ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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B7XIB8 | MILITSGAEAEIYESENMIIKRRVKKNYRIDELDSMLNKTRTKREVNIIKKLNALNIPSPMFYTTNKYDIVMEKIKGIPVKNILNNESLTSNQFLNKICAKTHKDILIEIGNIVYAMHNNNIIHGDLTTLNFIYSDKIHIIDFGLSFYSNKDEDKAVDLYLFEKSLISVHNEEFVSYFYSGYIVNETLNKKLLEIRKRGRKRE | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 23778
Sequence Length: 203
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q9UYB9 | MKLIKQGAEAKIYLAEFSELYFDYPIKVIVKERIKKRYRIPEIDLKLRKERTIREARILRRAKEFGVNVPYVFEVDTKNMIIVMEYIEGERLKELLEKLPMEERLKVCREVGRQIGKLHEAGIVHGDLTTSNMILREGKVYFIDFGLAEFDDTIEAQGVDLHLLKRAMESTHYKWFERGFEEVLKGYIEIRGEDKGREIREKIREIELRGRYRERSWITQ | Function: Component of the KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Bud32 has ATPase activity in the context of the KEOPS complex and likely plays a supporting role to the catalytic subunit Kae1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 26343
Sequence Length: 220
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). Bud32 has protein kinase activity in vitro, but in the context of the KEOPS complex, the catalytic subunit Kae1 switches the activity of Bud32 from kinase into ATPase .
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q9P7N1 | MSEKPDLRQRCSDIYREIKEKKLTVVKQGAEAITIKTEFYPGEVCLLKCRPAKRWRHPILDQKLSRKRCLVEARLLAKCHYVGIKCPMLYFIDANRGQIYMEWIDGPCVRDYIREICECEIEKKLIPLMKRIGSEVAKMHKNDIVHGDLTTSNMMLESHNNPVPIFIDFGLGSVSESEEDKAVDIYVLERALSSTLPESESLFHHVLDSYAQSWKQSKATLRRFEEVRMRGRKRTMIG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 27707
Sequence Length: 238
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q6C2A3 | MITLPEQLEKLSKQENLIAQGAESLVYSAQHPYLPQQECIVKYRPKKPYRLPELDAQLSKHRTLAEARVLQKLALGDVEVPHLVFIDAKNGLIYMEKIEGLSVKQWIWNEEGDTEGGAQEAGDKSRSLPDGDVSSLKDTLVLVGQEIGKLHKSDIVHGDLTTSNVMLRDGKPVIIDFGLASVSTLAEDKAVDLYVMERAVLSTHPVHSQQYCDWLFEGYLAVVGKSQKEVMRKLEDVRQRGRKRSMLG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 27804
Sequence Length: 248
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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P53323 | MTQEFIDKVSSYLTPDVDIAPISQGAEAIVFTTTTHPYLPRAKDSHQKYIIKYRPPKRYRHPQIDQALTKHRTLNESRLLAKLYLIPGLCVPQLIACDPYNGFIWLEFLGEDLPGGHGFSNLKNFLWMHDQDPYSDLVATTLRKVGRQIGLLHWNDYCHGDLTSSNIVLVRDGARWTPHLIDFGLGSVSNLVEDKGVDLYVLERAILSTHSKHAEKYNAWIMEGFEEVYREQGAKGAKKLKEVTKRFEEVRLRGRKRSMLG | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. Important for bud site selection.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 29936
Sequence Length: 261
Domain: This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event . BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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P0C2K6 | ADSRKPDDRYDMSGNDALGDVKLATYEDNPWETFK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity).
PTM: Contains 2 disulfide bonds.
Catalytic Activity: an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline
Sequence Mass (Da): 4021
Sequence Length: 35
Subcellular Location: Secreted
EC: 4.6.1.-
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Q84TC2 | MAPTTATKDDSGYGDERRRELQAFDDTKLGVKGLVDSGVKSIPSIFHHPPEALSDIISPAPLPSSPPSGAAIPVVDLSVTRREDLVEQVRHAAGTVGFFWLVNHGVAEELMGGMLRGVRQFNEGPVEAKQALYSRDLARNLRFASNFDLFKAAAADWRDTLFCEVAPNPPPREELPEPLRNVMLEYGAAVTKLARFVFELLSESLGMPSDHLYEMECMQNLNVVCQYYPPCPEPHRTVGVKRHTDPGFFTILLQDGMGGLQVRLGNNGQSGGCWVDIAPRPGALMVNIGDLLQLVTNDRFRSVEHRVPANKSSDTARVSVASFFNTDVRRSERMYGPIPDPSKPPLYRSVRARDFIAKFNTIGLDGRALDHFRL | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-dependent dioxygenase required for hydroxylation in position C-7 of the benzoxazinoids. Can use 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside (DIBOA-glucoside) as substrate, but not aglucone DIBOA.
Catalytic Activity: 2-oxoglutarate + DIBOA beta-D-glucoside + O2 = CO2 + succinate + TRIBOA beta-D-glucoside
Sequence Mass (Da): 41369
Sequence Length: 374
Subcellular Location: Cytoplasm
EC: 1.14.11.59
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B1P123 | MGHQAQHGTDDTEELLAAHRQLWCHALGYVKSMALKCALDLRIPDTIDRCGGSATLGELLAASEISASNHDYLRRVMRTLTAMRIFAASHDPAKADDAAAISYQLTPASRLLVSSSSSVDDAAGASKENTTTPSILPNIAHLVRPNTISLLFSMGEWMKDESAASVSLYETVHRQGMWACVEDDAANRASFYESMDADTRLVMQAVVRRCPHVFDGIKSLVDVGGGRGTAAAAVVAAFPHIQRCTVMDLPHVVAEAPAGTAGLSFHGGDMFEHIPSADALMLKWILHDWDEDKCIKIMERCKEAIGGKEAGGKVIIIDTVLGSRADDDDDDKTCRETYVLDLHILSFVNGAEREEHEWRRIFLAAGFRDYKITHTRGIPSIIEVFP | Function: O-methyltransferase involved in the benzoxazinoid glucoside biosynthesis. Can use 2,4,7-trihydroxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside (TRIBOA-glucoside) as substrate, but not aglucone TRIBOA, caffeic acid, ferulic acid, apigenin or quercetin.
Catalytic Activity: S-adenosyl-L-methionine + TRIBOA beta-D-glucoside = DIMBOA beta-D-glucoside + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42131
Sequence Length: 386
EC: 2.1.1.241
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B4G072 | MASSRTGAGAGGRVVVFPFPFQGHFNPVMRLARALHARGLAITVFHSGALDPADYPADYRFVPVTVEADPKLLASEDIAAIVTTLNASCDAPFRARLSALLAAEGRDSVRCVFTDVSWNAVLTASSDLGVPALGMMTASAASLRDYMAYRTLIDKGYLPVKEERKEDPVPELPPYLVKDLLRVDTSDLEEFAELLARTVTAARRASGLIFNTFPLIETDTLAEIHKALSVPVFAVAPLNKLVPTATASLHGVVQADRGCLQWLDTQQPGSVLYVSFGSMAAMDPHEFVELAWGLADSKRPFVWVVRPNLIRGFESGALPDGVEDEVRGRGIVVAWAPQEEVLAHPAVGGFLTHNGWNSTVEAISEGVPMVCCPRHGDQFGNMRYVCDVWKVGTELVGEQLERGQVKAAIDRLFGTKEGEEIKERMKEFKIAAAKGIGIGVDVDETASPRTDLTDLVDLIKSF | Function: Glucosyltransferase involved in the last step of benzoxazinoid glucoside biosynthesis. Catalyzes the glucosylation of hydroxamic acids utilizing UDP-glucose as glucose doner, reducing the toxicity of these natural insecticides for storage. Can use DIMBOA and DIBOA as substrates, HMBOA (2-hydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one) and HBOA (2-hydroxy-2H-1,4-benzoxazin-3(4H)-one) with a lower efficiency, but not indole acetic acid or quercitin.
Catalytic Activity: DIMBOA + UDP-alpha-D-glucose = DIMBOA beta-D-glucoside + H(+) + UDP
Sequence Mass (Da): 50017
Sequence Length: 462
EC: 2.4.1.202
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Q07021 | MLPLLRCVPRVLGSSVAGLRAAAPASPFRQLLQPAPRLCTRPFGLLSVRAGSERRPGLLRPRGPCACGCGCGSLHTDGDKAFVDFLSDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLVRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSTGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ | Function: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria . In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppression of interleukin-12 production in monocyte-derived dendritic cells. Involved in regulation of antiviral response by inhibiting RIGI- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31362
Sequence Length: 282
Subcellular Location: Mitochondrion matrix
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P02746 | MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPDMEA | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
PTM: Hydroxylated on lysine and proline residues. Hydroxylated lysine residues can be glycosylated. Human C1Q contains up to 68.3 hydroxylysine-galactosylglucose residues and up to 2.5 hydroxylysine-galactose per molecule. Total percentage hydroxylysine residues glycosylated is 86.4%.
Sequence Mass (Da): 26722
Sequence Length: 253
Subcellular Location: Secreted
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P31721 | MKTQWSEILTPLLLLLLGLLHVSWAQSSCTGSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGPPGPRGPKGGSGDYKATQKVAFSALRTVNSALRPNQAIRFEKVITNVNDNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNIVRGRDRDRMQKVLTFCDYAQNTFQVTTGGVVLKLEQEEVVHLQATDKNSLLGVEGANSIFTGFLLFPDMDV | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
PTM: Hydroxylated on lysine and proline residues. Hydroxylated lysine residues can be glycosylated.
Sequence Mass (Da): 26589
Sequence Length: 253
Subcellular Location: Secreted
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P02747 | MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEPGIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQSVFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCVLLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGFLLFPD | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
PTM: O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.
Sequence Mass (Da): 25774
Sequence Length: 245
Subcellular Location: Secreted
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Q02105 | MVVGPSCQPPCGLCLLLLFLLALPLRSQASAGCYGIPGMPGMPGAPGKDGHDGLQGPKGEPGIPAVPGTRGPKGQKGEPGMPGHRGKNGPRGTSGLPGDPGPRGPPGEPGVEGRYKQKHQSVFTVTRQTTQYPEANALVRFNSVVTNPQGHYNPSTGKFTCEVPGLYYFVYYTSHTANLCVHLNLNLARVASFCDHMFNSKQVSSGGVLLRLQRGDEVWLSVNDYNGMVGIEGSNSVFSGFLLFPD | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.
Sequence Mass (Da): 25992
Sequence Length: 246
Subcellular Location: Secreted
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P31722 | MVVGTSCQPQHGLYLLLLLLALPLRSQANAGCYGIPGMPGLPGTPGKDGHDGLQGPKGEPGIPAIPGTQGPKGQKGEPGMPGHRGKNGPMGTSGSPGDPGPRGPPGEPGEEGRYKQKHQSVFTVTRQTAQYPAANGLVKFNSAITNPQGDYNTNTGKFTCKVPGLYYFVHHTSQTANLCVQLLLNNAKVTSFCDHMSNSKQVSSGGVLLRLQRGDEVWLAVNDYNGMVGTEGSDSVFSGFLLFPD | Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
PTM: Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.
Sequence Mass (Da): 25686
Sequence Length: 245
Subcellular Location: Secreted
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Q8CFR0 | MALGLLIAVPLLLQAAPPGAAHYEMLGTCRMICDPYSVAPAGGPAGAKAPPPGPSTAALEVMQDLSANPPPPFIQGPKGDPGRPGKPGPRGPPGEPGPPGPRGPPGEKGDSGRPGLPGLQLTTSAAGGVGVVSGGTGGGGDTEGEVTSALSAAFSGPKIAFYVGLKSPHEGYEVLKFDDVVTNLGNHYDPTTGKFSCQVRGIYFFTYHILMRGGDGTSMWADLCKNGQVRASAIAQDADQNYDYASNSVVLHLDSGDEVYVKLDGGKAHGGNNNKYSTFSGFLLYPD | Function: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses.
PTM: Glycosylated, but not with N-linked glycans.
Sequence Mass (Da): 29292
Sequence Length: 287
Subcellular Location: Secreted
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Q9NPY3 | MATSMGLLLLLLLLLTQPGAGTGADTEAVVCVGTACYTAHSGKLSAAEAQNHCNQNGGNLATVKSKEEAQHVQRVLAQLLRREAALTARMSKFWIGLQREKGKCLDPSLPLKGFSWVGGGEDTPYSNWHKELRNSCISKRCVSLLLDLSQPLLPSRLPKWSEGPCGSPGSPGSNIEGFVCKFSFKGMCRPLALGGPGQVTYTTPFQTTSSSLEAVPFASAANVACGEGDKDETQSHYFLCKEKAPDVFDWGSSGPLCVSPKYGCNFNNGGCHQDCFEGGDGSFLCGCRPGFRLLDDLVTCASRNPCSSSPCRGGATCVLGPHGKNYTCRCPQGYQLDSSQLDCVDVDECQDSPCAQECVNTPGGFRCECWVGYEPGGPGEGACQDVDECALGRSPCAQGCTNTDGSFHCSCEEGYVLAGEDGTQCQDVDECVGPGGPLCDSLCFNTQGSFHCGCLPGWVLAPNGVSCTMGPVSLGPPSGPPDEEDKGEKEGSTVPRAATASPTRGPEGTPKATPTTSRPSLSSDAPITSAPLKMLAPSGSPGVWREPSIHHATAASGPQEPAGGDSSVATQNNDGTDGQKLLLFYILGTVVAILLLLALALGLLVYRKRRAKREEKKEKKPQNAADSYSWVPERAESRAMENQYSPTPGTDC | Function: Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion.
PTM: N- and O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 68560
Sequence Length: 652
Subcellular Location: Membrane
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O89103 | MAISTGLFLLLGLLGQPWAGAAADSQAVVCEGTACYTAHWGKLSAAEAQHRCNENGGNLATVKSEEEARHVQQALTQLLKTKAPLEAKMGKFWIGLQREKGNCTYHDLPMRGFSWVGGGEDTAYSNWYKASKSSCIFKRCVSLILDLSLTPHPSHLPKWHESPCGTPEAPGNSIEGFLCKFNFKGMCRPLALGGPGRVTYTTPFQATTSSLEAVPFASVANVACGDEAKSETHYFLCNEKTPGIFHWGSSGPLCVSPKFGCSFNNGGCQQDCFEGGDGSFRCGCRPGFRLLDDLVTCASRNPCSSNPCTGGGMCHSVPLSENYTCRCPSGYQLDSSQVHCVDIDECQDSPCAQDCVNTLGSFHCECWVGYQPSGPKEEACEDVDECAAANSPCAQGCINTDGSFYCSCKEGYIVSGEDSTQCEDIDECSDARGNPCDSLCFNTDGSFRCGCPPGWELAPNGVFCSRGTVFSELPARPPQKEDNDDRKESTMPPTEMPSSPSGSKDVSNRAQTTGLFVQSDIPTASVPLEIEIPSEVSDVWFELGTYLPTTSGHSKPTHEDSVSAHSDTDGQNLLLFYILGTVVAISLLLVLALGILIYHKRRAKKEEIKEKKPQNAADSYSWVPERAESQAPENQYSPTPGTDC | Function: Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion. Marker for early multipotent hematopoietic precursor cells. May play a role in cell-cell interactions during hematopoietic and vascular development.
PTM: N- and O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 69354
Sequence Length: 644
Subcellular Location: Membrane
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O46051 | MYLELFAILLATALAWDYMRKRRHNKMYAEAGIRGPKSYPLVGNAPLLINESPKTIFDMQFRLIAEFGKNIKTQMLGESGFMTADSKMIEAIMSSQQTIQKNNLYSLLVNWLGDGLLISQGKKWFRRRKIITPAFHFKILEDFVEVFDQQSATMVQKLYDRADGKTVINMFPVACLCAMDIIAETAMGVKINAQLQPQFTYVQSVTTASAMLAERFMNPLQRLDFTMKLFYPKLLDKLNDAVKNMHDFTNSVITERRELLQKAIADGGDADAALLNDVGQKRRMALLDVLLKSTIDGAPLSNDDIREEVDTFMFEGHDTTTSSIAFTCYLLARHPEVQARVFQEVRDVIGDDKSAPVTMKLLGELKYLECVIKESLRLFPSVPIIGRYISQDTVLDGKLIPADSNVIILIYHAQRDPDYFPDPEKFIPDRFSMERKGEISPFAYTPFSAGPRNCIGQKFAMLEMKSTISKMVRHFELLPLGEEVQPVLNVILRSTTGINCGLKPRVY | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57481
Sequence Length: 507
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9VLZ7 | MWILLGIAVLIMTLVWDNSRKQWRVNTFEKSRILGPFTIPIVGNGLQALTLRPENFIQRFGDYFNKYGKTFRLWILGECLIYTKDLKYFESILSSSTLLKKAHLYRFLRDFLGDGLLLSTGNKWTSRRKVLAPAFHFKCLENFVEIMDRNSGIMVEKLKNYADGKTCVDLFKFVSLEALDVTTETAMGVQVNAQNEPNFPYTKALKSVVYIESKRLASVSMRYNWLFPLAAPLVYRRLQKDIAIMQDFTDKVIRERRAILERARADGTYKPLIMGDDDIGGKAKMTLLDILLQATIDNKPLSDVDIREEVDVFIFAGDDTTTSGVSHALHAISRHPKVQECIYEELVSVLGPDPDASVTQTKLLELKYLDCVIKETMRLHPPVPILGRYIPEDLKIGEITIPGNTSILLMPYYVYRDPEYFPDPLVFKPERWMDMKTTSNTPPLAYIPFSSGPKNCIGQKFANLQMKALISKVIRHYELLPLGADLKATYTFILSSSTGNNVGLKPRTRVK | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58265
Sequence Length: 511
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q9VYY4 | MEVLKKDAALGSPSSVFYFLLLPTLVLWYIYWRLSRAHLYRLAGRLPGPRGLPIVGHLFDVIGPASSVFRTVIRKSAPFEHIAKMWIGPKLVVFIYDPRDVELLLSSHVYIDKASEYKFFKPWLGDGLLISTGQKWRSHRKLIAPTFHLNVLKSFIELFNENSRNVVRKLRAEDGRTFDCHDYMSEATVEILLETAMGVSKKTQDKSGFEYAMAVMRMCDILHARHRSIFLRNEFVFTLTRYYKEQGRLLNIIHGLTTKVIRSKKAAFEQGTRGSLAQCELKAAALEREREQNGGVDQTPSTAGSDEKDREKDKEKASPVAGLSYGQSAGLKDDLDVEDNDIGEKKRLAFLDLMLESAQNGALITDTEIKEQVDTIMFEGHDTTAAGSSFFLSLMGIHQDIQDRVLAELDSIFGDSQRPATFQDTLEMKYLERCLMETLRMYPPVPLIARELQEDLKLNSGNYVIPRGATVTVATVLLHRNPKVYANPNVFDPDNFLPERQANRHYYAFVPFSAGPRSCVGRKYAMLKLKILLSTILRNYRVYSDLTESDFKLQADIILKREEGFRVRLQPRTS | Function: Probably involved in steroid hormones biosynthesis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65380
Sequence Length: 574
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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Q28GG3 | MTEFLFCFSCCIGEQPQPKRRRRIDRSMIGEPMNFVHTAHVGSGDTNAGFAMGGSFQDQMKSKGGYTPGISEVAL | Function: Probably involved in the organization of the actin cytoskeleton by acting downstream of CDC42, inducing actin filament assembly.
Location Topology: Lipid-anchor
Sequence Mass (Da): 8218
Sequence Length: 75
Subcellular Location: Cytoplasm
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Q54PT3 | MFLTSILYTIIIILIFYKGLEYLIEKRSFPLVHPIKGVMNGTKPYFIFGDLPFQRLLNLKPKLKELGSIYFRWFFWYPIVEIKDINAIQYVYNEKSNNYSLYWNLNKSSNFILTGSEIKRFFRIYYCAFNCKDSLQRIMPVIKSQVFDFIHSHKFQNSTLSTNDDVTNFMLKLLSRVYLGSSDEAYHCFKANYKKFNKSYLDFFHYLFPTLLKIPSKFSRKYIKNKNKRALYQVLAMKAYYGVVKQSSDDHIEESMINIIAETSYNDKEGLSLEEIKMPSYLLNASSIKGPMIMVENLMFQLIEKSEIESKIRKEIKLVFEKNGKDVNSFDFDDIMEMKYLEATLDEINRLYPPFPKLMPRQTKESDRILGYHIPKGTMISCPVADILRDPSNFQDPLTFKPERQLIFSNPKFASPSITSIQEINGLSSSSSNSFALHHRSLPSINNNNNNNNNNNNNNNNNNNNNNNNNSNNNSINGNNKNNNRNCIQSFNNSALKKSFLSDSSSIIDNIVGTNRVDKLKLDSLNENSNINNNNNKDLLNVPNIIEINKNNPISNNKYNSYNNLTIEERNQRIIKNLPWGIGSKKCLGKELAKLIVKTIIVILYSQYTFDKHLDENDEELCDTNNQPKIQITFNPEIKPPLLLKSRKLFSISQPKQ | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76315
Sequence Length: 657
Subcellular Location: Membrane
EC: 1.14.-.-
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P35720 | MAALLLRHVGRHCLRAHLSPQLCIRNAVPLGTTAKEEMERFWSKNTTLNRPLSPHISIYGWSLPMAMSICHRGTGIALSAGVSLFGLSALLVPGSFESHLEFVKSLCLGPALIHTAKFALVFPLMYHTWNGIRHLMWDLGKGLTISQLHQSGVAVLVLTVLSSVGLAAM | Cofactor: The heme b is bound between the two transmembrane subunits SDHC and SDHD.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18389
Sequence Length: 169
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P41955 | MINIPTSILCRLGARSAISRSFGTSVVTKSEAKTPIQKFGWEYLKKQRDMKRPIAPHLTIYQPQLTWMLSGFHRISGCVMAGTLLVGGLGFAVLPLDFTTFVEYIRGWNLPCAVTAVFKYIIAFPIIFHTLNGIRFLGFDLAKGVDNIGQVYKSGWLVFGVSAVIALAIVINSCQNKSKAVKTA | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Mediates resistance to enteropathogenic E.coli infection (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20244
Sequence Length: 184
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P41956 | MINIPTAILCRLGARSSISRSFGTSIVTKSEAKTPIQKFGWEYLLKQRSKNRPIAPHLTVYQPQLTWMLSGFHRISGCVMAGTLLVGGIGFAVLPFDFTAFVDFIRSWNLPCAVTAVFKYIIAFPIIFHTLNGIRFLGFDLAKGVNNVGQIYKSGYLVSGLSAILALAIVFNSCQNKSNKTA | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (By similarity). Mediates resistance to enteropathogenic E.coli infection .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19982
Sequence Length: 182
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P48934 | MFIKFKISNRPIAPHLLVYTPQLSSLFSIWHRISGVGLAFFFTTFLIFIRIILSSNFACNLLTLISFEISQWIIIYFNLFILLFLFYHLFNGTRHIIWDFGFLLDIKYLSKFSLFLLVSLSLILIFQ | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15054
Sequence Length: 127
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P70097 | MAALLLRHVGRHCLRAHLNSQICLRNAVPLGTTAKEEMERFWNKNTSSKRPVSPHLTIYRWSLPMVMSICHRGTGVALSGGVSLFGLSALLLPGNFESYLMFIKSLCLGPALIHSAKFVLVFPLMYHSLNGIRHLIWDLGKGLSISQVYQSGVAVLMLAVLSSVGLAAM | Cofactor: The heme b is bound between the two transmembrane subunits SDHC and SDHD.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18498
Sequence Length: 169
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P48935 | MFYKNRPLSPYVTIYSSQWTSISSIFHRLSGLYLVFFLFVLFCSIKFLFCFSTFWFVYKFVKTCFFFILSFFIVFIVFSMYSLFYHFFIGLRHLVWDEVILMEDNFVTMSTKLSLSLSLVLVLINCLRYFLV | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15979
Sequence Length: 132
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q8T2T5 | MFGRTLNTFTSRNAPLVRNFDKFIVNNTLTSKNIYLSQTNTTNTPLSYSTQAKKPFTITEKRIDELKTPYQPTSPHLTIYKFPLPAVMSIMHRATGICLALGITGLAGVTLFAPHDAIHYIQLLHTQYPALVYPAKFAVALPLTYHFCTGVRHIIWDETVKGLSISQIESSGKVLLAVVAVLSTIFTFVSFK | Cofactor: The heme b is bound between the two transmembrane cytochrome b560 subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21379
Sequence Length: 192
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q99643 | MAALLLRHVGRHCLRAHFSPQLCIRNAVPLGTTAKEEMERFWNKNIGSNRPLSPHITIYSWSLPMAMSICHRGTGIALSAGVSLFGMSALLLPGNFESYLELVKSLCLGPALIHTAKFALVFPLMYHTWNGIRHLMWDLGKGLKIPQLYQSGVVVLVLTVLSSMGLAAM | Cofactor: The heme b is bound between the two transmembrane subunits SDHC and SDHD.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18610
Sequence Length: 169
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P35721 | MKINRPLSPHLTIYKPQLTSTFSIFHRISGAFLATMVLFSILFFKIGDLSLTFYHFYQYFFFLTFYLNWFIISLVNFTLLALCYHMSNGVRHLLWDLGFFLELSKVYTSGIIMLFCAAFLALLNIIRQHWSNGQIPY | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16173
Sequence Length: 137
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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O48958 | MATTATPQLLGGSVPQQWQTCLLVLLPVLLVSYYLLTSRSRNRSRSGKLGGAPRLPPGPAQLPILGNLHLLGPLPHKNLRELARRYGPVMQLRLGTVPTVVVSSAEAAREVLKVHDVDCCSRPASPGPKRLSYDLKNVGFAPYGEYWREMRKLFALELLSMRRVKAACYAREQEMDRLVADLDRAAASKASIVLNDHVFALTDGIIGTVAFGNIYASKQFAHKERFQHVLDDAMDMMASFSAEDFFPNAAGRLADRLSGFLARRERIFNELDVFFEKVIDQHMDPARPVPDNGGDLVDVLINLCKEHDGTLRFTRDHVKAIVLDTFIGAIDTSSVTILWAMSELMRKPQVLRKAQAEVRAAVGDDKPRVNSEDAAKIPYLKMVVKETLRLHPPATLLVPRETMRDTTICGYDVPANTRVFVNAWAIGRDPASWPAPDEFNPDRFVGSDVDYYGSHFELIPFGAGRRICPGLTMGETNVTFTLANLLYCYDWALPGAMKPEDVSMEETGALTFHRKTPLVVVPTKYKNRRAA | Function: Catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile. The dehydration of the oxime to the corresponding nitrile is followed by a C-hydroxylation of the nitrile to produce p-hydroxymandelonitrile.
Catalytic Activity: (E)-4-hydroxyphenylacetaldehyde oxime + O2 + reduced [NADPH--hemoprotein reductase] = (S)-4-hydroxymandelonitrile + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59088
Sequence Length: 531
Pathway: Secondary metabolite biosynthesis; dhurrin biosynthesis; dhurrin from L-tyrosine: step 2/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.37
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A0A3Q7HS74 | MDPFILYSLAFALVYISLYFIFKGNYSNNKHTNLPLGSNGWPILGENIDMAYSSSPEKFIHERMEKHSSQVFKTSLLGQKIAIFCGTSGNKFLFSNENKLLTTWWPPSLTKPLMCPTQSQSQNSVKEIALLNRGFLREILKPENLKQYIPFMDSMARDHLKQEWIPFKEVKIYPLVKKYTFSLACKLFLSIDDFRHVKKLSDPFVLVTSGMFTVPINLPGTPYNRAIKGGKMVHEELMKIIKERKINEKNNHSNDLLSQLISFSDENGQFMNDAEIYNNIIGLLVASYDTTSAAITFVLKYLAELPNIFNEVYKEQMEIAKSKGEGELLNWDDIQKMKYSWNVACEAIRLMPPAQGAFREAITDFTFGGFTVPKGWKTFWSVYSTHKNPKYFPEPEKFDPCRFEGSGPEPYTFVPFGGGPRMCPGKEYARLEILVFMYNIVTNFKLEKLVPHEKIIYKSSPVPLNGLPVRIQPIA | Function: Catalyzes the C-6 beta-hydroxylation of beta-amyrin to form daturadiol . Catalyzes the C-6 beta-hydroxylation of alpha-amyrin to form 6-beta-hydroxy-alpha-amyrin .
Catalytic Activity: beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] = daturadiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54462
Sequence Length: 475
Subcellular Location: Membrane
EC: 1.14.14.64
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Q6XQ14 | MSVAILTSLPPQWLSILAVFLLPILTLLLFRGKDDNQKKGLKLPPGPRQLPLIGNLHQLGGQPYVDFWKMAKKYGPVMYLQLGRCPTVVLSSTETSKELMKDRDVECCSRPLSVGPGQLSYNFLDVAFSPYSDYWREMRKLFIFELLSMRRVQTFWYAREEQMDKMIEILDGAYPNPVNLTEKVFNMMDGIIGTIAFGRTTYAQQEFRDGFVKVLAATMDMLDNFHAENFFPVVGRFIDSLTGALAKRQRTFTDVDRYFEKVIEQHLDPNRPKPETEDIVDVLIGLMKDESTSFKITKDHVKAILMNVFVGGIDTSAVTITWAFSELLKNPKLMKKAQEEVRRAVGPNKRRVEGKEVEKIKYIDCIVKETFRKHPPVPLLVPHFSMKHCKIGGYDILPGTTIYVNAWAMGKDPTIWENPEEYNPDRFMNSEVDFRGSDFELVPFGAGRRICPGLAMGTTAVKYILSNLLYGWDYEMPRGKKFEDFPLIEEGGLTVHNKQDIMVIPKKHKWD | Function: Catalyzes the conversion of (E)-2-methylpropanal oxime (valox) to 2-hydroxy-2-methylpropanenitrile (acetone cyanohydrin) and of (E)-2-methylbutanal oxime (ilox) to 2-hydroxy-2-methylbutyronitrile. The reaction takes place in three steps. First, the oxime is isomerized to the (Z)- isomer, next the (Z)-isomer is dehydrated to the corresponding nitrile, followed by a C-hydroxylation of the nitrile. Can use both aliphatic and aromatic oximes as substrates.
Catalytic Activity: (1E,2S)-2-methylbutanal oxime + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-2-methylbutanenitrile + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58578
Sequence Length: 511
Subcellular Location: Microsome membrane
EC: 1.14.14.41
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Q2QUC5 | MELTMASTMSLALLVLSAAYVLVALRRSRSSSSKPRRLPPSPPGWPVIGHLHLMSGMPHHALAELARTMRAPLFRMRLGSVPAVVISKPDLARAALTTNDAALASRPHLLSGQFLSFGCSDVTFAPAGPYHRMARRVVVSELLSARRVATYGAVRVKELRRLLAHLTKNTSPAKPVDLSECFLNLANDVLCRVAFGRRFPHGEGDKLGAVLAEAQDLFAGFTIGDFFPELEPVASTVTGLRRRLKKCLADLREACDVIVDEHISGNRQRIPGDRDEDFVDVLLRVQKSPDLEVPLTDDNLKALVLDMFVAGTDTTFATLEWVMTELVRHPRILKKAQEEVRRVVGDSGRVEESHLGELHYMRAIIKETFRLHPAVPLLVPRESVAPCTLGGYDIPARTRVFINTFAMGRDPEIWDNPLEYSPERFESAGGGGEIDLKDPDYKLLPFGGGRRGCPGYTFALATVQVSLASLLYHFEWALPAGVRAEDVNLDETFGLATRKKEPLFVAVRKSDAYEFKGEELSEV | Function: Involved in serotonin biosynthesis. Catalyzes the conversion of tryptamine to serotonin . Accumulation of serotonin may play a role in innate immunity .
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + tryptamine = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + serotonin
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57765
Sequence Length: 523
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
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W8JDE2 | MDQLMNFSLTSPIFLLLSSLFLIILLNKLMRGNKIQKGKKLPPGPKKIAIIGNLPSNGRFTSLIVFLNNLAEKYGPIMHLRIGQLSAVIISSAEKAKEILNTHGVRVADRPQTTVAKIMLYNSLGVTFAPYGDYLKQLRQIYAMELLSPKTVKSFWTIMDDELSTMITSIKSEVGQPMILHDKMMTYLYAMLCRATVGSVCNGRETLIMAAKETSALSASIRIEDLFPSVKILPVISGLKSKLTNLLKELDIVLEDIISAREKKLLSQPQQPLMLDEEDMLGVLLKYKNGKGNDTKFRVTNNDIKAIVFELILAGTLSSAAIVEWCMSELMKNPELLKKAQDEVRQVLKGKKTISGSDVGKLEYVKMVVKESVRLHPPAPLLFPRECREEFEIDGMTIPKKSWVIINYWAIGRDPKIWPNADKFEPERFSNNNIDFYGSNFELIPFGAGRRVCPGILFGTTNVELLLAAFLFHFDWELPGGMKPEELDMNELFGAGCIRENPLCLIPSISTVVEGN | Function: Involved in monoterpene indole alkaloids (MIAs) biosynthesis . Converts by aromatization the tetrahydro-beta-carboline alkaloids tetrahydroalstonine and ajmalicine to the corresponding beta-carboline alkaloids alstonine and serpentine, respectively .
Catalytic Activity: A + O2 + reduced [NADPH--hemoprotein reductase] + tetrahydroalstonine = AH2 + alstonine + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 57776
Sequence Length: 516
Pathway: Alkaloid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.-
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A0A2Z5D854 | MDPAAIFLILAIPIASVYLLFYHKKRVNGLSSPPGPRGLPFIGHFYQIYKSECAHEYISNLSKQYGSLMTLHLGSVPALVVSSPKMAQEVLKTQDLVFCSRAQMTGSGKLSYNGLEMAFAPYGEHWRNVRKMCTLELFTQKRAQFNFRPVREDEVSRMVGRLSEAAAASEDVNAYECFTNFATSIISRVAFGKRYDEDNLGKEKFQRMVADIEAMFAAFFVSDFFPMFGWIDRLSGVKAVLDRNFNEMDTFYQELIDEHLKPDRPESLNGDLIDVMLKNKGSFLTMDSIKAILLNVFSGGIGTTGSALVFAMTALLRNQRVMKKAQEEVRSVIGKKEIVDEDDIQKLPYLRAVVKETLRLYPPGPLLIPRVAMESCVLGEDEDHMYMIKPNTIVYVNTWGIGRDPKYWKNPLEFMPERFFERPDLNYTGQQFEYLPFGSGRRICAGIIIGQNNVEVGLANLLYSFDWEPPTGKTFEDIDDQPCNGLTLAKKNPLYIRPKIYVHP | Function: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes . Catalyzes the conversion of psoralen into xanthotoxol and of 6-methoxycoumarin into scopoletin . Can also convert with a lower efficiency scopoletin into fraxetin and 7-methoxycoumarin into daphnetin-7-methylether, and use 7-methoxy-3-methylcoumarin as substrate .
Catalytic Activity: O2 + psoralen + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + xanthotoxol
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57254
Sequence Length: 504
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Microsome membrane
EC: 1.14.14.-
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A0A1D6GQ67 | MEDKVLLAVAMVALIAVLSKLKSLLETKPKLNLPPGPWTLPLIGSIHHLVSSPLPYRAMRELAHKHGPLMMLWLGEVPTLVVSSPEAAQAITKTHDVTFADRHMNSTVDILTFNGNDIVFGTYGEQWRQLRKLSVLELLSVARVQSFQRIREEEVARFMRNLAASAGAGATVDLSKMISSFINDTFVRESIGSRCKHQDEYLDALHTGIRVAAELSVANLFPSSRLLQSLSTARRKAVAARDEMARILGQIIRETKEAMDWGDKASNESMISVLLRLQKEAGLPIELTDDIVMALMFDLFGAGSDTSSTTLTWCMTEMIRYPATMAKAQAEVREAFKGKTTITEDDLSRANLSYLKLVVKEALRLHCPVPLLIPRKCRETCQIMGYDIPKDTCVLVNVWAICRDSRYWEDADEFKPERFENSSLDYKGTSHEYLPFGSGRRMCPGGNLGVANMELALASLLYHFDWKLPSGQEPKDVDVWEAAGLVGRKNAGLVLHPVSRFAPVNA | Function: Involved in the production of antifungal dolabralexin phytoalexins in response to biotic and abiotic stresses . Catalyzes the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3, to yield the epoxides 15,16-epoxydolabrene (epoxydolabrene) and 3b-hydroxy-15,16-epoxydolabrene (epoxydolabranol) .
Catalytic Activity: dolabradiene + O2 + reduced [NADPH--hemoprotein reductase] = 15,16-epoxydolabrene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56314
Sequence Length: 506
Subcellular Location: Membrane
EC: 1.14.14.159
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A3A871 | MEDKLILDLCLSALFVVVLSKLVSSAMKPRLNLPPGPWTLPLIGSLHHLVMTKSPQTHRSLRALSEKHGPIMQLWMGEVPAVVVSSPAVAEEVLKHQDLRFADRHLTATTEEVFFGGRDVIFGPYSERWRHLRKICMQELLTAARVRSFQGVREREVARLVRELAADAGAGGDAGVNLNERISKLANDIVMVSSVGGRCSHRDEFLDALEVAKKQITWLSVADLFPSSKLARMVAVAPRKGLASRKRMELVIRRIIQERKDQLMDDSAAGAGEAAAGKDCFLDVLLRLQKEGGTPVPVTDEIIVVLLFDMISGASETSPTVLIWTLAELMRNPRIMAKAQAEVRQAVAGKTTITEDDIVGLSYLKMVIKETLRLHPPAPLLNPRKCRETSQVMGYDIPKGTSVFVNMWAICRDSRYWEDPEEYKPERFENNSVDYKGNNFEFLPFGSGRRICPGINLGVANLELPLASLLYHFDWKLPNGMAPKDLDMHETSGMVAAKLITLNICPITHIAPSSA | Function: Enzyme of the diterpenoid metabolism involved in the biosynthesis of antibacterial oryzalides such as phytocassane.
Catalytic Activity: ent-isokaurene + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = ent-isokaurene-2beta,3beta-diol + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57157
Sequence Length: 515
Subcellular Location: Membrane
EC: 1.14.14.76
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B8AV52 | MVGGELVLAALVILLALLLTLVLSHFLPLLLNPKAPKGSFGWPLLGETLRFLSPHASNTLGSFLEDHCSRYGRVFKSHLFCTPTIVSCDQELNHFILQNEERLFQCSYPRPIHGILGKSSMLVVLGEDHKRLRNLALALVTSTKLKPSYLGDIEKIALHIVGSWHGKSKDKGMVNVIAFCEEARKFAFSVIVKQVLGLSPEEPVTAMILEDFLAFMKGLISFPLYIPGTPYAKAVQARARISSTVKGIIEERRNAGSSNKGDFLDVLLSSNELSDEEKVSFVLDSLLGGYETTSLLISMVVYFLGQSAQDLELVKREHEGIRSKKEKDEFLSSEDYKKMEYTQHVINEALRCGNIVKFVHRKALKDVRYKEYLIPSGWKVLPVFSAVHLNPLLHGNAQQFQPCRWEGASQGTSKKFTPFGGGPRLCPGSELAKVEAAFFLHHLVLNYRWRIDGDDIPMAYPYVEFQRGLPIEIEPLCSES | Function: Involved in brassinosteroid biosynthesis (By similarity). Involved in internode elongation and seed development (By similarity). Catalyzes the conversion of campesterol (CR) to (22S)-22-hydroxycampesterol (22-OHCR, 22-hydroxyCR) (By similarity).
Catalytic Activity: campesterol + O2 + reduced [NADPH--hemoprotein reductase] = (22S)-22-hydroxycampesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 53704
Sequence Length: 480
Pathway: Plant hormone biosynthesis; brassinosteroid biosynthesis.
Subcellular Location: Membrane
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H1A988 | MDASSTPGAIWVVLTVILAAIPIWVCHMVNTLWLRPKRLERHLRAQGLHGDPYKLSLDNSKQTYMLKLQQEAQSKSIGLSKDDAAPRIFSLAHQTVHKYGKNSFAWEGTAPKVIITDPEQIKEVFNKIQDFPKPKLNPIAKYISIGLVQYEGDKWAKHRKIINPAFHLEKLKGMLPAFSHSCHEMISKWKGLLSSDGTCEVDVWPFLQNLTCDVISRTAFGSSYAEGAKIFELLKRQGYALMTARYARIPLWWLLPSTTKRRMKEIERGIRDSLEGIIRKREKALKSGKSTDDDLLGILLQSNHIENKGDENSKSAGMTTQEVMEECKLFYLAGQETTAALLAWTMVLLGKHPEWQARARQEVLQVFGNQNPNFEGLGRLKIVTMILYEVLRLYPPGIYLTRALRKDLKLGNLLLPAGVQVSVPILLIHHDEGIWGNDAKEFNPERFAEGIAKATKGQVCYFPFGWGPRICVGQNFALLEAKIVLSLLLQNFSFELSPTYAHVPTTVLTLQPKHGAPIILHKL | Function: Involved in the biosynthesis of Glycyrrhetinic acid (GA), a natural product which exhibits anti-inflammatory activity . Involved in the biosynthesis of the triterpenoid saponin glycyrrhizin . Catalyzes three sequential oxidation steps at C-30 of 11-oxo-beta-amyrin . Also able to catalyze C-30 monohydroxylation of beta-amyrin to produce 30-hydroxy-beta-amyrin . May be also responsible for the oxidation at positions C-22 and C-29 in addition to C-30 .
Catalytic Activity: 11-oxo-beta-amyrin + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = glycyrrhetinate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59020
Sequence Length: 523
Subcellular Location: Membrane
EC: 1.14.14.115
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A0A481NR20 | MEISVASVTVSVVIAVVTWWVWRTLKWVWFQPKMLESYLRRQGLSGTPYTPLVGDLKRNSKMLTEAISKPIRLNDDITQRVVPYPLQMLKTYGRTHFTWLGPIPAITIMDPELIKEVFNRVYDFQKARLFPLARLIATGLVRYDGDKWAKHRKIINPAFHLEKLKNMVPAFHQCCSEVVGAWDKLVSDKRSSCEVDVWPGLVSMTADMISRTAFGSSYKEGQRIFELQEEIKELLIQSLGKAFIPGYHYLPTKGNRRMKAADREIKVILRGIVNKRLRAREAGEAPSEDLLGILLESNLGQAKGNGMSIEDVMEECKLFYLAGQETTSVLLVWTMVMLSQHQDWQARAREEVKQVFGDKEPNTEGLNQLKVMTMILYEVLRLYPPVTQLPRAIHKEMKLGDMTLPAGVHINLPIMLVQRDTELWGNDAAEFKPERFKDGLSKAAKNQVSFFSFAWGPRICIGQNFALMEAKMAMALILQRFSLELSPSYVHAPYSVITLHPQFGAHLILHKLY | Function: Catalyzes the oxidation of oleanolate at the C-23 position to form hederagenin.
Catalytic Activity: O2 + oleanolate + reduced [NADPH--hemoprotein reductase] = H(+) + H2O + hederagenin + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58607
Sequence Length: 513
Subcellular Location: Membrane
EC: 1.14.14.-
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Q50EK6 | MADQISLLLVVFTAAVALLHLIYRWWNAQRGQKRTSNEKNQELHLPPGSTGWPLIGETYSYYRSMTSNRPRQFIDDREKRYDSDVFVSHLFGSQAVISSDPQFNKYVLQNEGRFFQAHYPKALKALIGDYGLLSVHGDLQRKLHGIAVNLLRFERLKFDFMEEIQNLVHSTLDRWVDKKEIALQNECHQMVLNLMAKQLLDLSPSKETNEICELFVDYTNAVIAIPIKIPGSTYAKGLKARELLIRKISNMIKERRDHPHIVHKDLLTKLLEEDSISDEIICDFILFLLFAGHETSSRAMTFAIKFLTTCPKALTQMKEEHDAILKAKGGHKKLEWDDYKSMKFTQCVINETLRLGNFGPGVFRETKEDTKVKDCLIPKGWVVFAFLTATHLDEKFHNEALTFNPWRWELDQDVSNNHLFSPFGGGARLCPGSHLARLELALFLHIFITRFRWEALADEHPSYFPLPYLAKGFPMRLYNRE | Function: Multifunctional and multisubstrate cytochrome P450 that oxidizes the respective carbon 18 of abietadienol, abietadienal, levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol, and dehydroabietadienal.
Catalytic Activity: abieta-7,13-dien-18-ol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = abieta-7,13-dien-18-oate + 3 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55702
Sequence Length: 481
Subcellular Location: Membrane
EC: 1.14.14.145
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A0A517FNC5 | MAPVVILFFLFPTLLVLVVAVLGLRGGDDSWKKRGLKVPPGSMGWPLLGETIAFRRLHPCTSLGEYMEEHVNKYGKIYRSNLFGAPTIVSADAELNRFVLMNDERLFEPCFPKSVADILGHTSMLVLTGEMHRYMKSLSVNFMGIARLRNNFLGDSELYITQNFNRWKENIPFPAKEEACKVTFNLMVKNILSLNPGEPESEHLRKLYMSFMKGVVAIPLNLPGTAYKKAIQSRATILKMIEKLMEERIRNKKAGTDKIGEADLLGFILEQSNLDAEQFGDLLLGLLFGGHETSATAITLVIYFLYDCPKAVDHLREEHLGIVRAKKARGEPPALTWDDYKQMEFSQCVVSETLRLGNIIKFVHRKAKTDVQFKGYDIPKGWSVIPVFAAAHLDPSVYENPQKFDPWRWQTISTGTARIDNYMPFGQGLRNCAGLELAKMEIVVFLHHLTLNFDWEMAEPDHPLAYAFPDFPKGLPIKVRRLALK | Function: Involved in the biosynthesis of spiroketal steroid and saponin natural products from cholesterol such as diosgenin and analogs (e.g. furostanol and spirostanol), plant defense compounds used as main precursors for the industrial production of steroid hormones . During the 5,6-spiroketalization of cholesterol, catalyzes the hydroxylation of cholesterol to form 16S,22S-dihydroxycholesterol and, possibly, the subsequent conversion of 16S,22S-dihydroxycholesterol into 16-oxo-22-hydroxy-cholesterol and 16-hydroxy-22-oxo-cholesterol . 16-hydroxy-22-oxo-cholesterol submit a spontaneous reaction leading to the production of furostanol-type steroid diastereomers, precursors of diosgenin .
Catalytic Activity: cholesterol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (16S,22S)-dihydroxycholesterol + 2 H(+) + 2 H2O + 2 oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54979
Sequence Length: 485
Pathway: Steroid metabolism; cholesterol metabolism.
Subcellular Location: Membrane
EC: 1.14.14.-
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A0A1D6HSP4 | MELASTMSVAMALAAAIFVVLCSVVASARGRREKALKLPPGPRGWPVLGSLGALAGALPPHRALAALAARHGPLMHLRLGSYHTVVASSADAARLVLRTHDSALADRPDTAAGEITSYGYLGIVHTPRGAYWRMARRLCATELFSARRVESFQDVRAQEMRALARGLFGCAAGRRAVAVREHVAGATMRNILRMAVGEKWSGCYGSPEGEAFRRSLDEAFAATGAVSNVGEWVPWLGWLDVQGFKRKMKRLHDLHDHFYEKILVDHEERRRLAQASGGEFVATDLVDVLLQLSEESTKLESESEARLPRDGVKALIQDIIAGGTESSAVTIEWAMAELLRHPEAMAKATDELDRVVGSGRWVAERDLPELHYIDAVVKETLRLHPVGPLLVPHYARERTVVAGYDVPAGARVLVNAWAIARDPASWPDAPDAFQPERFLGAAAAVDVRGAHFELLPFGSGRRICPAYDLAMKLVAAGVANLVHGFAWRLPDGVAAEDVSMEEHVGLSTRRKVPLFAVAEPRLPVHLYSATE | Function: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps) (By similarity). Component of the volatile terpenes biosynthesis pathways . Converts mainly nerolidol to dimethylnonatriene (DMNT) and, to a lower extent, geranyllinalool to trimethyltridecatetraene (TMTT) .
Catalytic Activity: (6E,10E)-geranyllinalool + O2 + reduced [NADPH--hemoprotein reductase] = (3E,7E)-4,8,12-trimethyltrideca 1,3,7,11-tetraene + but-3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57704
Sequence Length: 531
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.14.59
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Q42798 | MAYQVLLICLVSTIVFAYILWRKQSKKNLPPSPKALPIIGHLHLVSPIPHQDFYKLSTRHGPIMQLFLGSVPCVVASTAEAAKEFLKTHEINFSNRPGQNVAVKGLAYDSQDFLFAFAPFGPYWKFMKKLCMSELLSGRMMDQFLPVRQQETKRFISRVFRKGVAGEAVDFGDELMTLSNNIVSRMTLSQKTSENDNQAEEMKKLVSNIAELMGKFNVSDFIWYLKPFDLQGFNRKIKETRDRFDVVVDGIIKQRQEERRKNKETGTAKQFKDMLDVLLDMHEDENAEIKLDKKNIKAFIMDIFVAGTDTSAVSIEWAMAELINNPDVLEKARQEIDAVVGKSRMVEESDIANLPYLQAIVRETLRLHPGGPLVVRESSKSAVVCGYDIPAKTRLFVNVWAIGRDPNHWEKPFEFRPERFIRDGQNQLDVRGQHYHFIPFGSGRRTCPGASLAWQVVPVNLAIIIQCFQWKLVGGNGKVDMEEKSGITLPRANPIICVPVPRINPFPTI | Function: Cytochrome P450 involved in the biosynthesis of the phytoalexin glyceollin. Stereospecific for (6aR,11aR)-3,9-dihydroxypterocarpan.
Catalytic Activity: (6aR,11aR)-3,9-dihydroxypterocarpan + O2 + reduced [NADPH--hemoprotein reductase] = (6aS,11aS)-3,6a,9-trihydroxypterocarpan + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 57870
Sequence Length: 509
Subcellular Location: Membrane
EC: 1.14.14.93
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P93149 | MEPQLVAVSVLVSALICYFFFRPYFHRYGKNLPPSPFFRLPIIGHMHMLGPLLHQSFHNLSHRYGPLFSLNFGSVLCVVASTPHFAKQLLQTNELAFNCRIESTAVKKLTYESSLAFAPYGDYWRFIKKLSMNELLGSRSINNFQHLRAQETHQLLRLLSNRARAFEAVNITEELLKLTNNVISIMMVGEAEEARDVVRDVTEIFGEFNVSDFIWLFKKMDLQGFGKRIEDLFQRFDTLVERIISKREQTRKDRRRNGKKGEQGSGDGIRDFLDILLDCTEDENSEIKIQRVHIKALIMDFFTAGTDTTAISTEWALVELVKKPSVLQKVREEIDNVVGKDRLVEESDCPNLPYLQAILKETFRLHPPVPMVTRRCVAECTVENYVIPEDSLLFVNVWSIGRNPKFWDNPLEFRPERFLKLEGDSSGVVDVRGSHFQLLPFGSGRRMCPGVSLAMQEVPALLGAIIQCFDFHVVGPKGEILKGDDIVINVDERPGLTAPRAHNLVCVPVDRTSGGGPLKIIEC | Function: Catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively . Can also convert eriodictyol to luteolin .
Catalytic Activity: (2S)-liquiritigenin + O2 + reduced [NADPH--hemoprotein reductase] = 2 H(+) + H2O + licodione + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59496
Sequence Length: 523
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.14.140
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Q9SXS3 | MLVELAITLLVIALFIHLRPTLSAKSKSLRHLPNPPSPKPRLPFVGHLHLLDKPLLHYSLIDLSKRYGPLYSLYFGSMPTVVASTPELFKLFLQTHEASSFNTRFQTSAIRRLTYDNSVAMVPFGPYWKFIRKLIMNDLLNATTVNKLRPLRSQEIRKVLRVMAQSAESQVPLNVTEELLKWTNSTISRMMLGEAEEIRDIARDVLKIFGEYSLTDFIWPLKKLKVGQYEKRIDDIFNRFDPVIERVIKKRQEIRKKRKERNGEIEEGEQSVVFLDTLLDFAEDETMEIKITKEQIKGLVVDFFSAGTDSTAVATDWALSELINNPRVFQKAREEIDAVVGKDRLVDEADVQNLPYIRSIVKETFRMHPPLPVVKRKCVQECEVDGYVIPEGALILFNVWAVGRDPKYWDRPTEFRPERFLENVGEGDQAVDLRGQHFQLLPFGSGRRMCPGVNLATAGMATLLASVIQCFDLSVVGPQGKILKGNDAKVSMEERAGLTVPRAHNLICVPVARSSAVPKLFSS | Function: 2-hydroxyisoflavanone synthase, which catalyzes the hydroxylation associated with 1,2-aryl migration of flavanones. Converts liquiritigenin and naringenin into highly unstable precursors of the isoflavones daidzein and genistein. Acts only on substrates with (2S)-chirality.
Catalytic Activity: (2S)-liquiritigenin + O2 + reduced [NADPH--hemoprotein reductase] = (2R,3S)-2,4',7-trihydroxyisoflavanone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59429
Sequence Length: 523
Subcellular Location: Microsome membrane
EC: 1.14.14.87
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Q9XHC6 | MLDIKGYLVLFFLWFISTILIRSIFKKPQRLRLPPGPPISIPLLGHAPYLRSLLHQALYKLSLRYGPLIHVMIGSKHVVVASSAETAKQILKTSEEAFCNRPLMIASESLTYGAADYFFIPYGTYWRFLKKLCMTELLSGKTLEHFVRIRESEVEAFLKRMMEISGNGNYEVVMRKELITHTNNIITRMIMGKKSNAENDEVARLRKVVREVGELLGAFNLGDVIGFMRPLDLQGFGKKNMETHHKVDAMMEKVLREHEEARAKEDADSDRKKDLFDILLNLIEADGADNKLTRESAKAFALDMFIAGTNGPASVLEWSLAELVRNPHVFKKAREEIESVVGKERLVKESDIPNLPYLQAVLKETLRLHPPTPIFAREAMRTCQVEGYDIPENSTILISTWAIGRDPNYWDDALEYKPERFLFSDDPGKSKIDVRGQYYQLLPFGSGRRSCPGASLALLVMQATLASLIQCFDWIVNDGKNHHVDMSEEGRVTVFLAKPLKCKPVPRFTPFAA | Function: Heme-containing cytochrome P450 involved in the biosynthesis of soyasaponins. Hydroxylates specifically the C-24 methyl group of the triterpenes beta-amyrin and sophoradiol. No activity with lupeol, butyrospermol, tirucalla-7,21-dien-3beta-ol, taraxasterol, psi-taraxasterol, bauerenol, alpha-amyrin and multiflorenol as substrates.
Catalytic Activity: beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] = 24-hydroxy-beta-amyrin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58262
Sequence Length: 513
Subcellular Location: Membrane
EC: 1.14.14.134
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P0C8U3 | ITCCTRGTCAQHC | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
Sequence Mass (Da): 1397
Sequence Length: 13
Domain: The cysteine framework is I (CC-C-C). Alpha4/3 pattern.
Subcellular Location: Secreted
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P0C8U5 | NGRCCHPACAKYFSCGR | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
Sequence Mass (Da): 1873
Sequence Length: 17
Domain: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
Subcellular Location: Secreted
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P0DPM2 | IMYDCCSGSCSGYTGRC | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
Sequence Mass (Da): 1806
Sequence Length: 17
Domain: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
Subcellular Location: Secreted
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P0C8U9 | MFTVFLLVILATTVVPFPSDRDPASNHENSKGSNRNAWLTPEECCAAPACREMILEFCLAGEAFAAALDGFRRLPYRLSSE | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By similarity). Has possibly a distinct nAChR binding mode from other alpha-conotoxins, due to a different three residue motif (lacks the Ser-Xaa-Pro motif) (By similarity).
Sequence Mass (Da): 8937
Sequence Length: 81
Domain: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
Subcellular Location: Secreted
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P58782 | GCCGPYPNAACHPCGCKVGRPPYCDRPSGG | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin binds with high affinity to both fetal (alpha-1/beta-1/epsilon/delta subunits) and adult (alpha-1/beta-1/gamma/delta subunits) mammalian muscle nicotinic acetylcholine receptors (nAChR).
Sequence Mass (Da): 3023
Sequence Length: 30
Domain: The cysteine framework is IV (CC-C-C-C-C).
Subcellular Location: Secreted
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P69746 | CCGVPNAACHPCVCKNTC | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks the fetal muscle subtype (alpha-1/beta-1/gamma/delta subunits) (IC(50)=0.51 nM) with 600-fold greater affinity than the adult subtype (IC(50)=310 nM). It blocks the elicited currents completely and it dissociates very slowly from the fetal muscle receptor. This toxin causes an apparently irreversible paralysis upon intramuscular injection into gold fish.
Sequence Mass (Da): 1823
Sequence Length: 18
Domain: The cysteine framework is IV (CC-C-C-C-C).
Subcellular Location: Secreted
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P0C828 | MGMRMMFTVFLLVVLATTVVSTPSDRASDGRNAAVHERQKSLVPSVITTCCGYDPGTMCPPCRCTNSCG | Function: Neurotoxin with probable activity on sodium channel (Probable). Induces intense repetitive firing of the frog neuromuscular junction, leading to a tetanic contracture in muscle fiber (spastic paralysis) . In vivo, shows the same effect as the whole venom when injected on fish . Intraperitoneal injection into fish induces a period of rapid swimming followed by a spastic paralysis with stiff fibrillating fins . At high doses, the peptide is lethal to both fish and mice .
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 7373
Sequence Length: 69
Domain: The cysteine framework is IV (CC-C-C-C-C).
Subcellular Location: Secreted
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P0C1W8 | CCGVPNAACPPCVCNKTCG | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks the fetal muscle subtype (alpha-1/beta-1/gamma/delta subunits) (IC(50)=66 nM) with 1500/2000-fold greater affinity than the adult (alpha-1/beta-1/epsilon/delta) subtype (IC(50)=96000 nM). It blocks the currents completely and dissociates rapidly from the fetal muscle receptor. Has no inhibitory activity on various neuronal nAChRs. This toxin causes a reversible paralysis upon injection into gold fish.
Sequence Mass (Da): 1840
Sequence Length: 19
Domain: The cysteine framework is IV (CC-C-C-C-C).
Subcellular Location: Secreted
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P0DQY7 | APALVVTATTNCCGYTGPACHPCLCTQTC | Function: Probable neurotoxin with ion channel inhibitor activity.
PTM: O-linked glycans consist of Hex4-HexNAc2 hexasaccharides.
Sequence Mass (Da): 2900
Sequence Length: 29
Domain: The cysteine framework is IV (CC-C-C-C-C).
Subcellular Location: Secreted
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P0C2C5 | DCCGVKLEMCHPCLCDNSCKNYGK | Function: Probable neurotoxin with ion channel inhibitor activity (Probable). In vivo, elicits dose-dependently excitatory activity upon injection into fish. Its action is slowly reversible .
Sequence Mass (Da): 2664
Sequence Length: 24
Domain: The cysteine framework is IV (CC-C-C-C-C).
Subcellular Location: Secreted
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P27521 | MATVTTHASASIFRPCTSKPRFLTGSSGRLNRDLSFTSIGSSAKTSSFKVEAKKGEWLPGLASPDYLTGSLAGDNGFDPLGLAEDPENLKWFVQAELVNGRWAMLGVAGMLLPEVFTKIGIINVPEWYDAGKEQYFASSSTLFVIEFILFHYVEIRRWQDIKNPGSVNQDPIFKQYSLPKGEVGYPGGIFNPLNFAPTQEAKEKELANGRLAMLAFLGFVVQHNVTGKGPFENLLQHLSDPWHNTIVQTFN | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phosphorylation of its threonine residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27734
Sequence Length: 251
Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.
Subcellular Location: Plastid
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P0DUR2 | GCCSHPPCNVNNPHICG | Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
Sequence Mass (Da): 1752
Sequence Length: 17
Domain: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
Subcellular Location: Secreted
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Q9ULX7 | MLFSALLLEVIWILAADGGQHWTYEGPHGQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPLDLHNNGHTVQLSLPSTLYLGGLPRKYVAAQLHLHWGQKGSPGGSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHEVRHKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNYRALQPLNQRMVFASFIQAGSSYTTGEMLSLGVGILVGCLCLLLAVYFIARKIRKKRLENRKSVVFTSAQATTEA | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37668
Sequence Length: 337
Subcellular Location: Membrane
EC: 4.2.1.1
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Q9WVT6 | MLFFALLLKVTWILAADGGHHWTYEGPHGQDHWPTSYPECGGDAQSPINIQTDSVIFDPDLPAVQPHGYDQLGTEPLDLHNNGHTVQLSLPPTLHLGGLPRKYTAAQLHLHWGQRGSLEGSEHQINSEATAAELHVVHYDSQSYSSLSEAAQKPQGLAVLGILIEVGETENPAYDHILSRLHEIRYKDQKTSVPPFSVRELFPQQLEQFFRYNGSLTTPPCYQSVLWTVFNRRAQISMGQLEKLQETLSSTEEDPSEPLVQNYRVPQPLNQRTIFASFIQAGPLYTTGEMLGLGVGILAGCLCLLLAVYFIAQKIRKKRLGNRKSVVFTSARATTEA | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37505
Sequence Length: 337
Subcellular Location: Membrane
EC: 4.2.1.1
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Q99N23 | MWALDFLLSFLLIQLAAQVDSSGTWCYDSQDPKCGPAHWKELAPACGGPTQSPINIDLRLVQRDYTLKPFIFQGYDSAPQDPWVLENDGHTVLLRVNSCQQNCPAIRGAGLPSPEYRLLQLHFHWGSPGHQGSEHSLDEKHGSMEMHMVHMNTKYQSMEDARSQPDGFAILAVLLVEEDRDNTNFSAIVSGLKNLSSPGVAVNLTSTFALASLLPSALRLLRYYRYSGSLTTPGCEPAVLWTVFENTVPIGHAQVVQFQAVLQTGPPGLHPRPLTSNFRPQQPLGGRRISASPEASVRSSVSTLPCLHLALVGLGVGLRLWQGP | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 35482
Sequence Length: 324
Subcellular Location: Secreted
EC: 4.2.1.1
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P20507 | MARTGALLLVALALAGCAQACIYKFGTSPDSKATVSGDHWDHGLNGENWEGKDGAGNAWVCKTGRKQSPINVPQYQVLDGKGSKIANGLQTQWSYPDLMSNGTSVQVINNGHTIQVQWTYNYAGHATIAIPAMHNQTNRIVDVLEMRPNDAADRVTAVPTQFHFHSTSEHLLAGKIYPLELHIVHQVTEKLEACKGGCFSVTGILFQLDNGPDNELLEPIFANMPSREGTFSNLPAGTTIKLGELLPSDRDYVTYEGSLTTPPCSEGLLWHVMTQPQRISFGQWNRYRLAVGLKECNSTETAADAGHHHHHRRLLHNHAHLEEVPAATSEPKHYFRRVMLAESANPDAYTCKAVAFGQNFRNPQYANGRTIKLARYH | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 41628
Sequence Length: 377
Subcellular Location: Periplasm
EC: 4.2.1.1
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P00917 | MAHSDWGYDSPNGPZEWVKLYPIANGNNQSPIDIKTSETKHDTSLKPFSVSYDPATAKEIVNVGHSFQVKFEDSDNRSVLKDGPLPGSYRLVQFHFHWGSTDDYGSEHTVDGVKYSAELHLVHWNSSKYSSFDEASSQADGLAILGVLMKVGEANPKLQKVLDALNEVKTKGKKAPFKNFDPSSLLPSSPDYWTYSGSLTHPPLYESVTWIVCKENISISSQQLSQFRSLLSNVEGGKAVPIQHNNRPPQPLKGRTVRAFF | Function: Catalyzes the reversible hydration of carbon dioxide. Can hydrate cyanamide to urea.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 29025
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 4.2.1.1
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P00915 | MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF | Function: Catalyzes the reversible hydration of carbon dioxide . Can hydrate cyanamide to urea .
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 28870
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 4.2.1.1
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B3A0P2 | MKLQGAGCVVAAVLGALFIVNVESHFHKPELQLCKAFGEPCISYDVRSTIGPRCWFKLEFPREKCCNENGKRQSPIDIPDVKSIYKVPQKLRYSSRKFVGHLENTGIQPAFKRKVGADKVYLEGIGSPVGKRYFIENVHFHVGVRHKERQTENTLNGRSFDGEAHIVHIREDFGDLKEAANHPQGLLVISIFLSTSKGERRRDGFDDLIEMIQDVQEFEEEDGPCANVKIPDIFKFKQLIPFHPVWPICKKTFPVADDSDNSGSGVVCNFYLPNGLCGEKKESKINPNELLADDPEYYVFNGGLTTPPCSESVLWLVAKQPRKVSVFYPYVVRNMETQREGEIIGDFGNLRPLQDLNDRPVFLVRFRLKRNWEHGDTAANDNDAMDSPFSVLGIN | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 44718
Sequence Length: 395
Subcellular Location: Secreted
EC: 4.2.1.1
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Q8HY33 | MANLNWSYEGENGPEHWSKLYPIANGDNQSPIDIKTKEVKHDASLKPISVSYNPATAKEIVNVSHNFQVNFEDKDNQSVLKGGPFTGSFRLRQFHFHWGTADDHGSEHTVDGVKYSSELHIVHWNSEKYSSFSEAAEKPDGLAIIAVFIKAGQANPGLQKVIDALSSIKTKGKKAPFANFDPSLLIPQSSDYWSYHGSLTHPPLHESVTWIIYREPISASSEQLAKFRSLLSTAEGEKASSILHNHRLPQPLKGRQVKASFK | Function: Catalyzes the reversible hydration of carbon dioxide. Can hydrate cyanamide to urea.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 29175
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 4.2.1.1
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Q8XA34 | MDIIGGQHLRQMWDDLADVYGHKTALICESSGGVVNRYSYLELNQEINRTANLFYTLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQACLLVTSAQFYPMYQQIQQEDATQLRHICLTDVALPADDGVSSFTQLKNQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLVEKYSARAFWGQVQKYRATITECIPMMIRTLMVQPPSANDRQHRLREVMFYLNLSEQEKDTFCERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRAGFCYDAEIRDDHNRPLPAGEIGEICIKGVPGKTIFKEYFLNPKATAKVLEADGWLHTGDTGYRDEEGFFYFIDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFRFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIRKNLK | Function: Catalyzes the transfer of CoA to carnitine, generating the initial carnitinyl-CoA needed for the CaiB reaction cycle. Also has activity toward crotonobetaine and gamma-butyrobetaine.
Catalytic Activity: 4-(trimethylamino)butanoate + ATP + CoA = 4-(trimethylamino)butanoyl-CoA + AMP + diphosphate
Sequence Mass (Da): 58614
Sequence Length: 517
Pathway: Amine and polyamine metabolism; carnitine metabolism.
EC: 6.2.1.48
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P60977 | CISARYPCSNSKDCCSGNCGTFWTCFIRKDPCSKECLAP | Function: Causes paralysis to insect larvae (H.virescens). This toxin is active only on insects.
Sequence Mass (Da): 4296
Sequence Length: 39
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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A0A1V6PBC8 | MDEVTRTAQRSPSITETHAGETKLAGPGEKEGDVESPVDPSADSEQNRQQITGLQLFAILASVTLSAFLMLLDGSIIGVAIPNITSQFHSIDDIGWYTAAYQLASAALQPLSGKIYSSFSTKWTYLFFFGLFELGSLICGVANSSSMLIGGRAVAGLGSSGLLNGGMTIIAGAVPLEKRPVYTGIYLGISQLGIVCGPLIGGALTEYTTWRWCFYINLPVGAVTAILLLFLQVPELTEKPRFTFALVRRVIPELDLIGFTLFAPAAIMVLLALYYGGNDFPWDSSQVIGLFCGAGVTIIVFALWERRVGDRAMIPPSMVSHRIVYTSAINGAALVASILVAAQYLPIYFQGVRGYGPAMSGVNTLPGILSQLLTVILSGVLVQKVGYYLPFAAAGSAISAVGNGIVTLFSPTTPTAKWIGYQIVLGSGRGIGMQMGIIAIQNLLPPEKISVGIAFMIFCQNFAGAIFVVVGEVIFTQQLVKQIQAHAPSVKVDAALAAGASSSSLRALVPPGSPELQGVLLAFSNSVDRVFYLLMSLSLAGFVAAFGMGWVDTRKKNKSETE | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicyclic decalin containing polyketide and a linear 12 carbon dioic acid structure . Required for the secretion of calbistrin A and calbistrin C, as well as of related compounds decumbenone A, B and C .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59520
Sequence Length: 562
Subcellular Location: Cell membrane
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O86447 | MSILGLNGAPVGAEQLGSALDRMKKAHLEQGPANLELRLSRLDRAIAMLLENREAIADAVSADFGNRSREQTLLCDIAGSVASLKDSREHVAKWMEPEHHKAMFPGAEARVEFQPLGVVGVISPWNFPIVLAFGPLAGIFAAGNRAMLKPSELTPRTSALLAELIARYFDETELTTVLGDAEVGALFSAQPFDHLIFTGGTAVAKHIMRAAADNLVPVTLELGGKSPVIVSRSADMADVAQRVLTVKTFNAGQICLAPDYVLLPEESLDSFVAEATRFVAAMYPSLLDNPDYTSIINARNFDRLHRYLTDAQAKGGRVIEINPAAEELGDSGIRKIAPTLIVNVSDEMLVLNEEIFGPLLPIKTYRDFDSAIDYVNSKQRPLASYFFGEDAVEREQVLKRTVSGAVVVNDVMSHVMMDTLPFGGVGHSGMGAYHGIYGFRTFSHAKPVLVQSPVGESNLAMRAPYGEAIHGLLSVLLSTEC | Function: Catalyzes the NAD(+)-dependent oxidation of coniferyl aldehyde to ferulic acid and which is induced during growth with eugenol as the carbon source.
Catalytic Activity: (E)-coniferaldehyde + H2O + NADP(+) = (E)-ferulate + 2 H(+) + NADPH
Sequence Mass (Da): 51987
Sequence Length: 481
EC: 1.2.1.68
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Q9NYX4 | MVKLGCSFSGKPGKDPGDQDGAAMDSVPLISPLDISQLQPPLPDQVVIKTQTEYQLSSPDQQNFPDLEGQRLNCSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPTQAGAAAAATEPPGKPSAKAEKEAARKAAGSAAPPPAQ | Function: Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis.
PTM: Glycosylated.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23434
Sequence Length: 217
Subcellular Location: Cytoplasmic vesicle membrane
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P58821 | MVKLGCSFSGKPGKETGDQDGAAMDSVPLISPLDVSQLQPSFPDQVVIKTQTEYQLTSADQPKKFADLEGQRLACSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTEMPAIWGNSYRAGKEEHKGTTPAAMTVSTAAAAAAAEGNEPSGKPLDMREKEDPQKAEDVPSQSPK | Function: Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24718
Sequence Length: 226
Subcellular Location: Cytoplasmic vesicle membrane
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G5EGK5 | MSPRPEDDDLVIEPADDEGLHYGNASMEGTSTGQRPYIRLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRVNNVPDAVKLSQKKGSHHSTKHIAFDEYEDYEMMDRGRLPDEEDADLYRVPDSAAGSNYAPVAVSERWLDGIKYRVGDCVQYRGEACRQYLSNKFVMMTNESREEMYDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVCESDSNNQIVSICKHDCDVIQNDECPSELALAAQHELVGDTPKALFPLCSRLSSTSNCIPVMSTALQSSPVAEVNRGHLTHWCYVNSGTQYEGTVAQTSSGKQCAPWIDSTSRDFNVHRFPELMNSKNYCRNPGGKKSRPWCYSKPMGQEEYCDVPQCPSDMYPHLNDKKVEGSTKGGVSESVTALWDSLDPTMQVALVGGGVFFSLLLLLLFCCACCCRAKKKSQKTRHQNAHCSSAPSVINSAANSAYYRKLNGTSTPIMGRVPPHVEMTSLLPSAQHLGPPPYPMDQHLQQARRFPSQEPIDDNSYKVFEITPSQLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLASPAHSILQQHNNRAGSHSGSSGAGRPPTHQRGYPSQKLHRRVEGASPLMKRHDANYAYSEDGDSD | Cofactor: Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor.
Function: Tyrosine-protein kinase receptor for Wnt ligands egl-20, mom-2 and cwn-1 . Involved in the final positioning of migrating ALM, CAN, BDU and HSN neurons during development . Involved in the anterior-posterior migration of QR neuroblast descendants, QR.p and QR.pa, by maintaining QR.p cell polarization, probably through mig-2 . In addition, plays a role in ASI sensory neuron positioning and functions . Regulates asymmetric division of V cells (seam cells) and CA/CP neuroblast, and axon outgrowth . Probably by acting as a receptor for Wnt ligand cwn-2, plays a role in the positioning of the nerve ring by controlling axon guidance of SIA and SIB neurons . Involved in synapse plasticity by regulating delivery and/or stabilization of acetylcholine receptor acr-16 at post-synaptic membrane sites and the distribution of synaptic vesicles at pre-synaptic release sites . Probably by acting as a receptor for Wnt ligands cwn-1 and cwn-2, negatively regulates developmental neurite pruning of AIM neurons . Plays a role in ALM neuron polarity . By binding Wnt ligands mom-2, cwn-1 and egl-20 and thereby restricting their availability, negatively regulates Wnt signaling. This mechanism is involved in HSN neuron and QR neuronal descendent migration, and in vulva development . Involved in dauer formation, locomotion, tail morphology and egg-laying . May be involved in distal tip cell (DTC) migration during the development of the posterior gonad .
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
PTM: Autophosphorylated at tyrosine residues which are probably located in the activation loop (residues 724-732). Autophosphorylation does not increase kinase activity in vitro.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 103864
Sequence Length: 928
Domain: The FZ domain is involved in binding to Wnt ligands egl-20, cwn-1 and mom-2 . The domain is required for the final positioning of migrating ALM, CAN, BDU and HSN neurons, and maybe QR neuroblast descendants during development and for neurite pruning of AIM neurons . Required for the establishment of ALM polarity .
Subcellular Location: Cell membrane
EC: 2.7.10.1
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P16640 | MNANDNVVIVGTGLAGVEVAFGLRASGWEGNIRLVGDATVIPHHLPPLSKAYLAGKATAESLYLRTPDAYAAQNIQLLGGTQVTAINRDRQQVILSDGRALDYDRLVLATGGRPRPLPVASGAVGKANNFRYLRTLEDAECIRRQLIADNRLVVIGGGYIGLEVAATAIKANMHVTLLDTAARVLERVTAPPVSAFYEHLHREAGVDIRTGTQVCGFEMSTDQQKVTAVLCEDGTRLPADLVIAGIGLIPNCELASAAGLQVDNGIVINEHMQTSDPLIMAVGDCARFHSQLYDRWVRIESVPNALEQARKIAAILCGKVPRDEAAPWFWSDQYEIGLKMVGLSEGYDRIIVRGSLAQPDFSVFYLQGDRVLAVDTVNRPVEFNQSKQIITDRLPVEPNLLGDESVPLKEIIAAAKAELSSA | Function: The oxidation of camphor by cytochrome P450-CAM CamC requires the participation of the flavoprotein, putidaredoxin reductase CamA, and the iron-sulfur protein, putidaredoxin CamB, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
Catalytic Activity: H(+) + NAD(+) + 2 reduced [2Fe-2S]-[putidaredoxin] = NADH + 2 oxidized [2Fe-2S]-[putidaredoxin]
Sequence Mass (Da): 45579
Sequence Length: 422
Pathway: Terpene metabolism; (R)-camphor degradation.
EC: 1.18.1.5
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O80673 | MGICHGKPVEQQSKSLPVSGETNEAPTNSQPPAKSSGFPFYSPSPVPSLFKSSPSVSSSVSSTPLRIFKRPFPPPSPAKHIRAFLARRYGSVKPNEVSIPEGKECEIGLDKSFGFSKQFASHYEIDGEVGRGHFGYTCSAKGKKGSLKGQEVAVKVIPKSKMTTAIAIEDVSREVKMLRALTGHKNLVQFYDAFEDDENVYIVMELCKGGELLDKILQRGGKYSEDDAKKVMVQILSVVAYCHLQGVVHRDLKPENFLFSTKDETSPLKAIDFGLSDYVKPDERLNDIVGSAYYVAPEVLHRTYGTEADMWSIGVIAYILLCGSRPFWARTESGIFRAVLKAEPNFEEAPWPSLSPEAVDFVKRLLNKDYRKRLTAAQALCHPWLVGSHELKIPSDMIIYKLVKVYIMSTSLRKSALAALAKTLTVPQLAYLREQFTLLGPSKNGYISMQNYKTAILKSSTDAMKDSRVFDFVHMISCLQYKKLDFEEFCASALSVYQLEAMETWEQHARRAYELFEKDGNRPIMIEELASELGLGPSVPVHVVLQDWIRHSDGKLSFLGFVRLLHGVSSRTLQKA | Function: May play a role in signal transduction pathways that involve calcium as a second messenger (By similarity). Serine/threonine kinase that phosphorylates histone H3. Confers thermotolerance; involved in the heat-shock-mediated calmodulin-dependent signal transduction leading to the activation of heat-shock transcription factors (HSFs); phosphorylates HSFA1A.
PTM: Autophosphorylated.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 64315
Sequence Length: 576
Domain: There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (390-420) inactivates kinase activity under calcium-free conditions (By similarity).
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9LJL9 | MGGCTSKPSSSVKPNPYAPKDAVLQNDDSTPAHPGKSPVRSSPAVKASPFFPFYTPSPARHRRNKSRDGGGGESKSVTSTPLRQLARAFHPPSPARHIRDVLRRRKEKKEAALPAARQQKEEEEREEVGLDKRFGFSKELQSRIELGEEIGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVLHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKIDIPFDILIFKQIKAYLRSSSLRKAALMALSKTLTTDELLYLKAQFAHLAPNKNGLITLDSIRLALATNATEAMKESRIPDFLALLNGLQYKGMDFEEFCAASISVHQHESLDCWEQSIRHAYELFEMNGNRVIVIEELASELGVGSSIPVHTILNDWIRHTDGKLSFLGFVKLLHGVSTRQSLAKTR | Function: May play a role in signal transduction pathways that involve calcium as a second messenger.
PTM: Autophosphorylated.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 67207
Sequence Length: 599
Domain: There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (411-441) inactivates kinase activity under calcium-free conditions (By similarity).
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9ZUZ2 | MGQCYGKVNQSKQNGEEEANTTTYVVSGDGNQIQPLTPVNYGRAKNTPARSSNPSPWPSPFPHGSASPLPSGVSPSPARTSTPRRFFRRPFPPPSPAKHIKASLIKRLGVKPKEGPIPEERGTEPEQSLDKSFGYGKNFGAKYELGKEVGRGHFGHTCSGRGKKGDIKDHPIAVKIISKAKMTTAIAIEDVRREVKLLKSLSGHKYLIKYYDACEDANNVYIVMELCDGGELLDRILARGGKYPEDDAKAIVVQILTVVSFCHLQGVVHRDLKPENFLFTSSREDSDLKLIDFGLSDFIRPDERLNDIVGSAYYVAPEVLHRSYSLEADIWSIGVITYILLCGSRPFWARTESGIFRTVLRTEPNYDDVPWPSCSSEGKDFVKRLLNKDYRKRMSAVQALTHPWLRDDSRVIPLDILIYKLVKAYLHATPLRRAALKALAKALTENELVYLRAQFMLLGPNKDGSVSLENFKTALMQNATDAMRESRVPEILHTMESLAYRKMYFEEFCAAAISIHQLEAVDAWEEIATAGFQHFETEGNRVITIEELARELNVGASAYGHLRDWVRSSDGKLSYLGFTKFLHGVTLRAAHARPR | Function: May play a role in signal transduction pathways that involve calcium as a second messenger (By similarity). Serine/threonine kinase that phosphorylates histone H3 an GLN1-1.
PTM: Autophosphorylated.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 66600
Sequence Length: 595
Domain: There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (409-439) inactivates kinase activity under calcium-free conditions (By similarity).
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q94AH1 | MRVLSEIAESPFVISRLSPDSTATGGFIGGWVGKCHGFLHNTVLVLASILFVAYLAYEAKKSLSKLSNRRSYIMIAYYGFLWLVSLLNLAWCCLQAWECTPGKEVIWNLLTLFTTSGMLFLEVSLVAFLFQGNYASGAEALTRTFLISGLVIGLDLLLKAIYLFGFGVPLFIDNNEHIHKFKWGLWVIHKLLLAGIYGMIFFMYNSKWRERLPARPAFYKYITVMLALNGLSLFACALTANGAHFGLWLYGITSVCYHAFYLPLLYVTFLADFFQEEDLNLENVYYSEMKDAGFFDADWE | Function: Plays a role in plants and microbes interactions . G-protein coupled melatonin receptor involved in root growth mediated by the bacterial quorum-sensing signals N-acyl-homoserine lactones (AHLs) . Binds to melatonin . Phytomelatonin receptor required, in collaboration with GPA1, for melatonin-mediated stomatal closure involving H(2)O(2) and Ca(2+) signals . Essential for melatonin-mediated plant response to osmotic stress probably by activating reactive oxygen species (ROS) scavenging ability .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34063
Sequence Length: 300
Subcellular Location: Cell membrane
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Q9LZ39 | MTILPFLAAVFVLQLLSTLTVAEIKSFTISNDSRPVILLEKFGIIEIGHVTVSVSSVSVLSPILDSSKLGFFVLSEESLPHVLLELQQNFSFCVLDSHYILHFFTFVDLSPPPRSQFSKSYPITSPNDYSLFFANCVPETRVSMKVHTEIYHDLYPNGSRDYLLAGSAQLPGLYLVFFLCYLSFLCFWLCFCWNHKQIVKRIHLLMTALLLVKSLTLICAAVYKHYVKVTGTAHGWNIVFYIFQFISVVLLFMVIVLIGNGWSFLKPKLHVKEKKLLVIVVPLQVLANIASIVIGETGPYTQDWVSWNQIFFLADITCCCAIVFAMVWSMCCLRETSKTDGKAVKNLAKLPVLRKFYVLVIGYLFFTRIVVVVMKMKADFTYQWVSNAAEEIATLSFYCLMFYMFRPIEKNEYCDVDDEEEIVELSLK | Function: G-protein coupled receptor . Plays a role in plants and microbes interactions (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48883
Sequence Length: 428
Subcellular Location: Membrane
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F4JY11 | MAKMPLSVVVFLLFSAAFLAVSMAEIKSLVISDDARPMILFEKFGFTHTGHVTVSISSVSVVSTSSDPNPEASRLGFFLLSEESLLQVLLEIQQNPRFCVLDSHYVTHLFTFRDLSPPPNSRFNQSYPVTSPNEYSLFFANCVPETKVSMAVRTEMYNKDPNGSKDYLPAGSTQLPTLYSFFFLCYVAFLGFWSYTCWTNKQTVHRIHLLMAGLLLIKSLNLICAAEDKHYVKITGTPHGWDILFYIFQFIRVVLLFTVIILIGTGWSFLKPFLQEKEKNVLIIVIPLQVLANIASIVIGETGPFIKDWVTWNQVFLLVDIICCCAIIFPIVWSIRSLRETSKTDGKAARNLSKLTLFRQFYIVVIGYLYFTRIVVFALKTIAAYKYQWVSFAAEEIVSLVFYVIMFHMFRPEEKNEYFAVDDDEEEAAALALRDEEFEL | Function: Plays a role in plants and microbes interactions . G-protein coupled receptor involved in root growth mediated by the bacterial quorum-sensing signals N-acyl-homoserine lactones (AHLs) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50245
Sequence Length: 440
Subcellular Location: Membrane
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F4K2U8 | MRVLDEIAESPFLISPLNPNSTANGYRWVDKCHGFLHNTVLVAASLFFVAYLAYEAKKSLSKLSNRRSYIMIAYYGCLWLVSLLNLAWCCLQGWECTPGKEVVWNLLTLFTTSGMLFLEVSLVAFLFQGNYASGAEALTRTFLISGFIVALDLLLKAIFLFGFGVPLFIDNNENGKTFKWGLWIIHKLLLTGVYGMVFLMYNSRWREKLPARPAFYNYIIIMFALYSLYLVASAFTANNAHFGFWLYGIMSVCYHALYLPLLYITFLADFFQEEDLNLENVYYSEMKDAGFFDSDWE | Function: G-protein coupled receptor . Plays a role in plants and microbes interactions (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34138
Sequence Length: 297
Subcellular Location: Membrane
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P0DPE4 | MAILQIGAGGVGWVVAHKAAQNNDVLGDITIASRTVGKCEKIIESIQKKNNLKDSTKKLEARAVNADDVDSLVALIKEVQPDLVINAGPPWVNMSIMEACYQAKVSYLDTSVAVDLCSEGQQVPQAYDWQWGYREKFEEAGITGILGAGFDPGVVSVFAAYAVKHLFDEIDTIDVMDVNAGDHGKKFATNFDPETNMLEIQGDSFYWENGEWKQVPCHSRMLEFEFPNCGSHKVYSMAHDEVRSMQEFIPAKRIEFWMGFGDRYLNYFNVMRDIGLLSPDPLTLHDGTVVQPLHVLKALLPDPTSLAPGYTGLTCIGTWVQGKKDGKERSVFIYNNADHEVAYEDVEHQAISYTTGVPAITAALQFFRGKWADKGVFNMEQLDPDPFLETMPSIGLDWHVQELEPGQPVIHKLK | Function: Involved in norspermidine biosynthesis. Catalyzes the synthesis of carboxynorspermidine from L-aspartate 4-semialdehyde and 1,3-diaminopropane. Is also slightly active with putrescine as a substrate.
Catalytic Activity: carboxynorspermidine + H2O + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH + propane-1,3-diamine
Sequence Mass (Da): 46105
Sequence Length: 414
EC: 1.5.1.43
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Q8WVQ1 | MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLCSHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQEENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDVVNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVALKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI | Function: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP . Involved in proteoglycan synthesis .
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate
Sequence Mass (Da): 44840
Sequence Length: 401
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.6.1.6
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Q8VCF1 | MPIQPFDQREWNEPMHSLRISVGGLPVLASMTKATDPRFRPRWRVILTSFVGAALLWLLYSHHQGPVPGRPPTHNAHNWRLSQQRISHYNDTYPLSPPQRTPGGIRYRIAVIADLDTGSRAQEENTWFSYLKKGYLTLSDSGDRVSVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVIYQIEGTKAVPWVILSDGDGTVEKGFKAEWLAVKDEHLYVGGLGKEWTTTTGEVMNENPEWVKVVGHRGSVDHENWVSSYNALRAAAGIRPPGYLIHESACWSDTLQRWFFLPRRASHERYSEKDDERKGSNLLLSAAQDFRDISVRQVGTLIPTHGFSSFKFIPNTDDQIIVALKSEEDNGRIATYVMAFTLDGRFLLPETKIGTVKYEGIEFI | Function: Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > IDP >> UTP > CDP = GTP = ITP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.
Catalytic Activity: a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 45653
Sequence Length: 403
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.6.1.6
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P00789 | MMPFGGIAARLQRDRLRAEGVGEHNNAVKYLNQDYEALKQECIESGTLFRDPQFPAGPTALGFKELGPYSSKTRGVEWKRPSELVDDPQFIVGGATRTDICQGALGDCWLLAAIGSLTLNEELLHRVVPHGQSFQEDYAGIFHFQIWQFGEWVDVVVDDLLPTKDGELLFVHSAECTEFWSALLEKAYAKLNGCYESLSGGSTTEGFEDFTGGVAEMYDLKRAPRNMGHIIRKALERGSLLGCSIDITSAFDMEAVTFKKLVKGHAYSVTAFKDVNYRGQQEQLIRIRNPWGQVEWTGAWSDGSSEWDNIDPSDREELQLKMEDGEFWMSFRDFMREFSRLEICNLTPDALTKDELSRWHTQVFEGTWRRGSTAGGCRNNPATFWINPQFKIKLLEEDDDPGDDEVACSFLVALMQKHRRRERRVGGDMHTIGFAVYEVPEEAQGSQNVHLKKDFFLRNQSRARSETFINLREVSNQIRLPPGEYIVVPSTFEPHKEADFILRVFTEKQSDTAELDEEISADLADEEEITEDDIEDGFKNMFQQLAGEDMEISVFELKTILNRVIARHKDLKTDGFSLDSCRNMVNLMDKDGSARLGLVEFQILWNKIRSWLTIFRQYDLDKSGTMSSYEMRMALESAGFKLNNKLHQVVVARYADAETGVDFDNFVCCLVKLETMFRFFHSMDRDGTGTAVMNLAEWLLLTMCG | Cofactor: Binds 3 Ca(2+) ions.
Function: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
PTM: The N-terminus is blocked.
Catalytic Activity: Broad endopeptidase specificity.
Sequence Mass (Da): 80352
Sequence Length: 705
Subcellular Location: Cytoplasm
EC: 3.4.22.52
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P43920 | MTQEYSTLRNNISMLGRFLGETINDAQGEDILELIENIRKLSRNSRAGDDKARQALLDTLGSISNENIIPVARAFSQFLNLTNIAEQYQTISREHSLAQSSSQSLSELFKRLKEQNASVEEVHKTVEKLLIELVLTAHPTETTRRSLIHKHIEINKCLSKLEHHDLTEKERNIIERLLLRLIAEAWHTNEIRTVRPTPFDEAKWGFAMLENSLWQAVPEFLRQLNETAREFLGYDLSVGLKPVRISSWMGGDRDGNPFVTAQITKKVLYFARWKAADLFLQDISKLADELSMMKCSDEFRDKYGEHLEPYRFVVKNLRNQLTATLAYFDDHLSNRTPRVSESEIILEDNQLWEPLYDCYQSLIQCGMRIIANGSLLNILHRISCFGVTLSQMDIRQESTRHTDAIAEITRYIGLGDYSQWMEDDKQAFLIRELSSRRPLIPQNWTPSPETKEILDTCKVIAQQKQGVIACYVISMARSASDVLAVHLLLKESGVPYHIPVVPLFETLEDLDAAEKVMTQLFNVGWYRGVINNRQMVMIGYSDSAKDAGMMAASWAQYRAQEALVNLTEKLGIELTLFHGRGGTIGRGGAPAHAALLSQPPRSLKNGLRVTEQGEMIRFKLGLPAVAVETFDLYASAILEANLLPPPEPKPEWRTIMDELSTISCDIYRGVVRGDKDFVPYFRSATPEQELSKLPLGSRPAKRNPNGGVESLRAIPWIFAWMQNRLMLPAWLGAGAAIRQVIEQGKGDIIHKMCENWPFFSTRIGMLEMVFSKSDTWLSQQYDQRLVKKELWYLGENLRKQLEDDIQTVLSLSHQSELMSDLPWIADSIALRNIYTDPLNLLQVELLHRFRENPEQVNPDVEQALMITITGIAAGMRNTG | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 100055
Sequence Length: 879
EC: 4.1.1.31
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A1U2U4 | MTELHPDLRENVRLLGDLLGQSILRFPGQDCYDRIEEIRAAAKADRRQESGSGQRLVKLLGQLSDDELLPVTRAFNQFLNLANLAEQYHGIRRKQGHPSDLMVESLGEVFDRLKSGGIDPQELHRKVADLRIEFVLTAHPTEVARRTLILKYDEMSDCLSRLDHDDLMPGEREEIVDRLSLLIAEAWHTDEIRHERPTAVDEAKWGFAVIENSLWQALPKFLRSLDTSLSEATGQGLPLQVSPIRIASWMGGDRDGNPNVTHEVTREVFLLGRWMAADLYLRDIQALRAELSMWQASDELRAEVGDSREPYRQVLAQLRERLIKTREWAEASVKGEPADDSGILFENEDLTGPLELCYRSLMECGLETIANGPLLDTIRRAHTFGLPLIRLDIRQEASRHAEAVAEMVNYLGLGDYLSWSEQERQAFLVKELKGRRPLVPRNWQPSEPVREVLATCEVVAGQTPEALGSYVISMASKPSDVLNVILLLREAGMAFPMRVVPLFETLDDLKGAPDSMAALYEVDWYREYCSGRQEVMIGYSDSSKDAGQLMAAWAQYQAQEKLTEVANRYGVHLTLFHGRGGTVGRGGGPANRAILSQPPGSVNGSFRITEQGEMIRFKFGLPRLAVQSLTLYTTAVIEATLAPPPVPKDEWREVMDWLTERSLRSYREVVRENPDFVPYFRQVTPETALGKLALGSRPARRKATGGVESLRAIPWIFAWTQMRLMLPSWLGSDVALEQAAQADRLPELREMMQGWPFFRTYVDMLEMVLAKADLRIASYYEQTLVEDEHLLALGQSLRQRLQGCIERLLELKQQQTLLEQEPVFAHSMKVRNPYTDPLHYLQAELLRRDRESEGAGKVPELVERALKVTMAGISAGMRNTG | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 99626
Sequence Length: 881
EC: 4.1.1.31
|
Q49136 | MTKTLHARPSAATDTTFAPPVITGTATEDALEILFHALLDVARRHDPELEDVLHGRADISSFTPEMLARALQVQGIWFQLVSIAEQNAAMRRRRHVERDQGREALNGSFAKVLAEASARGIGPQQIHALLKDLRIRPTITAHPTEGKRVTVLEKLRRIYLVLRELELPRWTERERNGLMNELRDQIELIWMTGELHLEKATVEREVAWGLHFFDETLFEMLPEMLLSLEESLAQYYPDETFEVPPFFQFGSWIGGDRDGNPYVTASVTRETLQRNALASLRRYRDGITHLGRVLSITERSLPVPETFRSELAHMLAESGDARAIANRNPGEAYRQFLSCVLRKLEATIARNKGARSVGPDYPSADGLINDLRTLEKGLADAKCGALATDIVRPVRRMVEIFRFSTVRLDLRENSTRTTKTLHALWKLRNGDREPPALDSPAWKDWLLTELARPRTPETSFEDFADRLPDDARETLATFALVGEMRDTLDREAFGAFILSMTRSTVDVLGAYLLAKEAGIFLDTTGTEICPLPIVPLFETIDDLRAAPAIMKELLGIPVVRRSTRWQGGVQEVMIGYSDSNKDGGFIASNWELYKAQVRLTTLGNHLGVPIAFFHGRGGSVSRGGVPTHRGIAAQPPGSIQGRFRITEQGEVVSFKYANRGTAAYQMELLAASVFEHALLSEGNGNGSRAEFDDALEALSGASRAAYVNLLQAEGLVDYFQAASPLDEISLLNIGSRPARRFGAKSLSDLRAIPWVFAWSQNRHVITGWYGVGSGLKSFIDVRGEAGEALLRRLFRDCRVFRLVLDEVEKTLLMVDLEIARDYAGLVEDAGIRARIFGMIEAEYALTREMVLRVSGDSELAQRFPQFSERLRGRLPTINQVSREQVELLRRYRSETDEDKREAVKSALLLSINCIAVGFGATG | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 103021
Sequence Length: 922
EC: 4.1.1.31
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P46710 | MVEFSDAILEPIGAVQRTRVGREATEPMRADIRLLGTILGDTLREQNGDEVFDLVERVRVESFRVRRSEIDRADMARMFSGLDIHLAIPIIRAFSHFALLANVAEDIHRERRRHIHLDAGEPLRDSSLAATYAKLDLAKLDSATVADALTGAVVSPVITAHPTETRRRTVFVTQRRITELMRLHAEGHTETADGRSIERELRRQILTLWQTALIRLARLQISDEIDVGLRYYSAALFHVIPQVNSEVRNALRARWPDAELLSGPILQPGSWIGGDRDGNPNVTADVVRRATGSAAYTVVAHYLAELTHLEQELSMSARLITVTPELATLAASCQDAACADEPYRRALRVIRGRLSSTAAHILDQQPPNQLGLGLPPYSTPAELCADLDTIEASLCTHGAALLADDRLALLREGVGVFGFHLCGLDMRQNSDVHEEVVAELLAWAGMHQDYSSLPEDQRVKLLVAELGNRRPLVGDRAQLSDLARGELAVLAAAAHAVELYGSAAVPNYIISMCQSVSDVLEVAILLKETGLLDASGSQPYCPVGISPLFETIDDLHNGAAILHAMLELPLYRTLVAARGNWQEVMLGYSDSNKDGGYLAANWAVYRAELALVDVARKTGIRLRLFHGRGGTVGRGGGPSYQAILAQPPGAVNGSLRLTEQGEVIAAKYAEPQIARRNLESLVAATLESTLLDVEGLGDAAESAYAILDEVAGLARRSYAELVNTPGFVDYFQASTPVSEIGSLNIGNRPTSRKPTTSIADLRAIPWVLAWSQSRVMLPGWYGTGSAFQQWVAAGPESESQRVEMLHDLYQRWPFFRSVLSNMAQVLAKSDLGLAARYAELVVDEALRRRVFDKIADEHRRTIAIHKLITGHDDLLADNPALARSVFNRFPYLEPLNHLQVELLRRYRSGHDDEMVQRGILLTMNGLASALRNSG | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Mass (Da): 102516
Sequence Length: 934
EC: 4.1.1.31
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Q9JGF1 | MAGGATAPAGAKPKQPKQKQKKPSSQARKKPSQKQKAMKPVKQELRKVEKQVRVLKARTNGPKVNDTMKTTVTVGTLVGQTQSGLNRQLRVSFNPLLMKSTEGGSTTPLSIRASMYEMWKPLSVEIFATPLSGFSSVVGSVGFMVITLNGLEASADSIDTIKARRHVQMALGRPYRLKLSARELAGPREGWWLVDTSEAPADAYGPAVDLMLAYATENLLGTSSGSTTSYTGTLWQVEMRVTYAFSTYNPKPGLQTLVSQSITGGQTVTIQPSPDDGSLIMTTNSQQVLALLTPRVAGQRKGKSQTIWAIAGSAVDAAATVLGPWGYLLKGGFWLVRLIFGGSSARNTTTRQYQIYPSVESALTDQPIFGNSTGTQSVTVPICHITEVVNPNAESNNLPPPTTGAQPQPQPPAPIEEILLPLAELTGQPGVPPLYTFDGSSYTPPTNWLGSTILLTGIPAHKRVTGNLAKFGVTNLQMSKVAATALEIYDFTDFGVFFGTGSYLSEGGIHTGKTLIYSLMSGQTPNPWLAANQSGTTWYMPSWAGFPQPGQGDYFLQMQDVTDTTTHTTSVNVYFLVAYRQSRRLIAFFNTGGTARPAPTSMLCLYNVDCGRAPQTPYPTFQSTLQSLNQIGVDAKSDPDSDDDISLAGSVIGDEFDSVDHLEREREDLMRRLRDLDLRRFQI | Function: Capsid polyprotein VP90: self-assembles to form an icosahedral T=3 capsid.
PTM: Specific enzymatic cleavages in vivo yield mature protein(s). VP90 undergoes a cascade of proteolytic cleavages presumably mediated by host caspases and extracellular proteases (By similarity).
Sequence Mass (Da): 73909
Sequence Length: 683
Subcellular Location: Virion
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P69466 | MDKSESTSAGRNRRRRPRRGSRSAPSSADANFRVLSQQLSRLNKTLAAGRPTINHPTFVGSERCRPGYTFTSITLKPPKIDRGSYYGKRLLLPDSVTEYDKKLVSRIQIRVNPLPKFDSTVWVTVRKVPASSDLSVAAISAMFADGASPVLVYQYAASGVQANNKLLYDLSAMRADIGDMRKYAVLVYSKDDALETDELVLHVDIEHQRIPTSGVLPV | Function: Capsid protein. Probably binds RNA and plays a role in packaging (By similarity).
Sequence Mass (Da): 24141
Sequence Length: 218
Domain: The N-terminal arginine-rich stretch does not seem to be the major RNA-binding region that allows formation of an infectious ribonucleoprotein complex.
Subcellular Location: Virion
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Q06934 | MDKSGSPNASRTSRRRRPRRGSRSASGADAGLRALTQQMLKLNKTLAIGRPTLNHPTFVGSESCKPGYTFTSITLKPPEIEKGSYFGRRLSLPDSVTDYDKKLVSRIQIRINPLPKFDSTVWVTVRKVPSSSDLSVAAISAMFGDGNSPVLVYQYAASGVQANNKLLYDLSEMRADIGDMRKYAVLVYSKDDNLEKDEIVLHVDVEHQRIPISRMLPT | Function: Capsid protein. Probably binds RNA and plays a role in packaging (By similarity).
Sequence Mass (Da): 24202
Sequence Length: 218
Domain: The N-terminal arginine-rich stretch does not seem to be the major RNA-binding region that allows formation of an infectious ribonucleoprotein complex.
Subcellular Location: Virion
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P10470 | MSTVVVKGNVNGGVQQPRRRRRQSLRRRANRVQPVVMVTASGQPRRRRRRRGGNRRSRRTGVPRGRGSSETFVFTKDNLMGNSQGSFTFGPSLSDCPAFKDGILKAYHEYKITSILLQFVSEASSTSSGSIAYELDPHCKVSSLQSYVNKFQITKGGAKTYQARMINGVEWHDSSEDQCRILWKGNGKSSDTAGSFRVTIRVALQNPK | Function: Major capsid protein that self-assembles to form an icosahedral capsid with a T=3 symmetry, about 23 nm in diameter, and consisting of 180 capsid proteins monomers. Most of the 180 monomers are the major capsid protein, but a small percentage contain the minor capsid protein, which has a long C-terminal extension.
Sequence Mass (Da): 23228
Sequence Length: 208
Domain: The N-terminus like those of many plant virus capsid proteins is highly basic. These regions may be involved in protein-RNA interaction.
Subcellular Location: Virion
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P0DQM5 | MVRLLAKLLRSTIHGSNGVSLDAVSSTHGTPGFQTPDARVISRFGFN | Function: Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP) . Inhibits transcription by binding in RNAP secondary channel, where it sterically blocks the folding of the trigger loop, which is essential for efficient catalysis . In contrast to MccJ25, does not restrict access of nucleotide substrates to the catalytic center and shows a non-competitive mode of inhibition . Shows activity against closely related Gram-negative Burkholderia and Pseudomonas strains . Is not active against Gram-positive bacteria .
PTM: It is assumed that the two processing enzymes CapB/CapC convert the precursor protein CapA into the mature lasso peptide capistruin. CapB is assumed to cleave the precursor protein CapA and to set an N-terminal Gly free, whose a-NH2 group acts as the nucleophile in the subsequent cyclization reaction. CapC is most likely involved in the side-chain carboxyl group activation of aspartic acid at position 9 generating the electrophile for the condensation reaction. CapD may export capistruin outside of the producing cells.
Sequence Mass (Da): 5013
Sequence Length: 47
Domain: Is composed of a ring composed by 9 residues, and a tail of 10 residues (Probable). The peptide is threaded when the C-terminal tail is inserted throught the isopeptide-bonded ring (Probable).
Subcellular Location: Secreted
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P54654 | MSEATIVELLKRLDQATTRLEAVEKSIASGVASSSSSSSPSSGAAGPSSASVKEFQNLVDQHITPFVALSKKLAPEVGNQVEQLVKAIDAEKALINTASQSKKPSQETLLELIKPLNNFAAEVGKIRDSNRSSKFFNNLSAISESIGFLSWVVVEPTPGPHVAEMRGSAEFYTNRILKEFKGVNQDQVDWVSNYVNFLKDLEKYIKQYHTTGLTWNPKGGDAKSATPAPASSAPAAPVAPAVSSTPVESKKGPGLGAVFGELSKGDGVTSGLKKVTNDMKSKNFTDKSSVVKAADTKVAKVDAPSRPAVFALQGNKWSIEYQVNNKEIVIAEPDSRQTVYIFQCVNSLVQIKGKVNAITLDGCKKTSIVFENAISSCEVVNCNGVEIQVTGRVPSIAIDKTSGCQIYLSKDSLETEIVSSKSSEMNVLIPGATENDDLVELAIPEQYKTSVKGNKLHTESTSHI | Function: May have a regulatory bifunctional role. Binds G-actin and PIP2. Involved in microfilament reorganization near the plasma membrane in a PIP2-regulated manner.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49641
Sequence Length: 464
Domain: The C-terminus is responsible for sequestering G-actin. The N-terminus is required for the PIP2 modulation of cap function.
Subcellular Location: Cell membrane
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P40122 | MEQLVSRLEAVTNRLEAVASRGGGSTIKAAVDDDPAWFDDFKVFNAKFLSGFVNDTIALGGELEQMGKFVNEAFHCHLVLMEVAARHNRPSQTDLEGLLKPLSEAISKVQDFREKNRSSKQFNHLSAISEGLPFLGWVGVAPKPVLYIQQMEESAQFYTNKLLKEFRESDPKQANWATSFIQLLKGFAAYVKDHHQAGLMWNKEKSAATPAALAVSAHKPPVPPPPSGFAPPPPPPIQAPTVTHAVTGSHSSEDSRSQLFAQLSKGSEVTAGLKKVTDDMKTHKNPELRNQPPLKSSALDPRPYTPPNLKKFSAPVSKPAKKPALFQLQNKKWVIENQDGNTNLEISECNDKQTVYMYKCHASKVHINGKVNSIILDSCEKCVIEFTDVISTFEFTNCKACKVQIDGFAPTISIEKTDGAQVFINPKCLESQIVTAKSSEMNICVMKPDGDLTEYPLPEQFKTVWNPATSKFITTTMDLNL | Function: May have a regulatory bifunctional role.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53144
Sequence Length: 481
Subcellular Location: Cell membrane
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