocalcin (BGLAP) or matrix Gla protein (MGP) .
Catalytic Activity: 2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+) + H2O = CO2 + L-glutamyl-[protein] + O2 + phylloquinol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87561
Sequence Length: 758
Subcellular Location: Endoplasmic reticulum membrane
EC: 4.1.1.90
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O88496 | MAVHRGSARAAPASDKVQKNKPAQTSGLEQGSRMARIFGFEWADLSSWQSVVTLLNRPTDPANLAVFRFLFAFLMLLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLWYRLSCMLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLSAQKKNAHVPLWNYTVLRGQIFIVYFIAGVKKLDADWVEGYSMEHLSRHWLFSPFKLVLSEELTSLLVVHWCGLLLDLSAGFLLFFDASRPIGLVFVSYFHCMNSQLFSIGMFPYVMLASSPLFCSAEWPRKLVARCPKRLQELLPAKAAPRPSASCVYKRARAKAGQKPGLRHHLGTVFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGLTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSLLLPKYNVTEPQIYFDIWVSINDRFQQRLFDPRVDIVQAVWSPFRRTPWVQPLLMDLSPWRTKLQDIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTVSSSPSCYMYIYVNTTEVALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQRKLQEIERRRNSPLHERFLRFVLRKLYVFRRSFLMTRISLRNLLFGRPSLEQLAQEVTYANLRPFEPVDESSASNTDSSDPHPSEPDSEHVHSEL | Function: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. Catalyzes gamma-carboxylation of various proteins, such as blood coagulation factors (F2, F7, F9 and F10), osteocalcin (BGLAP) or matrix Gla protein (MGP).
Catalytic Activity: 2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+) + H2O = CO2 + L-glutamyl-[protein] + O2 + phylloquinol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87479
Sequence Length: 758
Subcellular Location: Endoplasmic reticulum membrane
EC: 4.1.1.90
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Q9BQB6 | MGSTWGSPGWVRLALCLTGLVLSLYALHVKAARARDRDYRALCDVGTAISCSRVFSSRWGRGFGLVEHVLGQDSILNQSNSIFGCIFYTLQLLLGCLRTRWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVCITTYAINVSLMWLSFRKVQEPQGKAKRH | Function: Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development.
Catalytic Activity: [protein]-disulfide + H2O + phylloquinone = 2,3-epoxyphylloquinone + [protein]-dithiol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18235
Sequence Length: 163
Domain: Partially oxidized VKORC1 forms a cysteine adduct with substrates, vitamin K 2,3-epoxide, inducing a closed conformation, juxtaposing all cysteines (S-S or SH) for unimpeded electron transfer . VKOR becomes fully oxidized with an open conformation that releases reaction products, vitamin K quinone, or hydroquinone . Cys-132 and Cys-135 constitute the catalytic redox-active center . Cys-43 and Cys-51 are the cysteine pair that mediates transfer of reducing equivalents during catalysis .
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.17.4.4
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Q9CRC0 | MGTTWRSPGLVRLALCLAGLALSLYALHVKAARARDENYRALCDVGTAISCSRVFSSRWGRGFGLVEHMLGADSVLNQSNSIFGCLFYTLQLLLGCLRGRWASILLVLSSLVSVAGSVYLAWILFFVLYDFCIVCITTYAINVGLMLLSFQKVPEHKTKKH | Function: Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development.
Catalytic Activity: [protein]-disulfide + H2O + phylloquinone = 2,3-epoxyphylloquinone + [protein]-dithiol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17768
Sequence Length: 161
Domain: Partially oxidized VKORC1 forms a cysteine adduct with substrates, vitamin K 2,3-epoxide, inducing a closed conformation, juxtaposing all cysteines (S-S or SH) for unimpeded electron transfer. VKOR becomes fully oxidized with an open conformation that releases reaction products, vitamin K quinone, or hydroquinone. Cys-132 and Cys-135 constitute the catalytic redox-active center. Cys-43 and Cys-51 are the cysteine pair that mediates transfer of reducing equivalents during catalysis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.17.4.4
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Q8N0U8 | MAAPVLLRVSVPRWERVARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYILQLLLGMTASAVAALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLIINYKRLVYLNEAWKRQLQPKQD | Function: Involved in vitamin K metabolism. Can reduce inactive vitamin K 2,3-epoxide to active vitamin K, and may contribute to vitamin K-mediated protection against oxidative stress. Plays a role in vitamin K-dependent gamma-carboxylation of Glu residues in target proteins.
Catalytic Activity: [protein]-disulfide + H2O + phylloquinone = 2,3-epoxyphylloquinone + [protein]-dithiol
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19836
Sequence Length: 176
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.17.4.4
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P27558 | MLARQRVKRANPEQLYKTCKATGGDCPPDVIKRYEQTTPADSILKYGSVGVFFGGLGIGTGRGGGGTVLGAGAVGGRPSISSGAIGPRDILPIESGGPSLAEEIPLLPMAPRVPRPTDPFRPSVLEEPFIIRPPERPNILHEQRFPTDAAPFDNGNTEITTIPSQYDVSGGGVDIQIIELPSVNDPGPSVVTRTQYNNPTFEVEVSTDISGETSSTDNIIVGAESGGTSVGDNAELIPLLDISRGDTIDTTILAPGEEETAFVTSTPERVPIQERLPIRPYGRQYQQVRVTDPEFLDSAAVLVSLENPVFDADITLTFEDDLQQALRSDTDLRDVRRLSRPYYQRRTTGLRVSRLGQRRGTISTRSGVQVGSAAHFFQDISPIGQAIEPIDAIELDVLGEQSGEGTIVRGDPTPSIEQDIGLTALGDNIENELQEIDLLTADGEEDQEGRDLQLVFSTGNDEVVDIMTIPIRAGGDDRPSVFIFSDDGTHIVYPTSTTATTPLVPAQPSDVPYIVVDLYSGSMDYDIHPSLLRRKRKKRKRVYFSDGRVASRPK | Function: Minor protein of the capsid that localizes along the inner surface of the virion, within the central cavities beneath the L1 pentamers. Plays a role in capsid stabilization through interaction with the major capsid protein L1. Once the virion enters the host cell, L2 escorts the genomic DNA into the nucleus by promoting escape from the endosomal compartments and traffic through the host Golgi network. Mechanistically, the C-terminus of L2 possesses a cell-penetrating peptide that protudes from the host endosome, interacts with host cytoplasmic retromer cargo and thereby mediates the capsid delivery to the host trans-Golgi network. Plays a role through its interaction with host dynein in the intracellular microtubule-dependent transport of viral capsid toward the nucleus. Mediates the viral genome import into the nucleus through binding to host importins. Once within the nucleus, L2 localizes viral genomes to host PML bodies in order to activate early gene expression for establishment of infection. Later on, promotes late gene expression by interacting with the viral E2 protein and by inhibiting its transcriptional activation functions. During virion assembly, encapsidates the genome by direct interaction with the viral DNA.
PTM: Highly phosphorylated.
Sequence Mass (Da): 59975
Sequence Length: 554
Subcellular Location: Virion
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Q98995 | MIQVLLVTICLAVFPYQGSSKTLKSGNVNDYEVVNPQAVTGLPKGAVKQPEKKYEDTMQYEFEVNGEPVVLHLEKNRGLFSKDYSETHYSPDGREITTNPAVEDHCYYHGRIQNDADSTASISACNGLKGYFTLRGETYLIEPLKLPDSEAHAVYKYENIEKEDEAPKMCGVTQTNWASDEPIKKASQLNLTPEQQRFEPRYIELVIVADHAMVTKYNGDLAAITTWVHQLVNNINGFYRDLNVHITLSAVEVWTNGDLINVQPAASVTLNLFGEWRERDLLNRRMHDHAQLLTGIDLDDNIIGLAYDDSMCDPRYSVGIVQDHSAIIRLVAVTMAHELGHNLGMNHDGDQCNCGANGCVMSVVLIEQRSYQFSDCSKNKYQTYLTNRNPQCILNQPLRTDTVSTPVSGNELLQNSGNPCCDPVTCQPRRGEHCVSGKCCRNCKFLRAGTVCKRAVGDDMDDYCTGISSDCPRNPYKD | Cofactor: Binds 1 zinc ion per subunit.
Function: Fibrinolytic and fibrinogenolytic metalloproteinase that hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of fibrin and fibrinogen. Its fibrinolytic activity is direct, without any plasminogen activation. Also hydrolyzes casein and B-chain of oxidized insulin. Inhibits ADP-induced and collagen-induced platelet aggregation. Shows low hemorrhagic activity. Cleaves the plasma proteinase inhibitors alpha(2)-macroglobulin (A2M) and pregnancy zone protein (PZP), and is inhibited by them. The metalloprotease has no strict P1-P1' specificity requirement. Hydrolysis at sites with a Pro residue at P1 is observed with bradykinin, substance P, PZP and alpha chain fibrinogen (FGA) .
Sequence Mass (Da): 53480
Sequence Length: 478
Subcellular Location: Secreted
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Q698K8 | EDEAPKMCGVTQNWESYEPIKKASQSNLTPAHQRYIELVIVADHGMFTKYNGDSDKIREWVRQMVNTVDEIYSYMYIDVALAGLEIWSNEDLINVQPAAPHTLDSFGKWRERDLLHRIHHDNAMLLTAIDFDGPTIGLAYVGTMCKPKGSTGVVQDHSTINLRVAVTMAHEIGHNLGIHHDTGSCSCGGYSCIMSPVISHEPSKYFSDCSYTQCWDFIMNQKPQCILNKPLRTDTVSTPVSGNELLEAGEECDCGSPGNPCCDAATCKLRQGAQCAEGLCCDQCRFMKKGTVCRIARGDDMDDYCNGISAGCPRNPFHA | Cofactor: Binds 1 zinc ion per subunit.
Function: metalloproteinase that impairs hemostasis in the envenomed animal (By similarity). Shows autoproteolysis dependent on pH and temperature. Does not show hemorrhagic activity.
Sequence Mass (Da): 35314
Sequence Length: 319
Subcellular Location: Secreted
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A2VDK9 | MERLDKAALNALQPSDFRNESSLASTLKTLLFFTALMITVPIGLYFTTKSYVFEGAFGMSNRDSYFYAAIVAVVAVHVVLALFVYVAWNEGSRQWREGKQD | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11366
Sequence Length: 101
Subcellular Location: Endoplasmic reticulum membrane
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A5JYQ9 | MTTSSSSEPSTMATLFPNFRDQEVQSAVKNLLTYSLVILIVPLASMFLLKQFFFEGLLGVSANDALTYSAIIAVVLVHVVLGIWLFAATKQEDRKKRENKQD | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11354
Sequence Length: 102
Subcellular Location: Endoplasmic reticulum membrane
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Q1DPX9 | MATRRNPTKESITTSPPPDQQPRQPGELEHREAIQLRDLPGYPQQVLWKLIIYSIAVLVLPLSAYFYSVNYVFDGNTTYAGATAAITANLILFSYIVVAMREDKGDQEQLREQQQLRGNKEETKKMK | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14500
Sequence Length: 127
Subcellular Location: Endoplasmic reticulum membrane
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P0CS25 | MSNRVSTGKMAMAPQESVQPAVLYKLVLFALLMAVVPIGTYFSTLNYLWDGASRCGFPSGLCSTTFAAISAIAAANLILVGYVVVAFREDAASRTGPLPEKKTS | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10993
Sequence Length: 104
Subcellular Location: Endoplasmic reticulum membrane
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B8JLV7 | MQNYDKKEVGSVPGAMPDFRGNDGSLVSVLKTLLFFTILMITLPIGLYFTSKSLLFEATLGYSSNDSYFYAAILAVLAVHVVLALFVYVAWNEGSRQWREGKQD | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11606
Sequence Length: 104
Subcellular Location: Endoplasmic reticulum membrane
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Q6BXM0 | MPADIPKSVVQKLVFFTAAMIICPVATFFICQYLFSNNAIISGGVSALVANIVLIGYVVAAFMEDTTEQEPEETKKSR | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8489
Sequence Length: 78
Subcellular Location: Endoplasmic reticulum membrane
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B3M9A8 | MSNKNKKSGGAGNGAAQKQTRQQSHDSQDYSSFKIVLFYCMLIVFLPVVTFFLLKGFVLDRFFSLSEVKVNIASAVGAVVSLHIALGLYIYRAYFGATGSKAVKED | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11606
Sequence Length: 106
Subcellular Location: Endoplasmic reticulum membrane
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Q9VPE4 | MSTKNKKAAGGNGVAPKQTRQQSHDSQDYSSFKTVLFYCMLIVFLPVLTFFVLKGFVLDQFLDISEVKVNIASAVGAVVALHIALGLYIYRAYFGAPGSKGSKTD | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11397
Sequence Length: 105
Subcellular Location: Endoplasmic reticulum membrane
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Q5B905 | MATRRPGKSYADAAVPGSTPGETPSELSSDTSPAVPMHVIYKLIGFTIAMITTPVGMYFVSVTFGASTTVAGIIAAVMANIILFLYIYVAWQEDKEEREADAARRKGAKAQ | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11845
Sequence Length: 111
Subcellular Location: Endoplasmic reticulum membrane
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Q3ZAQ7 | MERPDKAALNALQPPEFRNESSLASTLKTLLFFTALMITVPIGLYFTTKSYIFEGALGMSNRDSYFYAAIVAVVAVHVVLALFVYVAWNEGSRQWREGKQD | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11354
Sequence Length: 101
Subcellular Location: Endoplasmic reticulum membrane
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A4R0J5 | MATRRIVATEKSILEKDDHIGSSPAAGEKSNITPAVPLDVILKLLAFTLAMVVIPIGSYFVTVNSIFKGNSTYAGALAAIMANVVLVAYVVVAMNEDQTEQEKAKEGKKDR | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11866
Sequence Length: 111
Subcellular Location: Endoplasmic reticulum membrane
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P85006 | ASDVTLNSFAEDVTVGECCDCVDLTTVY | Cofactor: Binds 1 zinc ion per subunit.
Sequence Mass (Da): 2970
Sequence Length: 28
Subcellular Location: Secreted
EC: 3.4.24.-
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P85842 | SPCIIIDYLCVTETCFCERFKTNKELLEYITVMFTGVQNLLDTLNLGIVGVAQDYSDYNERVDTVAHETAHLIGAPHDEEGPCQDT | Cofactor: Binds 1 zinc ion per subunit.
Sequence Mass (Da): 9642
Sequence Length: 86
Subcellular Location: Secreted
EC: 3.4.24.-
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Q9GZP7 | MVGDTLKLLSPLMTRYFFLLFYSTDSSDLNENQHPLDFDEMAFGKVKSGISFLIQTGVGILGNSFLLCFYNLILFTGHKLRPTDLILSQLALANSMVLFFKGIPQTMAAFGLKYLLNDTGCKFVFYYHRVGTRVSLSTICLLNGFQAIKLNPSICRWMEIKIRSPRFIDFCCLLCWAPHVLMNASVLLLVNGPLNSKNSSAKNNYGYCSYKASKRFSSLHAVLYFSPDFMSLGFMVWASGSMVFFLYRHKQQVQHNHSNRLSCRPSQEARATHTIMVLVSSFFVFYSVHSFLTIWTTVVANPGQWIVTNSVLVASCFPARSPFVLIMSDTHISQFCFACRTRKTLFPNLVVMP | Function: Putative pheromone receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40021
Sequence Length: 353
Subcellular Location: Cell membrane
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Q8NFZ6 | MTHTLYPTPFALYPINISAAWHLGPLPVSCFVSNKYQCSLAFGATTGLRVLVVVVPQTQLSFLSSLCLVSLFLHSLVSAHGEKPTKPVGLDPTLFQVVVGILGNFSLLYYYMFLYFRGYKPRSTDLILRHLTVADSLVILSKRIPETMATFGLKHFDNYFGCKFLLYAHRVGRGVSIGSTCLLSVFQVITINPRNSRWAEMKVKAPTYIGLSNILCWAFHMLVNAIFPIYTTGKWSNNNITKKGDLGYCSAPLSDEVTKSVYAALTSFHDVLCLGLMLWASSSIVLVLYRHKQQVQHICRNNLYPNSSPGNRAIQSILALVSTFALCYALSFITYVYLALFDNSSWWLVNTAALIIACFPTISPFVLMCRDPSRSRLCSICCRRNRRFFHDFRKM | Function: Putative pheromone receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44476
Sequence Length: 395
Subcellular Location: Cell membrane
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Q9BXE9 | MASKDFAIGMILLSQIMVGFLGNFFLLYHYSFLCFTRGMLQSTDLILKHLTIANSLVILSKGIPQTMAAFGLKDSLSDIGCKFVFYVHRVGRAVCVGNACLLSVFQVITISPSEFRWAELKLHAHKYIRSFILVLCWILNTLVNITVLLHVTGKWNSINSTKTNDYGYCSGGSRSRIPHSLHIVLLSSLDVLCLGLMTLASGSMVFILHRHKQQVQHIHGTNLSARSSPESRVTQSILVLVSTLCYFTRSPPSLHMSLFPNPSWWLLNTSALITACFPMVSPFVLMSRHPRIPRLGSACCGRNPQFPKLVR | Function: Putative pheromone receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34713
Sequence Length: 311
Subcellular Location: Cell membrane
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Q7Z5H5 | MASRYVAVGMILSQTVVGVLGSFSVLLHYLSFYCTGCRLRSTDLIVKHLIVANFLALRCKGVPQTMAAFGVRYFLNALGCKLVFYLHRVGRGVSIGTTCLLSVFQVITVSSRKSRWAKLKEKAPKHVGFSVLLCWIVCMLVNIIFPMYVTGKWNYTNITVNEDLGYCSGGGNNKIAQTLRAMLLSFPDVLCLGLMLWVSSSMVCILHRHKQRVQHIDRSDLSPRASPENRATQSILILVSTFVSSYTLSCLFQVCMALLDNPNSLLVNTSALMSVCFPTLSPFVLMSCDPSVYRFCFAWKR | Function: Putative pheromone receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33557
Sequence Length: 301
Subcellular Location: Cell membrane
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Q7Z5H4 | MLKLVIIENMAEIMLFSLDLLLFSTDILCFNFPSKMIKLPGFITIQIFFYPQASFGISANTILLLFHIFTFVFSHRSKSIDMIISHLSLIHILLLFTQAILVSLDFFGSQNTQDDLRYKVIVFLNKVMRGLSICTPCLLSVLQAIISPSIFSLAKLKHPSASHILGFFLFSWVLNMFIGVIFCCTLRLPPVKRGQSSVCHTALFLFAHELHPQETVFHTNDFEGCHLYRVHGPLKRLHGDYFIQTIRGYLSAFTQPACPRVSPVKRASQAILLLVSFVFTYWVDFTFSFSGGVTWINDSLLVWLQVIVANSYAAISPLMLIYADNQIFKTLQMLWFKYLSPPKLMLKFNRQCGSTKK | Function: Putative pheromone receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40779
Sequence Length: 357
Subcellular Location: Cell membrane
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Q8WQK0 | MSKIILAIFLIVLCGLIFVTVDAMIDAPCKDNDDCDRFTEYCAIYADENGNEAGKRCEDAIGLLV | Function: Endoparasitoid venom protein that interferes with the activation of host hemolymph prophenoloxidase. May act in conjunction with other venom proteins (such as Vn50), by competitive binding to the zymogen and thereby interrupting the enzyme.
PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 7133
Sequence Length: 65
Subcellular Location: Secreted
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P06817 | MNNATFNCTNINPITHIRGSIIITICVSLIVILIVFGCIAKIFINKNNCTNNVIRVHKRIKCPDCEPFCNKRDDISTPRAGVDIPSFILPGLNLSEGTPN | Function: Putative viral proton channel. May play a role in virus entry.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 11024
Sequence Length: 100
Subcellular Location: Virion membrane
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P27382 | MEKVKAWLIKYKWWIVAAIGGLAAFLLLKNRGGGSGGGGEYMVGSGPVYQQAGSGAVDNTMALAALQANTQLSAQNAQLQAQMDASRLQLETQLNIETLAADNAHYSTQSQLQLGMAQVDLSKYLGDLQSTTSTALAGMQSDTAKYQSNIQLQAENIRANTSLAEIDAQKYIVGKQADIAKYQAKTERRGQDYGFALGLLNFGGKFF | Function: Component of the phage ejection machinery. Pilot protein for the formation of the tube that conducts the genome into the target cell. Probably involved in penetration of the bacterial outer membrane and for making the peptidoglycan layer accessible to the viral transglycosylase. Essential for viral infectivity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22209
Sequence Length: 207
Subcellular Location: Virion membrane
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P35260 | MASSSNYNTYMQYLNPPPYADHGANQLIPADQLSNQQGITPNYVGDLNLDDQFKGNVCHAFTLEAIIDISAYNERTVKGVPAWLPLGIMSNFEYPLAHTVAALLTGSYTITQFTHNGQKFVRVNRLGTGIPAHPLRMLREGNQAFIQNMVIPRNFSTNQFTYNLTNLVLSVQKLPDDAWRPSKDKLIGNTMHPAVSIHPNLPPIVLPTVKKQAYRQHKNPNNGPLLAISGILHQLRVEKVPEKTSLFRISLPADMFSVKEGMMKKRGENSPVVYFQAPENFPLNGFNNRQVVLAYANPTLSAV | Function: Plays an essential role virus particle assembly and budding . Promotes virus assembly and budding by interacting with host proteins of the multivesicular body pathway. The interaction with host E3 ubiquitin ligase SMURF2 facilitates virus budding . The interaction with the nucleocapsid and the plasma membrane may also facilitate virus budding. Specific interactions with membrane-associated GP and VP24 during the budding process may also occur (By similarity). May play a role in genome replication (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33794
Sequence Length: 303
Domain: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. VP40 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase and the three WW domains of SMURF2 E3 ubiquitin ligase.
Subcellular Location: Virion membrane
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Q9T1Q4 | MRLIREDSIEKHLVSEVRKIGGIAYKFVSPGRRGVPDRLVALPNGKIIFVECKAPGEKPTPYQLREHARLFALGHQVIVLDSQDLSSILPAVN | Cofactor: Divalent metal cations. Mg(2+) is the most probable.
Function: Nuclease.
Sequence Mass (Da): 10356
Sequence Length: 93
EC: 3.1.-.-
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P04509 | MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWNFDFGLLGTTLLNLDANYVETARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLIKLSGIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPYSASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANTQQFEHIVQLRRVLTTATITLLPDAERFSFPRVITSADGATTWYFNPVILRPNNVEIEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLMRPPNMTPAVAALFPNAQPFEHHATVGLTLRIESAVCESVLADASETMLANVTSVRQEYAIPVGPVFPPGMNWTDLITNYSPSREDNLQRVFTVASIRSMLVK | Function: Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices . This capsid constitutes the middle concentric layer of the viral mature particle . The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes (By similarity). VP6 is required for the transcription activity of the DLP .
PTM: The N-terminus is blocked.
Sequence Mass (Da): 44843
Sequence Length: 397
Subcellular Location: Virion
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Q54J20 | MNPDNDNDSLPLLTLPEQLFLLILNPETGKLPYTFVPLFHGFVGCGIAELQLMDKVIVTKQNSQSFNNNKMLIKVIDHSKTGDTFLDYILSKLSNSFAQKGLQMATAILTISVGLNKMKRITETIAQSLIKKGFIRGTLKRSVLFKNKSIYEVIDYQAKLSVESSICKVLSTPPDYPDNCLRELIILLTFKQYEDFLIKPKLMDSLISRLYHPEQCAHIKANLRLINKNFYKEPSEVHLTNDPSVKMLSLVIGGIRNAITSE | Function: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. May be involved in vacuolar protein sorting (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29609
Sequence Length: 262
Subcellular Location: Golgi apparatus
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P16790 | MDRKTRLSEPPTLALRLKPYKTAIQQLRSVIRALKENTTVTFLPTPSLILQTVRSHCVSKITFNSSCLYITDKSFQPKTINNSTPLLGNFMYLTSSKDLTKFYVQDISDLSAKISMCAPDFNMEFSSACVHGQDIVRESENSAVHVDLDFGVVADLLKWIGPHTRVKRNVKKAPCPTGTVQILVHAGPPAIKFILTNGSELEFTANNRVSFHGVKNMRINVQLKNFYQTLLNCAVTKLPCTLRIVTEHDTLLYVASRNGLFAVENFLTEEPFQRGDPFDKNYVGNSGKSRGGGGGGGSLSSLANAGGLHDDGPGLDNDLMNEPMGLGGLGGGGGGGGKKHDRGGGGGSGTRKMSSGGGGGDHDHGLSSKEKYEQHKITSYLTSKGGSGGGGGGGGGGLDRNSGNYFNDAKEESDSEDSVTFEFVPNTKKQKCG | Function: Accessory subunit of the DNA polymerase that plays an essential role in viral DNA replication and acts by increasing the processivity of polymerization . Forms dimers that binds to double-stranded DNA and UL54 specifically to stimulates long chain DNA synthesis efficiently. Plays an important role in maintaining the structure of viral replication compartments by interacting with host nucleolin/NUC . In addition, suppresses innate immune responses through effects on host IRF3 and NF-kappa-B. Mechanistically, interfere with the binding of IRF3 and the p65 NF-kappa-B subunit to the promoters of antiviral genes, thereby inhibiting the expression of these genes .
PTM: Phosphorylated by UL97 on serine residues, phosphorylation seems important for UL44 nuclear entry but does not directly affect its role in replication.
Sequence Mass (Da): 46233
Sequence Length: 433
Domain: The C-terminal region is required for viral DNA synthesis.
Subcellular Location: Virion
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B3A0N1 | ALVLIAFAQVLQQCP | Cofactor: Binds divalent metal cations.
Function: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa (By similarity). Potent calcium-independent prothrombin activator, possesses high hemorrhagic activity along with metalloproteinase activity. Has considerably stronger activity than FXa.
PTM: N-glycosylated.
Sequence Mass (Da): 1614
Sequence Length: 15
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Q84LM2 | MAARCWVWGFVVALLAVAAAADGEEEEGKWEPLIRMPTEEGDDAEAAAPAPAPAAADYGGTRWAVLVAGSSGYGNYRHQADVCHAYQILQKGGVKEENIVVFMYDDIAHNILNPRPGTIINHPKGGDVYAGVPKDYTGHQVTTENFFAVLLGNKTAVTGGSGKVIDSKPEDHIFIYYSDHGGPGVLGMPNLPYLYAGDFIKVLQKKHASNSYSKMVIYVEACESGSIFEGLMPENLNIYVTTASNAVENSWGTYCPGEEPSPPPEYITCLGDMYSVAWMEDSETHNLKKETIEDQYELVKKRTSNANKLNEGSHVMEYGDKTFKDEKLFLYQGFNPANGNITNELIWPVPKATVNQRDADLLFMWKRYEQLNGVSEDKLRALREIEDTIAHRKHLDSSIDFIGKLVFGFENGPLALEAARSSGQPLVDNWDCLKKMVRIFESQCGSLTQYGMKYMRAFANICNNGVSEAKMMEASINACGRYNSARWSPMTEGGHSA | Function: Asparagine-specific endopeptidase that may be involved in processing of proteins targeted to vacuoles. Cysteine protease required for post-translational proteolysis of seed storage proteins in the protein storage vacuole (PSV) of developing seeds, by processing of proglutelin precursor to mature glutelin subunits, thus contributing to the formation of protein crystalline structures in PSV .
PTM: Auto-catalytic activation.
Catalytic Activity: Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Sequence Mass (Da): 54886
Sequence Length: 497
Subcellular Location: Protein storage vacuole
EC: 3.4.22.34
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Q39044 | MAKSCYFRPALLLLLVLLVHAESRGRFEPKILMPTEEANPADQDEDGVGTRWAVLVAGSSGYGNYRHQADVCHAYQILRKGGLKEENIVVLMYDDIANHPLNPRPGTLINHPDGDDVYAGVPKDYTGSSVTAANFYAVLLGDQKAVKGGSGKVIASKPNDHIFVYYADHGGPGVLGMPNTPHIYAADFIETLKKKHASGTYKEMVIYVEACESGSIFEGIMPKDLNIYVTTASNAQESSYGTYCPGMNPSPPSEYITCLGDLYSVAWMEDSETHNLKKETIKQQYHTVKMRTSNYNTYSGGSHVMEYGNNSIKSEKLYLYQGFDPATVNLPLNELPVKSKIGVVNQRDADLLFLWHMYRTSEDGSRKKDDTLKELTETTRHRKHLDASVELIATILFGPTMNVLNLVREPGLPLVDDWECLKSMVRVFEEHCGSLTQYGMKHMRAFANVCNNGVSKELMEEASTAACGGYSEARYTVHPSILGYSA | Function: Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms (By similarity). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds .
PTM: Auto-catalytic activation.
Catalytic Activity: Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Sequence Mass (Da): 53828
Sequence Length: 486
Subcellular Location: Vacuole
EC: 3.4.22.34
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Q9LJX8 | MSSPLGHFQILVFLHALLIFSAESRKTQLLNDNDVESSDKSAKGTRWAVLVAGSNEYYNYRHQADICHAYQILRKGGLKDENIIVFMYDDIAFSSENPRPGVIINKPDGEDVYKGVPKDYTKEAVNVQNFYNVLLGNESGVTGGNGKVVKSGPNDNIFIYYADHGAPGLIAMPTGDEVMAKDFNEVLEKMHKRKKYNKMVIYVEACESGSMFEGILKKNLNIYAVTAANSKESSWGVYCPESYPPPPSEIGTCLGDTFSISWLEDSDLHDMSKETLEQQYHVVKRRVGSDVPETSHVCRFGTEKMLKDYLSSYIGRNPENDNFTFTESFSSPISNSGLVNPRDIPLLYLQRKIQKAPMGSLESKEAQKKLLDEKNHRKQIDQSITDILRLSVKQTNVLNLLTSTRTTGQPLVDDWDCFKTLVNSFKNHCGATVHYGLKYTGALANICNMGVDVKQTVSAIEQACSM | Function: Asparagine-specific endopeptidase that may be involved in processing of proteins targeted to vacuoles (By similarity). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds . Exhibits a caspase-1-like activity in extracellular granules. At the early stage of seed development, required for the formation of the seed coat, by regulating cell death of specific cell layers in inner integument .
PTM: Auto-catalytic activation.
Catalytic Activity: Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Sequence Mass (Da): 52085
Sequence Length: 466
Subcellular Location: Secreted
EC: 3.4.22.34
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Q39119 | MATTMTRVSVGVVLFVLLVSLVAVSAARSGPDDVIKLPSQASRFFRPAENDDDSNSGTRWAVLVAGSSGYWNYRHQADICHAYQLLRKGGLKEENIVVFMYDDIANNYENPRPGTIINSPHGKDVYQGVPKDYTGDDVNVDNLFAVILGDKTAVKGGSGKVVDSGPNDHIFIFYSDHGGPGVLGMPTSPYLYANDLNDVLKKKHALGTYKSLVFYLEACESGSIFEGLLPEGLNIYATTASNAEESSWGTYCPGEEPSPPPEYETCLGDLYSVAWMEDSGMHNLQTETLHQQYELVKRRTAPVGYSYGSHVMQYGDVGISKDNLDLYMGTNPANDNFTFADANSLKPPSRVTNQRDADLVHFWEKYRKAPEGSARKTEAQKQVLEAMSHRLHIDNSVILVGKILFGISRGPEVLNKVRSAGQPLVDDWNCLKNQVRAFERHCGSLSQYGIKHMRSFANICNAGIQMEQMEEAASQACTTLPTGPWSSLNRGFSA | Function: Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms . Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds .
PTM: Auto-catalytic activation.
Catalytic Activity: Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Sequence Mass (Da): 54336
Sequence Length: 494
Subcellular Location: Vacuole
EC: 3.4.22.34
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P36116 | MAEQISHKKSLRVSSLNKDRRLLLREFYNLENEPNKGRQEARIGEKASEAHSGEEQVTDVNIDTEANTEKPVKDDELSATEEDLKEGSEDAEEEIKNLPFKRLVQIHNKLLGKETETNNSIKNTIYENYYDLIKVNDLLKEITNANEDQINKLKQTVESLIKEL | Function: Involved in retrograde transport from early and late endosomes to late Golgi. Links the Golgi-associated retrograde protein (GARP) complex to the t-SNARE TLG1, leading to the fusion between the endosomal vesicles with the late Golgi. May also be indirectly involved in apical bud growth.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18912
Sequence Length: 164
Subcellular Location: Golgi apparatus
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Q8N1B4 | MAAAATMAAAARELVLRAGTSDMEEEEGPLAGGPGLQEPLQLGELDITSDEFILDEVDVHIQANLEDELVKEALKTGVDLRHYSKQVELELQQIEQKSIRDYIQESENIASLHNQITACDAVLERMEQMLGAFQSDLSSISSEIRTLQEQSGAMNIRLRNRQAVRGKLGELVDGLVVPSALVTAILEAPVTEPRFLEQLQELDAKAAAVREQEARGTAACADVRGVLDRLRVKAVTKIREFILQKIYSFRKPMTNYQIPQTALLKYRFFYQFLLGNERATAKEIRDEYVETLSKIYLSYYRSYLGRLMKVQYEEVAEKDDLMGVEDTAKKGFFSKPSLRSRNTIFTLGTRGSVISPTELEAPILVPHTAQRGEQRYPFEALFRSQHYALLDNSCREYLFICEFFVVSGPAAHDLFHAVMGRTLSMTLKHLDSYLADCYDAIAVFLCIHIVLRFRNIAAKRDVPALDRYWEQVLALLWPRFELILEMNVQSVRSTDPQRLGGLDTRPHYITRRYAEFSSALVSINQTIPNERTMQLLGQLQVEVENFVLRVAAEFSSRKEQLVFLINNYDMMLGVLMERAADDSKEVESFQQLLNARTQEFIEELLSPPFGGLVAFVKEAEALIERGQAERLRGEEARVTQLIRGFGSSWKSSVESLSQDVMRSFTNFRNGTSIIQGALTQLIQLYHRFHRVLSQPQLRALPARAELINIHHLMVELKKHKPNF | Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD . Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 82221
Sequence Length: 723
Subcellular Location: Golgi apparatus
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Q9UST3 | MQRASTQDVYDGSGDDLNKLDSLKSVLNDVLSSLERFQVDLDVATSDIYKVSERSNKIQVNLNNLKAVESALGAEIDGAILPPDLIKTISTGDMDHPSWNSALEKLTSFLEGGEDDSSLGNMFNSLQINKDQKKLVDKLRDKAIERIRNYIVVTIKMFRQAFVDVFPIRKHRLIANKNYYLFLFKFNRKLALELQRAYINTMNWFYLYHFEQYSRFLDKVHVLKGETIRVEEDRKGLFNLSKGAQQSYGNQMLSVNLRPQDFDMNSVLTASTMHHIESSPQYIERVYCSWELVLTEHVSSEYAFLLEYFNLSKDQQATVFAAIFEKTLHFSRKYITGLISSSIDCIGILKSIRFTQKLALQAQTNIVPVIEPHYNSMILFLWPRFQAVMDMHCESLRKTNLSVKPEEITSRPHPLSQRVAELLYSLSMLSVNVVEAEPVARSASRLAQDYVSMLQNLCKTVNDKRRQSRFLSNNYTLISTVLSGVSGNLAIEQKTYFEKLNENLTNFQ | Function: Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58385
Sequence Length: 508
Subcellular Location: Golgi apparatus
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P39904 | MDVLKEVLSLDQDKFDQLKETSRDKTNETDDPFENYLKDCKFKAPSNKDQSPFAKLKSLQETHSNNEAAINIIIPQLIDYLTEFTNRLSNYTQDLDFIKKKSNELQSLLEYNSTKLAHISPMVNDLMIPPELIDDIIKGKINESWQDNITFIADKEEIYNKYRSNNLDQDNKDAENSAMLAPKDFDKLCQLLDILKNVILERSKRLIISKIKTLRSHNPVPSQRIQNKLLKVQKIFPFIRDNNLSLALELRQAYCYTMKWYYREYFSRYIRSLTILQFQQIDSQFALGNGLSTTSVSGFNNSPSLFFSNYLTTSASNAFYNKLPVTDEKIDKYFQIKKRLNILTQEDNTVMVSQIAENNTTKNYIEIGFKNLNLAILDNCTVEYHFLKDFFAMNGDNFEEINGLLEQIFQPTFDEATTYTQQLIQYNYDIFGVLISIRVANQLQFESERRGIPSMFDSFLNGQLIQLWPRFQQLVDFQCESLRKAAITTNVAKYAGNSSTSNSSPLTSPHELTVQFGKFLSSFLTLAITHKQSIDERSEPLYNSIIRLRNDFETVMTKCSKKTKSPERFLATNYMYLYNNLQQLHLHLNINDSDAQNYNFDSAENVGTKVANDDDNDSSVPLIIRETENHFKTLVEAFTRN | Function: Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. May also be involved in the actin cytoskeleton organization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74333
Sequence Length: 641
Subcellular Location: Golgi apparatus
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P34561 | MEEPTTSELKLSDNVMNEISDMCITEYCKPNMSLMAQINELFPTEQSLTQLDSIIASVEGEIGELDNELAYLVETNANVSERGEEALKHAQDAMIELEKSIGSIRERTKSSDEIVREMTRDIKQLDIAKRNLTASITTLHHLHILLTGVESLGAWVDKKDYSSIARQLPAILNVLQLFDAYKESDQIANLSGQLDKLKASLTIQLAKDLKNAFQTGQLSDRITDMCRVAAALEGNVKENFVKWFIEQQLSEYVIIYADNEEGAWLDKVDDRYKWFVRKLTDFERAGLSNIFPADWHMGRRLTSEFCTVTRDILYRIMTRRRQDLDWKLLGHAIQHTKMFEALLTKRFPEKDGISFEKAIWSVFDTFLDVFINAQEKTLNEFLDTCASKIRSGEEKPSRESSTHAVPFPSSADMFLLLKKVITESSKLSSEPDALIRDVIGVVRVCLRGYATSCLVAFLPSLGSQQSGAANLFSLIREEIAYPRLTPDQQFLVCCILATADWCAETSIQLQEKLSQRIPGVDISQETEAFYSITNQSLQVLVQDVESTCDAALQSISKVNWTAVDCVGDESPFIGSMRAHLRQAVPLIRDMLSDRRKYFAHFCLKLATQLAHKFVGSLFRCRTISTHGAEQLLLDTHSLKTFLLSVPSIDSIINSKPPTAYVTSVNAALTKAEMILKVVMCSLETVDEFVEQYIKLLPASDAAEMQKVLEMKGVKRQEHSAVLNAYRLKIGASGSDPIQQSNSLTSRIGGALPTVGSAASVSEAFNAVVSMAADGLSDQAVTSSIDKLKRFERLVKRQL | Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN) . The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi . Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1 . Important for neuronal function .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89229
Sequence Length: 798
Subcellular Location: Golgi apparatus
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Q5VIR6 | MMEEEELEFVEELEAVLQLTPEVQLAIEQVFPSQDPLDRADFNAVEYINTLFPTEQSLANIDEVVNKIRLKIRRLDDNIRTVVRGQTNVGQDGRQALEEAQKAIQQLFGKIKDIKDKAEKSEQMVKEITRDIKQLDHAKRHLTTSITTLNHLHMLAGGVDSLEAMTRRRQYGEVANLLQGVMNVLEHFHKYMGIPQIRQLSERVKAAQTELGQQILADFEEAFPSQGTKRPGGPSNVLRDACLVANILDPRIKQEIIKKFIKQHLSEYLVLFQENQDVAWLDKIDRRYAWIKRQLVDYEEKYGRMFPREWCMAERIAVEFCHVTRAELAKIMRTRAKEIEVKLLLFAIQRTTNFEGFLAKRFSGCTLTDGTLKKLESPPPSTNPFLEDEPTPEMEELATEKGDLDQPKKPKAPDNPFHGIVSKCFEPHLYVYIESQDKNLGELIDRFVADFKAQGPPKPNTDEGGAVLPSCADLFVYYKKCMVQCSQLSTGEPMIALTTIFQKYLREYAWKILSGNLPKTTTSSGGLTISSLLKEKEGSEVAKFTLEELCLICNILSTAEYCLATTQQLEEKLKEKVDVSLIERINLTGEMDTFSTVISSSIQLLVQDLDAACDPALTAMSKMQWQNVEHVGDQSPYVTSVILHIKQNVPIIRDNLASTRKYFTQFCVKFANSFIPKFITHLFKCKPISMVGAEQLLLDTHSLKMVLLDLPSISSQVVRKAPASYTKIVVKGMTRAEMILKVVMAPHEPLVVFVDNYIKLLTDCNTETFQKILDMKGLKRSEQSSMLELLRQRLPAPPSGAESSGSLSLTAPTPEQESSRIRKLEKLIKKRL | Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD . Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 94405
Sequence Length: 832
Subcellular Location: Golgi apparatus
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P87129 | MSNGNDNSLIIKNIGNNEFKFVETLHELLPEDITYDDLGSLRLSLSERLQESVKKLDANKKTYEDAKLSMGEKMDDLNSSIVSLLQELSTLQSVAENTQSSIVQMTSEIKNLDFAKQNLATSMTMLKRLQMLVTAYEKLRTLRQNQKFGEAISLMQATLQLLNFFKKYRSVERIASLSRSISEFQKSFYEQVFDTFQSQFKKESGMRGGFSPSSVQYLNELCRFIDIFAGDPPESVIRWYCRHQLEDFMKVFRENEEAGSLENLPRRYTWFKKLLQTYDQLHKPIFPPHWKVDFRLYEVFCEETKNDLSKLLKDDRLSLQVFVASLEQTLEFESFIDHRFYNTKSRFNSNFEPKERQAYNALSSVFEPHYTLYFNQQSQEFSILFENFALEKQTSTDESSQVLSSSIKLFQAYRKTLTQFVRLTRSSPLVGLKNLFIKWLRRYTQVELLDYQESSTFKDIAIRLNTAEYIYRTTIELEKRFQEISNKEFKDKMSFSEVLEVISSSRGTLLKFATGKFENVLNSDLEPLSKMDLKNIETVGDQSSYVGGAVQNMTAKASEFLSVVDLNMFARNFCDRSCESFTRQFLNAIYLAKPISEVGAEQLLLDLYSFKNALLKLPDLKQDYSITDSYINHLTIFMGYIETVLKTLLTPASPKAGFIQSYIFLVKDRSVTNFTVLLELKGVGKSDISSFLQQFSDFVKKTPQLEESSPIFKYLTINTAVEQAATRSRLSLDLAPESSRTLQNLGRLFTSKKKHV | Function: Involved in retrograde transport from early and late endosomes to late Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 87506
Sequence Length: 756
Subcellular Location: Cytoplasm
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P47061 | MLEGTVDYDPLEDITNILFSKESLNNIDELISITRSYKKQLQEDILKEENELKEHPKNSAEIEASLRKVFQDFKETQDVSASTELTISNLTEGISYLDIAKKNLTHSLTLFQNLKILTDSYIQCNELLSQGSFKKMVSPYKIMCSLAENTFISYKSLDEINYLLSSISRLKGDTLSKIKQNYNALFSGGNISEHDTALTMELREGACELLDCDTSTRAQMIDWCLDKLLFEMKEIFRVDDEAGSLENLSRRYIYFKKILNNFNSKFADYFLKDWEMAVRLTTTFYHITHKDLQTLLKREFKDKNPSIDLFMTALQSTLDFEKYIDVRFSKKIKEPKLSSCFEPYLTLWVSHQNQMMEKKFLSYMSEPKYPSNETESLVLPSSADLFRTYRSVLTQTLELIDNNANDSILTSLANFFSRWLQTYSQKILLPLLLPDNIEVQDKLEAAKYTVLLINTADYCATTIDQLEDKLSEFSGNREKLANSFTKTKNIYDDLLAKGTSFLLNRVIPLDLNFVWREFINNDWSNAAIEDYSRYMVTLKSVLKMPALTDASIKQQQEQPSTLAFILSQFNRDVYKWNFLDKVIDIITTNFVSNTIRLLQPVPPFSLAGSKRKFETRTVVNIGEQLLLDLELLKEIFHTLPESVSNDSDLRENTSYKRVKRHADNNIDQLLKFIKLLMAPLDSADDYYETYSKLTNNNPDSAVWSFVLALKGIPWDLALWKKLWSAYNLETDDTDEGSRPDSNRDLFIFKWDKVLLGQFENNLARMQDPNWSKFVRQDLKISPPVMKRIVSTPQIQQQKEEQKKQSLSVKDFVSHSRFFNRGT | Function: Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 95449
Sequence Length: 822
Subcellular Location: Golgi apparatus
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Q9M8L3 | MSHQQPPSYATEPNTMFVQADPSNFRNIVQKLTGAPPDISSSSFSAVSAAHQKLPLTPKKPAFKLHERRQSSKKMELKVNNITNPNDAFSHFHRGFLVSPVSHLDPFWARVSPHSAREEHHAQPDKEEQKAIAEKGFYFLPSPRSGSEPAPELLPLFPLRSPNGTNHRIHEDNHRDS | Function: May modulate WRKY transcription factor activities.
PTM: Phosphorylated on serine residues by MPK6.
Sequence Mass (Da): 19925
Sequence Length: 177
Subcellular Location: Nucleus
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O23660 | MEKSPRYRDKAKNLLPSPSSCTTTPTRYVKDDMYETTFIRTDPSSFKQVVQLLTGIPKNPTHQPDPRFPPFHSIPPIKAVTNKKQSSSFRLSERRNSMKHYLNINPTHSGPPEILTPTILNFPALDLSPDTPLMSDPFYRPGSFSQSPSDSKPSFDDDQERSIKEKGFYLRPSPSTTPRDTEPRLLSLFPMTPIHSPAPSPHDH | Function: May modulate WRKY transcription factor activities.
PTM: Phosphorylated on serine and threonine residues by MPK6.
Sequence Mass (Da): 23115
Sequence Length: 204
Subcellular Location: Nucleus
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Q9FNP0 | MNSKGSQNVATTCKPVTTFVQTDTNTFREIVQRLTGPTENNAAAATPEATVIKTAIQKRPTSKLHERRQCMRPKLEIVKPPLSFKPTGTTPSSKSGNTNLLTSPVGTPSSLFSNLSLIEGEPDSCTTNIEEEEKAIKERRFYLHPSPRSKPGYTEPELLTLFPLTSPNSSGKP | Function: May modulate WRKY transcription factor activities.
PTM: Phosphorylated on serine and threonine residues by MPK6.
Sequence Mass (Da): 18899
Sequence Length: 173
Subcellular Location: Nucleus
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Q9FHZ3 | MEVSTSSMSSKPEQMQNPPPMISSPRFQPQIISPHHHDQHQHLSNPYPTTFVQADTSTFKQVVQMLTGSSTDTTTGKHHEAPSPVNNNNKGSSFSIPPIKKTNSFKLYERRQNNNNMFAKNDLMINTLRLQNSQRLMFTGGNSSHHQSPRFSPRNSSSSENILLSPSMLDFPKLGLNSPVTPLRSNDDPFNKSSPLSLGNSSEEDKAIADKGFYLHPSPVSTPRDSQPLLLPLFPVASPARNS | Function: May modulate WRKY transcription factor activities.
PTM: Phosphorylated on serine and threonine residues by MPK6.
Sequence Mass (Da): 26919
Sequence Length: 243
Subcellular Location: Nucleus
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Q86917 | MNYTLSTVSSATMYNSSSNITTIATTIISTILSTISTNQNNVTTPSTYENTTTISNYTTAYNTTYYSDDYDDYEVSIVDIPHCDDGVDTTSFGLITLYSTIFFLGLFGNIIVLTVLRKYKIKTIQDMFLLNLTLSDLIFVLVFPFNLYDSIAKQWSLGDCLCKFKAMFYFVGFYNSMSFITLMSIDRYLAVVHPVKSMPIRTKRYGIVLSMVVWIVSTIESFPIMLFYETKKVYGITYCHVFYNDNAKIWKLFINFEINIFGMIIPLTILLYCYYKILNTLKTSQTKNKKAIKMVFLIVICSVLFLLPFSVTVFVSSLYLLNVFSGCMALRFVNLAVHVAEIVSLCHCFINPLIYAFCSREFTKKLLRLRTTSSAGSISIG | Function: Putative chemokine receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43421
Sequence Length: 381
Subcellular Location: Host cell membrane
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Q5M750 | MENSPRYREATNLIPSPRCHNSNNSCGMSSSSESNKPPTTPTRHVTTRSESGNPYPTTFVQADTSSFKQVVQMLTGSAERPKHGSSLKPNPTHHQPDPRSTPSSFSIPPIKAVPNKKQSSSSASGFRLYERRNSMKNLKINPLNPVFNPVNSAFSPRKPEILSPSILDFPSLVLSPVTPLIPDPFDRSGSSNQSPNELAAEEKAMKERGFYLHPSPATTPMDPEPRLLPLFPVTSPRVSGSSSASTS | Function: Acts as negative regulator of WRKY33 transcription factor activity in the promotion of defense gene expression. Acts as a negative regulator of pathogen-associated molecular pattern (PAMP)-induced responses to modulate resistance to pathogens.
PTM: Phosphorylated on serine and threonine residues by MPK6 following treatment with the pathogen-associated molecular pattern (PAMP) flg22. MAP kinase-mediated phosphorylation after PAMP elicitation causes degradation of VQ4, allowing WRKY33 to promote transcription from defense genes.
Sequence Mass (Da): 26863
Sequence Length: 247
Subcellular Location: Nucleus
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P0DKX3 | VIGGDICNINEHNFLVALYE | Function: Thrombin-like snake venom serine protease that coagulates human plasma and bovine fibrinogen by hydrolysis of the alpha chains (FGA) (minimum coagulation dose is 60 ug on fibrinogen). Has fibrinogenolytic activities, and degrades preferentially the Aalpha chain (FGA). Shows amidolytic activity toward N-benzoyl-L-Arg-p-nitroanilide, has a higher activity than Cdc SI. In vivo, intravenous injection induces defibrin(ogen)ation and a loss of the righting reflex and opisthotoxins, together with a typical gyroxin-like effect (18-20 minutes). Subcutaneous injection into the footpads induces moderate edema. Potentiates local hemorrhagic activity induced by metalloproteinases (BaP1).
Sequence Mass (Da): 2234
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.21.-
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P0C590 | VIGGDECNINEHRFLVAXY | Function: Thrombin-like snake venom serine protease that cleaves alpha-chain of fibrinogen (FGA) releasing fibrinopeptide A. Has high clotting activity.
PTM: N-glycosylated.
Sequence Mass (Da): 2161
Sequence Length: 19
Subcellular Location: Secreted
EC: 3.4.21.-
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P0C578 | VVGGDECNINEHRFLVALYY | Function: Thrombin-like snake venom serine protease. Releases both fibrinopeptides A and B from fibrinogen (FGA and FGB) to form fibrin clots.
PTM: Glycosylated.
Sequence Mass (Da): 2312
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.21.-
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Q9PTU8 | MVLIRVIANLLILQLSNAQKSSELVIGGDECNITEHRFLVEIFNSSGLFCGGTLIDQEWVLSAAHCDMRNMRIYLGVHNEGVQHADQQRRFAREKFFCLSSRNYTKWDKDIMLIRLNRPVNNSEHIAPLSLPSNPPSVGSVCRIMGWGTITSPNATFPDVPHCANINLFNYTVCRGAHAGLPATSRTLCAGVLQGGIDTCGGDSGGPLICNGTFQGIVSWGGHPCAQPGEPALYTKVFDYLPWIQSIIAGNTTATCPP | Function: Snake venom serine protease that has a potent and selective fibrinogenolytic activity. Preferentially cleaves the alpha-chain (FGA) of human and rat fibrinogen at Arg-|-Gly bonds, and slowly digests the beta-chain (FGB) . In vivo, completely avoids thrombus formation induced in rat, decreases the fibrinogen plasma level and prolonges the recalcification time. Possesses esterolytic and amidolytic activities.
PTM: N- and O-glycosylated. The glycosylation has a stabilizing effect on the protein . However, the removal of part of the carbohydrates enhances the proteolytic activity of the SVSP towards human and rat fibrinogen .
Sequence Mass (Da): 28058
Sequence Length: 258
Subcellular Location: Secreted
EC: 3.4.21.-
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C0HK19 | WDKDIMLIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRPHCANINLLDYEVCRTAHPQFRLPATSRILCAGVLEGGIDTCHR | Function: Thrombin-like snake venom serine protease.
Sequence Mass (Da): 8964
Sequence Length: 81
Subcellular Location: Secreted
EC: 3.4.21.-
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Q6UX27 | MTAEFLSLLCLGLCLGYEDEKKNEKPPKPSLHAWPSSVVEAESNVTLKCQAHSQNVTFVLRKVNDSGYKQEQSSAENEAEFPFTDLKPKDAGRYFCAYKTTASHEWSESSEHLQLVVTDKHDELEAPSMKTDTRTIFVAIFSCISILLLFLSVFIIYRCSQHSSSSEESTKRTSHSKLPEQEAAEADLSNMERVSLSTADPQGVTYAELSTSALSEAASDTTQEPPGSHEYAALKV | Function: Behaves as a cytokine, promoting IL17A secretion by CD4+ T-cells, and differentiation and activation of IL17 producing helper T-cells (TH17).
PTM: Isoform 2 is N-glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26109
Sequence Length: 236
Domain: Contains 2 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. Both motives are required for full inhibition of FCER1A-mediated degranulation.
Subcellular Location: Membrane
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Q8IW00 | MRLLALAAAALLARAPAPEVCAALNVTVSPGPVVDYLEGENATLLCHVSQKRRKDSLLAVRWFFAHSFDSQEALMVKMTKLRVVQYYGNFSRSAKRRRLRLLEEQRGALYRLSVLTLQPSDQGHYVCRVQEISRHRNKWTAWSNGSSATEMRVISLKASEESSFEKTKETWAFFEDLYVYAVLVCCVGILSILLFMLVIVWQSVFNKRKSRVRHYLVKCPQNSSGETVTSVTSLAPLQPKKGKRQKEKPDIPPAVPAKAPIAPTFHKPKLLKPQRKVTLPKIAEENLTYAELELIKPHRAAKGAPTSTVYAQILFEENKL | Function: Peptide Lv enhances L-type voltage-gated calcium channel (L-VGCC) currents in retinal photoreceptors.
PTM: Proteolytically cleaved to generate a bioactive peptide.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 36146
Sequence Length: 320
Subcellular Location: Secreted
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T1NXB5 | MRLRLLALAAAVLLGPAPEVCGALNVTVSPGPVVDYLEGENATLLCHVSQKRRKDSLLAVRWFFAPDGSQEALMVKMTKLRIIQYYGNFSRTANQQRLRLLEERRGVLYRLSVLTLRPTDQGQYVCKVQEISKHRNKWTAWSNGSSATEMRVISLKAGEDSSFEKKKVTWAFFEDLYVYAVLVCCVGILSVLLFTLVIAWQSVFHKRKSRVRHYLVKCPQNSSGETVTSVTSLAPLQPQKGKRQKKKVDVPPAVPAKAPIATTFHKPKLLKPQRKVALPKITEENLTYAELELIKPHRAAKGVPTSTVYAQILFEENQL | Function: Peptide Lv enhances L-type voltage-gated calcium channel (L-VGCC) currents in retinal photoreceptors.
PTM: Proteolytically cleaved to generate a bioactive peptide.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35899
Sequence Length: 319
Subcellular Location: Cell membrane
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A8MXK1 | MRPLPSGRRKTRGISLGLFALCLAAARCLQSQGVSLYIPQATINATVKEDILLSVEYSCHGVPTIEWTYSSNWGTQKIVEWKPGTQANISQSHKDRVCTFDNGSIQLFSVGVRDSGYYVITVTERLGSSQFGTIVLHVSEILYEDLHFVAVILAFLAAVAAVLISLMWVCNKCAYKFQRKRRHKLKESTTEEIELEDVEC | Function: Cell adhesion-like membrane protein of the central nervous system (CNS) which modulates both the position and complexity of central neurons by altering their membrane morphology and dynamics. Involved in the formation of neuronal dendrites and protrusions including dendritic filopodia. In synaptogenesis, regulates synapse formation by altering dendritic spine morphology and actin distribution. Promotes formation of unstable neuronal spines such as thin and branched types. Regulates neuronal morphogenesis and migration during cortical development in the brain.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 22377
Sequence Length: 200
Subcellular Location: Cell membrane
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Q9D806 | MRPLRCGERTQGIPLGLLAFWVTAARCLQSQGVSLYIPQSAINATVQQDILLSVDYICHGVPTIEWKYTPNWGVQRIVEWKPGTPANVSQSHRDRVCTFDNGSIQLFNVSVKDSGYYIVTVTEHPGSSQSGTILLRVSEIRYEDLHFVAVFFALLAAVAVVLISLMWVCNQCAYKFQRKRRYKLKESTTEEIEMKEVEC | Function: Cell adhesion-like membrane protein of the central nervous system (CNS) which modulates both the position and complexity of central neurons by altering their membrane morphology and dynamics. Involved in the formation of neuronal dendrites and protrusions including dendritic filopodia. In synaptogenesis, regulates synapse formation by altering dendritic spine morphology and actin distribution. Promotes formation of unstable neuronal spines such as thin and branched types. Regulates neuronal morphogenesis and migration during cortical development in the brain.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 22564
Sequence Length: 199
Subcellular Location: Cell membrane
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P60980 | MKTSVFVLVLGLVLLFAVSFATEMEESARECGKFMWKCKNSNDCCKDLVCSSRWKWCVLASPF | Function: Inhibits sodium channels Nav1.7/SCN9A and potassium channels Kv11.1/KCNH2. Also binds the voltage-sensor domain of the potassium channel KvAP (from the archaeon Aeropyrum pernix) with very slow apparent binding kinetics and affects channel gating. Reaches its target by dynamically partitioning into anionic or zwitterionic headgroup lipid membranes. May bind to the open state of KvAP.
Sequence Mass (Da): 7175
Sequence Length: 63
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P20946 | MSVLFLLLAITRTASVKAAEGDQAADFLPLCEAWQATKALANAAYKLPPFPPDLTDILNFNITVAPEEWKAIFTDGGSDNTWERFAEGHKNTLNGGNWKTRWEHIKQARQDTKEASSPWNALNSKLINTATVNTTRAYIASIADEAFDLYQGTQTPLQTPKALEAASLAEAAKAILCSDPLKPTADGQACTDITATPSKAATCPTGRSSKGGAPIGLDTVCLCSTNKPSMHSRRRKAAAVMTDGQLKDGILKKLLAACPKKPTLNEPAAAARHAVTVLATRLAQKVARAEEGQIILGTRAETDCASSGSACVEYTNFFKDGDGLAAVPWVKKLLAAADFYDTIEKRKESDKNAATAIAALKSALIREFRRPGQEQTLATTGTKSSSPQSTQQKASEAEANCNDKAKETECNSPCKWDKEEKDEKKRCKLSEEGKQAEKENQEGKDGKANTTGSSNSFVIKTSPLLLAVLLL | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 50537
Sequence Length: 471
Subcellular Location: Cell membrane
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P20947 | MWIILALLTLAGSRVAHGAGKNVNGVEFNLFCHIANMLNAEKIEDDKTDGLDRQAAEAWTAIDSIFTVTANESYYSEGPASAANTTDENQDAKPERVAKWVQKRNQIDKIAAPGNEKNGKYARRPRDRMSAATGAKLDTVFTLASEARVRLMQIDTEIATNKQEIRQQLGLHCSEGQGKGQSRNQHPDNAAFASDYSTACKGSTGPGKSLANDLVCICSTDTSQAQSTLQMCTSIDDANSLFSTLHKRSQCQGDFPCPHRVCAKTAETSELTETNINNCVTAFTATLGRHTKSSATNEGAYVFGSGQNSGDECNGGAATGQSCVSYHDLITAKSGTTLSGAITRLKQLQIAKAKLKARRLLLQNRERQQTRLMALADKMQELYQEALHDEVQLRKEAQNKPQETPDSDKQKACEKYHNKSKECKENGCQWSGTEETIGKCEAKPKAGTEAATTGPGERDAGATANTTGSSNSFVIKTSPLLFAFLLF | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 52724
Sequence Length: 487
Subcellular Location: Cell membrane
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O42250 | MTGREEATDEKPKVKLYPSFGIDKSRLNGSGFRSKGFAITDLLGLESELQPHQSGPGAGPNGEGQSAAVGGFSFPGGSLPLGLGFLCSLAAQQPPGAPCFLPSHIPLLQSRTESHFMQNLEQQRDVYSDDDCLSGDRNDGKNSGNSQKRKKRRHRTVFTSHQLEELEKAFNEAHYPDVYAREMLAMKTELPEDRIQVWFQNRRAKWRKREKCWGRSSVMAEYGLYGAMVRHSIPLPESIINSAKSGMMGSCAPWLLGEPAGMHKKSMEIVKKAPGTPESTHSDTYSEEHKGKDSDTTWSSGANGADDSEDMAIDLSSTSKQENKSTLKRSPPRTENSSDSENES | Function: May be involved in maintenance as well as cellular differentiation of retinal interneurons, such as bipolar cells. May play a role in establishing interneuronal cell classes in nonsensory as well as sensory systems.
Sequence Mass (Da): 37872
Sequence Length: 344
Domain: The NLS interacts with UBE2I.
Subcellular Location: Nucleus
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P80012 | MFPTRLARLLLAVALTLPGALCGEGALGKSSMARCSLFGADFINTFDESMYSFSGDCSYLLAGDCKTHSFSIVGDFQGGRRMGLSVYLGEFFDIHVFVNGTVLQGGQHVSMPYATRGLYLETEVGHHKLSSESYGFVARIDGSGNFQILLSDRHFNKTCGLCGDFNIFAEDDFRTQEGTLTSDPYDFANSWALSSEEQRCPRVSPPSSSCNVSSELQKGLWEKCQLLKTASVFARCHALVDPEPFVALCERMLCACAQGLRCPCPVLLEYARACAKQGMLLYGWADHSSCRPDCPTGMEYKECVSPCHRTCRSLSITEVCREQCVDGCSCPEGQLLDEGRCVESTECPCVHAGKPYPPGASLSRDCNTCICRNSQWVCSNEDCPGECLITGQSHFKSFDDRHFTFSGVCQYLLAQDCQDHSFSVVIETVQCADDPDAVCTRSVTVRLPSPHHGLLKLKHGGGVALDGQDVQIPLLQGDLRIQHTVTASLQLNFGEDLQIDWDGRGRLLLKLSPVYAGRTCGLCGNYNGNQRDDFLTPAGLVEPLVEHFGNSWKLRADCEDLQEQPSDPCSLNPRLTKFADQACAILTSPKFEACHSAVSPLPYLRNCRYDVCACSDGRDCLCDAVANYAAACARRGVHVGWREPSFCALSCPHGQVYQQCGTPCNLTCRSLSHPDEECTEVCLEGCFCPPGLFLDETGSCVPKAQCPCYYDGEIFQPEDIFSDHHTMCYCEDGFMHSATSGAPGSLLPEAVLSSPLSHRSKRSLSCRPPMVKVVCPADNPRAEGLECTKTCQNYDLECMSTGCVSGCLPAPGMVRHENRCVALERCPCFHQGREYAPGDRVKVDCNSCVCQDRKWNCTDHVCDASCSALGLAHYFTFDGLKYLFPGECQYVLVQDHCGSNPGTFRVLVGNEGCSVPSLKCRKRITILVEGGEIELFD | Function: Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma.
PTM: All cysteine residues are involved in intrachain or interchain disulfide bonds.
Sequence Mass (Da): 102599
Sequence Length: 937
Domain: The propeptide is required for multimerization of vWF and for its targeting to storage granules.
Subcellular Location: Secreted
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P0CW96 | MASPVTVLENPIPKSGQHLLFFLTSKQQLALEQRPIESSLGYSAYVDHGVSQGVIVNPSSIAAAMRSSLITVYGITKPGTDKQYISVISPTYNLIANRQNQPIETTQKALAACSDNDRNNWVYYLNLPQGTAQYAIYELNIQDSTSAPTVYSGPTPSGNSNLAAVYFSPNKDRFIIFSNTDTRHYLYWVNSTLQSANRIAGTGSVMSASPLAATTITNVQTRSMTIFLYYMDVNTLLNRIVGKVTDNEIHWYANQVVEGAPPMKVDTLLTGVVVEEKWNCLYYIPDGDTEFRAFNDTIRDSFFDEPREG | Function: May participate in wall plasticization and/or intussusception or in cell wall turnover.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34287
Sequence Length: 309
Subcellular Location: Secreted
EC: 3.4.21.-
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P01174 | MRCSISLVLGLLALEVALARNLQEHVFNSVQSMCSDDSFSEDTECINCQTNEECAQNDMCCPSSCGRSCKTPVNIEVQKAGRCPWNPIQMIAAGPCPKDNPCSIDSDCSGTMKCCKNGCIMSCMDPEPKSPTVISFQ | Function: Could be a protease inhibitor.
PTM: Contains 8 disulfide bonds.
Sequence Mass (Da): 14827
Sequence Length: 137
Subcellular Location: Secreted
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Q03631 | MDTQIAITGVAVGKEINNDNSKTDQKVSLPKADVPCIDKATQTIIEGCSKDDPRLSYPTKLETTEKGKTKRNSFACVCCHSLKQKCEPSDVNDIYRKPCRRCLKHKKLCKFDLSKRTRKRKPRSRSPTPFESPMVNVSTKSKGPTDSEESSLKDGTSYLASFPSDPNAKQFPNSRTVLPGLQQSLSDLWSTLSQPPSYGAREAETTSTGEITTNNHTKSNGSVPTNPAVLASNDEHTNISDAPVIYSTYNSPVPISSAPTSINSEALFKHRPKIVGDEETQNVKVKRQKKSYSRHMTRSFRKQLQSLIISQKGKIRDISMKLDTWSKQWNDLVEKSMFLPTIADPVSVGIISHEEATLRLHLYKTEISYLSKLPFIKVEENVSVDELRKKKPILFSVIMSCVSIVLTPKQTTRGTIMKLDSFVLNLITNQIFKANNKSIEIIESLSTLCLWYNFFEWSSKTRYHIFNYICCCLTRDLGPTYVNRSFGMFSDEDPKRFKSPLELYSNGASLTLLVYISALNISIFLRQSIQARWSHVTEKACEDLVKETKKSRHYDNDKLLLDSADDPILVQFAKMNHVLENIHTHLHERDLNDDEFDDPIFTKKYLNKLMEKYHKQLQEIFTKLDRNRPRVIAFYYSVEAYLYQYKLAVFIGEMSHTINEKVELPREIMDDFVKCYHCCKSALEEFSKLEPILITSLPLFHTSRIIYTVGMLLLKLRYSVVAIPSFHDLMPLTDDAIALVIGVNNLLEKTSELYPFNNSLYKFRYVIALFCQTYANKVIDVADRYNAEREKLKEKQVIDEVSNGHDGTKPINAYVTESQKMPTEEDPIIDNNTNQNITAVPDEMLPVYSRVRDDTAAMNLNINSTSYMNESPHEHRESMTGTTLLPPPFISNDVTNSADSTNIKPSPSSSVDNLNDYLTDINSLAWGVNSLNDEFWTDLFMNDI | Function: transcription factor which binds to a weak acid response element (WARE) to mediate stress induction of PDR12 and FUN34, encoding an acid transporter and a putative ammonia transporter, respectively.
PTM: Phosphorylation is required for PDR12 induction.
Sequence Mass (Da): 107561
Sequence Length: 944
Subcellular Location: Nucleus
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Q8IWB7 | MAAEIHSRPQSSRPVLLSKIEGHQDAVTAALLIPKEDGVITASEDRTIRVWLKRDSGQYWPSIYHTMASPCSAMAYHHDSRRIFVGQDNGAVMEFHVSEDFNKMNFIKTYPAHQNRVSAIIFSLATEWVISTGHDKCVSWMCTRSGNMLGRHFFTSWASCLQYDFDTQYAFVGDYSGQITLLKLEQNTCSVITTLKGHEGSVACLWWDPIQRLLFSGASDNSIIMWDIGGRKGRTLLLQGHHDKVQSLCYLQLTRQLVSCSSDGGIAVWNMDVSREEAPQWLESDSCQKCEQPFFWNIKQMWDTKTLGLRQHHCRKCGQAVCGKCSSKRSSYPVMGFEFQVRVCDSCYDSIKDEDRTSLATFHEGKHNISHMSMDIARGLMVTCGTDRIVKIWDMTPVVGCSLATGFSPH | Function: Positively regulates TLR3- and TLR4-mediated signaling pathways by bridging the interaction between TLR3 or TLR4 and TICAM1. Promotes TLR3/4 ligand-induced activation of transcription factors IRF3 and NF-kappa-B, as well as the production of IFN-beta and inflammatory cytokines .
Sequence Mass (Da): 46324
Sequence Length: 410
Domain: The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched membranes is substantially increased in acidic conditions. The FYVE domain is required for its function in regulating TLR3 signaling .
Subcellular Location: Early endosome
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Q96P53 | MAAEIQPKPLTRKPILLQRMEGSQEVVNMAVIVPKEEGVISVSEDRTVRVWLKRDSGQYWPSVYHAMPSPCSCMSFNPETRRLSIGLDNGTISEFILSEDYNKMTPVKNYQAHQSRVTMILFVLELEWVLSTGQDKQFAWHCSESGQRLGGYRTSAVASGLQFDVETRHVFIGDHSGQVTILKLEQENCTLVTTFRGHTGGVTALCWDPVQRVLFSGSSDHSVIMWDIGGRKGTAIELQGHNDRVQALSYAQHTRQLISCGGDGGIVVWNMDVERQETPEWLDSDSCQKCDQPFFWNFKQMWDSKKIGLRQHHCRKCGKAVCGKCSSKRSSIPLMGFEFEVRVCDSCHEAITDEERAPTATFHDSKHNIVHVHFDATRGWLLTSGTDKVIKLWDMTPVVS | Function: Acts in an adapter protein-like fashion to mediate the interaction between the kinase PRKCZ and its substrate VAMP2 and increases the PRKCZ-dependent phosphorylation of VAMP2 . Positively regulates adipocyte differentiation, by facilitating the phosphorylation and thus inactivation of the anti-adipogenetic transcription factor FOXO1 by the kinase AKT1 . Plays a role in endosomal control of AKT2 signaling; required for insulin-stimulated AKT2 phosphorylation and glucose uptake and insulin-stimulated phosphorylation of AKT2 substrates (By similarity). Participates in transferrin receptor endocytosis .
Sequence Mass (Da): 45154
Sequence Length: 400
Domain: The FYVE-type zinc finger is essential for its vesicular localization.
Subcellular Location: Endosome
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Q7XXR3 | MLGFAPAPGRPLFVLFGSSIVQFSFSNGGWGAALADIYARKADILLRGYIGWNSRRALQVIDKIFPKDSPVQPSLVIVYFGGNDSVAAHSSGLGPHVPLEEYIDNMRKIADHLKSLSEKTRVIFLSCPPLNEETLRKSTSTVLSEIVRTNETCRLYSEACVSLCKEMDLKVVDLWNAMQKRDDWATACFTDGLHLSEEGSKIVVEEILRILKEAEWDPCLHWKAMPTEFGEDSPYDLVSSSGQSTVNPSDWTFHRTIQWD | Function: Involved in the organization of leaf cuticle and wax crystals.
Sequence Mass (Da): 29115
Sequence Length: 260
Subcellular Location: Endoplasmic reticulum
EC: 3.1.1.-
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Q5FWK6 | MAGAIIENMSTKKLCMVGVALLLLQVLAFLVGGLIAPKPTTYVNPVAMKCIDVRKSHRSSKWLMPWGTEPCKSIQSFDEAANRLIEANDIVFAAHIPNSQFEMSPWFQFMLVVLQLDIAFKLNNYIEDHSMVTLDVAVAYRDDLKEEWKELARSVEQRKLNCILPVDKTVANEGRHYDCDVIPLMELGSVSHKYYLFNIRLPVNERQKMNIGIGEIRDMHVVSIFQNGGFTMVWFAMKTFLTPCIIIIMIWYWRRITMMTRSPVLLEKVIFALGISMTFINIPVEWFSIGYDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQAERNRISIYWKQVGPIAFGSCCLFIFDMCERGVQLKNPFYSIWTTDVGAEIAMAFIIVAGICACLYFLFLCFMVYQVFRNISGKRSNLPAMSKARRLHYEGLIFRFKFLMIITLACAALTVVFFITTQITEGNWKLGDLSIELNSAFFTGIYGMWNLYVFALMFLYAPSHKHYGDGQSNDGAGMSSGEELQLTTTITHIDGPTELYRLAGKEAQE | Function: Required for a subset of Wnt-dependent developmental processes, in particular, eye and pronephros development. Regulates the secretion of wnt4, which is required for eye development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62001
Sequence Length: 541
Subcellular Location: Golgi apparatus membrane
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Q7YWX7 | MAGGAVIENLSNRKLFVIFAGLLVIQIMFFLIGAWYAPSPSSYMEFEMITCRDETKGLSGEWIHRDNCQQISELSEYTPSSFDLREIVFIAKMPHTRDGIELEYSPWFQFLLGVLHVDVEYSEHFKYVAHAPLELEVRMGYRDKESKKNEWKELVTSNVTRILECTIAEDEKKAGGTYDCDMLDLFELGSSSYPFYLINIRIPINQQACQFDNKSANCQIGKLTGLRLIEIHQNGGFTLVWLWTKTFMTPVVAICLWWYYNRINQLARNPLLLERAILLLGLSLVILDFPIEWISLTYRIPFLLLISDLRQGLFYTVLFSFWLIFAGEHLIDDNTRNNLKSYRFNLSFIITASLGLLIYDLIERGIQLYDPFYSVWSSPTGSQIAYFAIFISAISTVAYFIFLFFKIARVWSTIKSKRSAQIYQTSENRRLKVEGVIYRFKFLMLFTLLCSAFTIAAYFMKQYGEAQLHGDEARDGFLTGSTSAFFTGAFGMCNIYVLLLLAMYAPSHKHYRGASQLIDENDDDEIMEDPSNQHTESNAMTTFLKPSTD | Function: Probable sorting receptor which regulates endocytosis and secretion of the wnt ligand egl-20 . Recycling of mig-14 from the plasma membrane to the Golgi apparatus by the retromer complex is essential for its function . Its endosomal trafficking is regulated by its association with sorting nexin snx-3 on early endosomes and the mtm-6/mtm-9 myotubularin complex . Required in embryonic development for endoderm specification and the correct positioning and orientation of the mitotic spindles and division planes in blastomere cells . Functions during vulval development, playing a role in vulval precursor cell fate specification . During development, specifically regulates the migration of HSN neurons, the left Q neuroblast (QL) and its descendants and the distal tip cells of the gonads . Positioning of Q neuroblasts may be both dependent and independent of hox gene mab-5 . Involved in establishing ALM and PLM neuronal cell polarity .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63306
Sequence Length: 549
Subcellular Location: Cell membrane
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Q5ZLR1 | MAGAIIENMSTRKLCIVGGILLVFQVIAFLVGGLIAPSPTTAVPYMSVKCIDVRKNHHKTKWLMPWGPNHCEKLKDFDEAVSRQIEANDIVFAVHIPLPSKEMSPWFQFMLFIMQLDIAFKMDNDLKENAEITLDVSLAYRDDMFNDWEEIAHAIEIRKLKCTFGSPKTLESEGRHYDCDFLPFMEIGSVAHKYYLINIRLPVNERKGINVGIGEVKDIRLVGIHQNGGFTKVWFAMKTFLTPSILIIMVWYWRRITLMTRAPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQNERNRLSGYWKQVGPIAVGSFCLFIFDMCERGVQLKNPFYSIWTTEVGTELAMAFIIVAGICLCLYFLFLCFMVFQVFRNISGKQSSLPAMSKARRLHYEGLIFRFKFLMLITLACAAMTVIFFIVSQVTEGHWKWGDITIQVNSAFFTGIYGMWNLYVFALMFLYAPSHKNYGEDQSNGDLGVSSGEELQLTTTITHVDGPTEVYKLARKEAQE | Function: May play an essential role in Wnt signaling pathway. May be required for Wnt-dependent patterning processes (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62137
Sequence Length: 541
Subcellular Location: Golgi apparatus membrane
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B4J2W3 | MSGTILENLSGRKLSILVSSLMLCQVVCFLMGGLFAPVPAGHQTVLGSKCRDVPGRQNDTSFFLYSRGNGACKSLQDIDIEQDELKMANQLVYVFQMPLPRDNNTLQYSRWQQNLIGVLQVDIAYDSASELREPPKELQLTIDTRLAYRNQKDADTDWKLYAHSVEQRYLDCHASHVGRLETLYTCDIIPLFELGALHHNFYLLNLRFPMDTPKQMNLQFGHMHDLTLTAIHQNGGFTQVWLVLKTLLFPFVIGIMMWFWRRVHILQRSPALLEYMLFYLGGALSFLNLPLELLTLGVEMPYMLLLSDVRQGIFYAMLLSFWLVFAGEHMLIQDSPSKSTIRSRYWKHLSAVVVGCISLFVFDICERGVQMRNPFYSIWTTPLGAKVAMSFIVLAGVSAAIYFLFLCFMVWKVFKDIGDKRTSLPSMSQARRLHYEGLIYRFKFLMLATLLCAGLTVAGFIMGQMAEGHWKWNENIEIQLTSAFLTGVYGMWNIYIFALIILYAPSHKQWPTMRHSDETTQSNENIVASAASEEIEFSNLPSDSNPSEISSLTSFTRKVAFD | Function: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64187
Sequence Length: 562
Subcellular Location: Presynaptic cell membrane
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Q95ST2 | MSGTILENLSGRKLSILVATLLLCQVLCFLLGGLYAPLPAGHVTVLGSLCREDHARQNDTSFLLYSRGAGACIPVTREEVEQDSTKMANELVHVFQMPLPRDLRDLDYSRWQQNLIGVLQVEFGYDSSSELREPPRELQLTIDMRLAYRNKGDPDNGWKLYAHGVEHRYLDCVTSHVGPTETLYSCDMIPLFELGALHHSFYLLNLRFPLDTPSQMNLQFGHMHDLTLTAIHQNGGFTQIWLLLKTMLFPFVVGIMIWFWRRVHLLQRSPALLEYMLIYLGAALTFLNLPLEYLSLVYEMPYMLLLSDIRQGIFYAMLLTFWLVFAGEHMLIQDAPNKSTIRSRYWKHLSAVVVGCISLFVFDICERGVQLRNPFYSIWTTPLGAKVAMTFIVLAGVSAAIYFLFLCYMIWKVFRNIGDKRTSLPSMSQARRLHYEVPLDQKVEDWAGIVYFYTKAFFFQLHKANESKGLIYRFKFLMLATLVCAALTVAGFIMGQMAEGQWDWNDNVAIQPTSAFLTGVYGMWNIYIFALLILYAPSHKQWPTMHHSDETTQSNENIVASAASEEIEFSHLPSDSNPSEISSLTSFTRKVAFD | Function: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67890
Sequence Length: 594
Subcellular Location: Presynaptic cell membrane
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Q5T9L3 | MAGAIIENMSTKKLCIVGGILLVFQIIAFLVGGLIAPGPTTAVSYMSVKCVDARKNHHKTKWFVPWGPNHCDKIRDIEEAIPREIEANDIVFSVHIPLPHMEMSPWFQFMLFILQLDIAFKLNNQIRENAEVSMDVSLAYRDDAFAEWTEMAHERVPRKLKCTFTSPKTPEHEGRYYECDVLPFMEIGSVAHKFYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRITMMSRPPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQHERNHIAGYWKQVGPIAVGSFCLFIFDMCERGVQLTNPFYSIWTTDIGTELAMAFIIVAGICLCLYFLFLCFMVFQVFRNISGKQSSLPAMSKVRRLHYEGLIFRFKFLMLITLACAAMTVIFFIVSQVTEGHWKWGGVTVQVNSAFFTGIYGMWNLYVFALMFLYAPSHKNYGEDQSNGDLGVHSGEELQLTTTITHVDGPTEIYKLTRKEAQE | Function: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins . Plays also an important role in establishment of the anterior-posterior body axis formation during development (By similarity).
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62253
Sequence Length: 541
Subcellular Location: Golgi apparatus membrane
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Q6DID7 | MAGAIIENMSTKKLCIVGGILLVFQIVAFLVGGLIAPAPTTAVPYTAIKCVDVRKNHHKTRWLAPWGPNKCDKIRDIEEAIPREIEANDIVFSVHIPLPSMEMSPWFQFMLFILQLDIAFKLNNQIRENAEISMDVSLGYRDDMFSEWTEMAHERVPRKLKCTFTSPKTPEHEGRYYNCDVLPFMEIGSVAHKYYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRITMMSRPPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQHERNHIAGYWKQVGPIAVGSFCLFIFDMCERGVQLTNPFYSIWTTDVGTELAMAFIIVAGICLCLYFLFLCFMVFQVFRNISGKQSSLPAMSKVRRLHYEGLIFRFKFLMLITLACAAMTVIFFIVSQVSEGHWKWGGVTVQVSSAFFTGIYGMWNLYVFALMFLYAPSHKNYGEDQSNGDLGVHSGEELQLTTTITHVDGPTEIYKLTRKEAQE | Function: Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Also plays an important role in establishment of the anterior-posterior body axis formation during development.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62188
Sequence Length: 541
Subcellular Location: Golgi apparatus membrane
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P27467 | MAPLGYLLVLCSLKQALGSYPIWWSLAVGPQYSSLSTQPILCASIPGLVPKQLRFCRNYVEIMPSVAEGVKAGIQECQHQFRGRRWNCTTVSNSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGSAAICGCSSRLQGSPGEGWKWGGCSEDIEFGGMVSREFADARENRPDARSAMNRHNNEAGRQAIASHMHLKCKCHGLSGSCEVKTCWWSQPDFRTIGDFLKDKYDSASEMVVEKHRESRGWVETLRPRYTYFKVPTERDLVYYEASPNFCEPNPETGSFGTRDRTCNVSSHGIDGCDLLCCGRGHNARTERRREKCHCVFHWCCYVSCQECTRVYDVHTCK | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family . Required for normal embryonic mesoderm development and formation of caudal somites . Required for normal morphogenesis of the developing neural tube . Mediates self-renewal of the stem cells at the bottom on intestinal crypts (in vitro) .
PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and formation of large disulfide-bond oligomers, leading to inactivation of WNT3A.
Sequence Mass (Da): 39258
Sequence Length: 352
Subcellular Location: Secreted
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P28142 | SGSCEVKTCWWSQPDFRVIGDYLKDKYDSASEMVVEKHRESRGWVETLRPKYNFFKAPTERDLVYYENSPNFCEPNPETGSFGTRDRICNVTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCIF | Function: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family. Required for normal embryonic mesoderm development and formation of caudal somites. Required for normal morphogenesis of the developing neural tube.
PTM: Disulfide bonds have critical and distinct roles in secretion and activity. Loss of each conserved cysteine results in high molecular weight oxidized Wnt oligomers, which are formed through inter-Wnt disulfide bonding.
Sequence Mass (Da): 14296
Sequence Length: 123
Subcellular Location: Secreted
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P31285 | MGCFGYLLLIIGLHQVLATYPIWWSLAVGQQYSSLGTQPIPCGTIPGLVAKQMRFCRNYMEIMPSVAEGVKIGIQECQHQFRGRRWNCTTVNDNLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGSATICGCDTHHKGPPGEGWKWGGCSEDMDFGSMVSREFADARENRPDARSAMNRHNNEAGRTSILDHRHLKCKCHGLSGSCEVKTCWWSQPDFRVIGDYLKDKYDSASEMVVEKHRESRGWVETLRPKYTFFKPPIERDLIYYESSPNFCEPNPETGSFGTRDRECNVTSHGIDGCDLLCCGRGQNTRTEKRKEKCHCIFHWCCYVSCQECMRVYDVHTCK | Function: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family. Required for normal embryonic mesoderm development and formation of caudal somites. Required for normal morphogenesis of the developing neural tube.
PTM: Disulfide bonds have critical and distinct roles in secretion and activity. Loss of each conserved cysteine results in high molecular weight oxidized Wnt oligomers, which are formed through inter-Wnt disulfide bonding.
Sequence Mass (Da): 39715
Sequence Length: 352
Subcellular Location: Secreted
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P28134 | SGSCEVKTCWWAQPDFRAIGDYLKDKYDSASEMAVEKHRESRGWVETLRARYALFKPPTERDLVYYEGSPNFCEPNPETGSFGTKDRTCNVTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCIF | Function: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters.
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 14078
Sequence Length: 123
Subcellular Location: Secreted
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P28114 | SGSCEVKTCWVAQPDFRSIGDHLKDKYDSASEMVVEKHKEARGWVETLRPKYPLFKPPTDRDLIYYERSPNFCDPNSETGSFGTKDRVCNLTSHGIDGCDLLCCGRGHNTRTEKRKDKCHCVF | Function: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Required for normal embryonic development (By similarity).
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 14048
Sequence Length: 123
Subcellular Location: Secreted
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P28090 | SGSCEVKTCWMQTPHFKEVGDRLLVKYQNAKRVVARNSIGGGLGLANVPKKKRKRAPPPPEDQLVFLEDSPNFCNPDGEIGIFGTKDRYCNRTSDGADRCDTMCCGRGYNIKLERRTEWCYCQF | Function: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Required for normal embryonic development (By similarity).
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 14040
Sequence Length: 124
Subcellular Location: Secreted
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P56703 | MEPHLLGLLLGLLLGGTRVLAGYPIWWSLALGQQYTSLGSQPLLCGSIPGLVPKQLRFCRNYIEIMPSVAEGVKLGIQECQHQFRGRRWNCTTIDDSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGTSTICGCDSHHKGPPGEGWKWGGCSEDADFGVLVSREFADARENRPDARSAMNKHNNEAGRTTILDHMHLKCKCHGLSGSCEVKTCWWAQPDFRAIGDFLKDKYDSASEMVVEKHRESRGWVETLRAKYSLFKPPTERDLVYYENSPNFCEPNPETGSFGTRDRTCNVTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCIFHWCCYVSCQECIRIYDVHTCK | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family . Required for normal gastrulation, formation of the primitive streak, and for the formation of the mesoderm during early embryogenesis. Required for normal formation of the apical ectodermal ridge (By similarity). Required for normal embryonic development, and especially for limb development .
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 39645
Sequence Length: 355
Subcellular Location: Secreted
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P17553 | MEPHLLGLLLGLLLSGTRVLAGYPIWWSLALGQQYTSLASQPLLCGSIPGLVPKQLRFCRNYIEIMPSVAEGVKLGIQECQHQFRGRRWNCTTIDDSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGTSTICGCDSHHKGPPGEGWKWGGCSEDADFGVLVSREFADARENRPDARSAMNKHNNEAGRTTILDHMHLKCKCHGLSGSCEVKTCWWAQPDFRAIGDFLKDKYDSASEMVVEKHRESRGWVETLRAKYALFKPPTERDLVYYENSPNFCEPNPETGSFGTRDRTCNVTSHGIDGCDLLCCGRGHNTRTEKRKEKCHCVFHWCCYVSCQECIRIYDVHTCK | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Required for normal gastrulation, formation of the primitive streak, and for the formation of the mesoderm during early embryogenesis . Required for normal formation of the apical ectodermal ridge and for normal embryonic limb development .
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 39659
Sequence Length: 355
Subcellular Location: Secreted
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P49337 | MSPEYFLRSLLLIILATFSANASNWLYLAKLSSVGSISEEETCEKLKGLIQRQVQMCKRNLEVMDSVRRGAQLAIEECQYQFRNRRWNCSTLDTLPVFGKVVTQGTREAAFVYAISSAGVAFAVTRACSSGELDKCGCDRTVQGGSPQGFQWSGCSDNIAYGVAFSQSFVDVRERSKGASSNRALMNLHNNEAGRKAILNNMRVECKCHGVSGSCEFKTCWKAMPPFRKVGNVLKEKFDGATEVEQSEIGSTKVLVPKNSQFKPHTDEDLVYLDSSPDFCDHDLKNGVLGTSGRQCNKTSKAIDGCELMCCGRGFHTDEVEVVERCSCKFHWCCSVKCKPCHRVVEIHTCR | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Plays an important role in embryonic development (By similarity).
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 38963
Sequence Length: 351
Subcellular Location: Secreted
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P40589 | MPSPTGVFVLMILTHLSFGLGQVRNEDQLLMVGQNGDLDSSNPAIHHQQHQQHQQHQQHQQHQSNHNLNNGNMNSTILNTLMGNNAGQVVNSSPGGGGSMINQLGSSTSSVPSVIGGGVGSVGNPWHSAVGLGVPGNGMGLPSSHGLGGNMGSHPHGHALAGLAKLGIIVPGGQGLPGNLGYGGTMLNGGGVGGAAGMGLGIGSNTNNMDMQQGLYNEHFISEHTVMAVFTSQGQVGGPCRYMPATRRQNHQCRKETGLPGTLSEARRLATTHCEEQFRYDRWNCSIETRGKRNIFKKLYKETAFVHALTAAAMTHSIARACAEGRMTKCSCGPKKHNREAQDFQWGGCNDNLKHGKRVTRSFLDLRGGDGDEVSEILRHDSEVGIEAVSSQMMDKCKCHGVSGSCSMKTCWKKMADFNATATLLRQKYNEAIRKAPNQRSMRQVSSSRMKKPKQRRKKPQQSQYTTLYYLETSPSYCAVTKDRQCLHPDNCGTLCCGRGYTTQVVKQVEKCRCRFNNGRCCQLICDYCQRLENKYFCK | Function: Binds as a ligand to a family of frizzled seven-transmembrane receptors and acts through a cascade of genes on the nucleus. Acts downstream of homeotic complex genes in the visceral mesoderm and is required for embryonic segmentation. Also required for cell movement and FAK regulation during ovarian morphogenesis.
PTM: Palmitoleoylated by porcupine. The lipid group functions as a sorting signal, targeting the ligand to polarized vesicles that transport Wnt4 to unique sites at the cell surface. Depalmitoleoylated by notum, leading to inhibit Wnt signaling pathway.
Sequence Mass (Da): 58685
Sequence Length: 539
Subcellular Location: Secreted
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P28115 | SGSCEVKTCWRAMPPFRKVGNVIKEKFDGATEVEMQRIGTRKQLVPKNPQFKPHTDEDLVYISPSPDFCIRDMKAGVPGTAGRHCNRTSKALGGCELLCCGRGFHTAEAELVERCSCKF | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Plays an important role in embryonic development (By similarity).
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition.
Sequence Mass (Da): 13192
Sequence Length: 119
Subcellular Location: Secreted
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Q6X5Y6 | MKKRLTTSTCSSSPSSSVSSSTTTSSPIQSEAPRPKRAKRAKKSSPSGDKSHNPTSPASTRRSSIYRGVTRHRWTGRFEAHLWDKSSWNSIQNKKGKQVYLGAYDSEEAAAHTYDLAALKYWGPDTILNFPAETYTKELEEMQRVTKEEYLASLRRQSSGFSRGVSKYRGVARHHHNGRWEARIGRVFGNKYLYLGTYNTQEEAAAAYDMAAIEYRGANAVTNFDISNYIDRLKKKGVFPFPVNQANHQEGILVEAKQEVETREAKEEPREEVKQQYVEEPPQEEEEKEEEKAEQQEAEIVGYSEEAAVVNCCIDSSTIMEMDRCGDNNELAWNFCMMDTGFSPFLTDQNLANENPIEYPELFNELAFEDNIDFMFDDGKHECLNLENLDCCVVGRESPPSSSSPLSCLSTDSASSTTTTTTSVSCNYLV | Function: May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). Transcriptional activator involved in the activation of a subset of sugar-responsive genes and the control of carbon flow from sucrose import to oil accumulation in developing seeds. Binds to the GCC-box pathogenesis-related promoter element. Promotes sugar uptake and seed oil accumulation by glycolysis. Required for embryo development, seed germination and, indirectly, for seedling establishment. Negative regulator of the ABA-mediated germination inhibition.
PTM: Ubiquitinated.
Sequence Mass (Da): 48436
Sequence Length: 430
Subcellular Location: Nucleus
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Q75JU2 | MSKKTNINTNTKINNFFQTKTNNANVVNEKGYIEDDNEIIDINDFEEDQNLYKIQNKSNGNNSINNNNNNKNTPTKPNLNLTPTKSHTISFPTRPKLPSFTQPNNNNNNNNNNNNNNNINNNNNNNNNNNNNNNNNNNNNNNNSSTNVKPTTTTTTTTTINNNNNNNNNNNINNNNIDLKNKYSFLTNFKKKSFAPLSEQMRPTELSDFIGQESLLVGDPIVKKLFQSPELPSFILYGPPGCGKTTLAQIVASKSNYNINALSAVGSGVKDIKEVIDKARNTLQFGKKTILFIDEIHRYNKLQQDVLLPAIESGIIILIGATTENPSFELNGALLSRCKVFKMEKLTKENLETLIKRTLEVTPLLMDRRLIMDEDAIKSLAEIADGDARVAINVLDMAIKANKEEQTYKERMEEKHSTSGIVRDIVLTKKQMGSLLQRTSLIYDKGGDAFYELISALHKSVRGSDANATAYWVIRMLESGCEPLYIVRRMVRMASEDIGLADNSALPLAIAAYQAVHFVGMPECTNAILQCAVYLANAAKSNSCDHWYAHTREYLEKHEGPPVPIHLRNAPTKMMKDWGYGADYQYNHAFDDQSQVTQIYLPEPIKNEKFFEYKLTCPSVKDRQQSQDQTQRSSQQQQQQQTQPQQQTQPQQQTQQQIQQQLEQLKQIQQQLEQQVQQQIQQQSSQSPSQQSQLQELQQIQQQLQQIQQTNSQINNKNNDSNIIKKNVNNSLDLNPTLPKKQKMIIPSILDNSNNNNNNNNINKSPTPIKKANISHNQLDSSINTSAITIDDSSECDINFDDDFDMASVSSTTMISNIPVGANVAGATEAETETKAISSTDTKESVSINDSDKDLTTTHKNEQDQNNPPDPISLDF | Function: Functions as a modulator for initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. Has an intrinsic ATPase activity that functions as a sensor of DNA damage or of arrested replication forks and regulates the extent of DNA synthesis (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 98566
Sequence Length: 876
Subcellular Location: Nucleus
EC: 3.6.1.-
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Q96S55 | MEVSGPEDDPFLSQLHQVQCPVCQQMMPAAHINSHLDRCLLLHPAGHAEPAAGSHRAGERAKGPSPPGAKRRRLSESSALKQPATPTAAESSEGEGEEGDDGGETESRESYDAPPTPSGARLIPDFPVARSSSPGRKGSGKRPAAAAAAGSASPRSWDEAEAQEEEEAVGDGDGDGDADADGEDDPGHWDADAAEAATAFGASGGGRPHPRALAAEEIRQMLQGKPLADTMRPDTLQDYFGQSKAVGQDTLLRSLLETNEIPSLILWGPPGCGKTTLAHIIASNSKKHSIRFVTLSATNAKTNDVRDVIKQAQNEKSFFKRKTILFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEAMVTILMRAINSLGIHVLDSSRPTDPLSHSSNSSSEPAMFIEDKAVDTLAYLSDGDARAGLNGLQLAVLARLSSRKMFCKKSGQSYSPSRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKSMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFASEDIGLADPSALTQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKACLRNHQGPLPPVPLHLRNAPTRLMKDLGYGKGYKYNPMYSEPVDQEYLPEELRGVDFFKQRRC | Function: Functions as a modulator of initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. In the presence of ATP, stimulation of DNA polymerase delta-mediated DNA synthesis is decreased. Also plays a role in the innate immune defense against viruses. Stabilizes the RIGI dsRNA interaction and promotes RIGI 'Lys-63'-linked polyubiquitination. In turn, RIGI transmits the signal through mitochondrial MAVS.
PTM: Sumoylated with SUMO1 and SUMO2/3.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 72133
Sequence Length: 665
Domain: The UBZ4-type zinc finger binds ubiquitin.
Subcellular Location: Nucleus
EC: 3.6.1.-
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Subsets and Splits