ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q83P94 | MKRVLTALAATLPFAANAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTSADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFSEAMAVHPKGVDIMKPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPEYKDAAGHLIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVADLTLAGASAVSHDLYANVFKKGATEREELRVSKITVLILGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMLGGWLGLITAVVLMILGPTIWVQILGHEKAIFPYEYPALFSISVAFLGIWFFSATDNSAEGARERELFRAQFIRSQTGFGVEQGRAH | Function: Transports acetate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59163
Sequence Length: 549
Subcellular Location: Cell inner membrane
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P0DMX4 | SAALAGTIIAGASLGFQILDKVLGELGKVSRKIAVGVDNE | Function: Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and cytolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers (By similarity). This toxin shows hemolytic activities .
Sequence Mass (Da): 3983
Sequence Length: 40
Domain: Composed of a long N-terminal alpha-helix and a core region rich in beta-sheet structures. Before the pore formation, the alpha-helix binds the lipid membrane, partitions into the lipid-water interface and stabilizes the monomeric molecule on the membrane. Finally, it traverses the bilayer, thus forming the transmembrane pore.
Subcellular Location: Secreted
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P9WEZ9 | MHFRTVNTPARLQFISRFVLQPLRPLLHYKDHTIRTAAEAGLDVAELAVGPAFVVARGYFTLRQADTSSAESRDPTKQQQLWEKTLEWLGMTEEQGAL | Function: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of aculins . The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) acuA via condensation of acetate and malonate units . The 6-methylsalicylic acid decarboxylase acuB then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol) (Probable). These first reactions occur in the cytosol (By similarity). The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase acuC converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by the oxidoreductase acuE that probably catalyzes hydroxylation of the aromatic ring (Probable). The aromatic system might then be opened by oxidation through a Baeyer-Villiger type of oxidation, which could be catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is formed, before the dehydrogenase acuH would reduce the double bond between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results in formation of aculinic acid, which exists as two diastereomers (both R/S configurations at C-1) by non-enzymatic hemiacetal formation (Probable). The carboxypeptidase acuI could be involved in the linking of aculinic acid to an aculene A moiety produced by the aculene biosynthesis cluster and which leads to the production of aculin A (Probable). AcuI may also be involved in the attachment of proline to aculinic acid to form epi-aculins A and B (Probable).
Sequence Mass (Da): 11126
Sequence Length: 98
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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A0A1L9WN42 | MLLPSFPVTGVATALLLRNAVHASQPGSSVQKARAYDRFSSRPTRDHAPRVQSSNTSTYRFWNDKTKPHLVESLPDVHFDLGEMYSGSINITSHRNESRSLFYIFQPKIGEPSDDLTIYLNGGPGCSSEQAFFQENGRFTWQPGTYAPVINQYSWVNLTNMLWVDQPVGTGYSVGTPTATNEAEVAADFLEFFSKFQDLYGIKNFRIFVSGESYAGRYVPYISSAMLDKNDTTHFNLSGKPAHPLHHLAPTNAVCTGALLYDACIGQWDWVQAELPAYPFVQQHASLFNFNETFMTSLATTYEECGYQAYFDEYFTFPASGIQPPKYMNYSECDIYNAIYNEAFSPNPCFNPYRVIDECPLLWDVLGFPTDLAYEPAPTTYFNRADVKRALHAPQNIEWELCSTDPVLVGGDGVSGPEQVGDDSPNPTEGSLPRVIEATNRVLIANGDWDYLIITNGTLLAIQNMTWHGQLGFAAAPATPIDIRMPDLQWAGVFDAQEGYGDLDGPQGVMGVQHYERGLMWAETFQAGHKQAQDQGRVSYRHLQWLLGEVDSL | Function: Serine-type carboxypeptidase; part of the gene cluster that mediates the biosynthesis of aculins . The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) acuA via condensation of acetate and malonate units . The 6-methylsalicylic acid decarboxylase acuB then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol) (Probable). These first reactions occur in the cytosol (By similarity). The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase acuC converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by the oxidoreductase acuE that probably catalyzes hydroxylation of the aromatic ring (Probable). The aromatic system might then be opened by oxidation through a Baeyer-Villiger type of oxidation, which could be catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is formed, before the dehydrogenase acuH would reduce the double bond between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results in formation of aculinic acid, which exists as two diastereomers (both R/S configurations at C-1) by non-enzymatic hemiacetal formation (Probable). The carboxypeptidase acuI could be involved in the linking of aculinic acid to an aculene A moiety produced by the aculene biosynthesis cluster and which leads to the production of aculin A (Probable). AcuI may also be involved in the attachment of proline to aculinic acid to form epi-aculins A and B (Probable).
Sequence Mass (Da): 61789
Sequence Length: 553
Pathway: Secondary metabolite biosynthesis.
EC: 3.4.16.-
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Q3J6K9 | MRAVLIEKSDDTQSVSVTELAEDQLPEGDVLVDVAYSTLNYKDALAITGKAPVVRRFPMVPGIDFTGTVAQSSHADFKPGDRVILNGWGVGEKHWGGLAERARVRGDWLVPLPAPLDLRQAAMIGTAGYTAMLCVLALERHGVVPGNGEIVVSGAAGGVGSVATTLLAAKGYEVAAVTGRASEAEYLRGLGAASVIDRNELTGKVRPLGQERWAGGIDVAGSTVLANMLSMMKYRGVVAACGLAAGMDLPASVAPFILRGMTLAGVDSVMCPKTDRLAAWARLASDLDPAKLEEMTTELPFSEVIETAPKFLDGTVRGRIVIPVTP | Function: Catalyzes the NADPH-dependent reduction of acrylyl-CoA to propanoyl-CoA. Is essential for growth with 3-hydroxypropanoate as a sole carbon source. Restores acrylate resistance when expressed in the E.coli strain K12 acuI deletion.
Catalytic Activity: NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH
Sequence Mass (Da): 34165
Sequence Length: 326
Subcellular Location: Cytoplasm
EC: 1.3.1.84
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P26646 | MQALLLEQQDGKTLASVQTLDESRLPEGDVTVDVHWSSLNYKDALAITGKGKIIRNFPMIPGIDFAGTVRTSEDPRFHAGQEVLLTGWGVGENHWGGLAEQARVKGDWLVAMPQGLDARKAMIIGTAGFTAMLCVMALEDAGVRPQDGEIVVTGASGGVGSTAVALLHKLGYQVVAVSGRESTHEYLKSLGASRVLPRDEFAESRPLEKQVWAGAIDTVGDKVLAKVLAQMNYGGCVAACGLAGGFTLPTTVMPFILRNVRLQGVDSVMTPPERRAQAWQRLVADLPESFYTQAAKEISLSEAPNFAEAIINNQIQGRTLVKVN | Function: Probably catalyzes the NADPH-dependent reduction of acrylyl-CoA to propanoyl-CoA.
Catalytic Activity: NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH
Sequence Mass (Da): 34724
Sequence Length: 324
Subcellular Location: Cytoplasm
EC: 1.3.1.84
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Q5LS56 | MFNALVVDKDEESGKTQAAVKQLSLTDLPVGEVTVAVEYSTVNYKDGLCIGPGGGLVRKYPHVPGIDFAGTVENSSDERYKPGDKVVLTGWRVGEAHWGGYSQKANVRADWLVPLPEGLDTRQAMAVGTAGFTAMLAVMALEDHGLTPGHGPVLVTGAAGGVGSVATAILAHLGYEVAAVTGRPETADYLTSLGATQIVARDEINETVKRPLESEIWAGCVDAVGGAMLARVLGQMKYGASVAAVGLAGGAGLPATVIPFLLRGVNLLGIDSVMQPYANRLRAWERIARDLPMDKLEAMIRPATLSDLPGLGADILKGQVQGRVVVDVNA | Function: Probably catalyzes the NADPH-dependent reduction of acrylyl-CoA to propanoyl-CoA. Restores acrylate resistance when expressed in an E.coli strain K12 acuI deletion.
Catalytic Activity: NADP(+) + propanoyl-CoA = acryloyl-CoA + H(+) + NADPH
Sequence Mass (Da): 34450
Sequence Length: 330
Subcellular Location: Cytoplasm
EC: 1.3.1.84
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Q9R1V6 | MQAAAAASFWLLCVLGTCPLARCGRAGVASLKGLERGKENRFLERQSIIPLRLIYRLGGEDETQHNQLDTRVRGDPGGPQLTHVDKASFRVDAFGTSFVLDVLLNHELLSSGYVERQIEHGGKVVENKGGEHCYYQGQIRGNPVSFVALSTCHGLHGMFYDGNHTYLIEPEENEKSQESSHCHSVYKSRQFEFPLDDLPSEFQRVNITPPQFILKPRLKRRKRQLLRFPRNVEEETKYIELMIVNDHLMFKKHRLSVVYTNTYAKSVVNMADVIYKDQLKTRIVLVAMETWAADNKFAISENPLITLREFMKYRRDFIKEKADAVHLFSGSQFESSRSGAAYIGGICSLLRGGGVNEFGKTDLMAVTLAQSLAHNVGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPKKFTQCNVEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECALEGAECCKKCTLTQDSQCSDGLCCKKCKFQPLGTVCREAVNDCDIREICSGNSSQCAPNVHKMDGYSCDGTQGICFGGRCKTRDRQCKYIWGQKVTASDRYCYEKLNIEGTEKGNCGKDKDTWTQCNKRDVLCGYLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGAHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPVASFNFSTCSSSKAGTVCSGNGVCSNELKCVCNRHWTGADCGTHFPHNDDAKTGITLSGNGVAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNMGGNKKKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAGRQSARLWETSI | Function: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation (By similarity). Neuronal receptor for LGI1.
PTM: The precursor is cleaved by a furin endopeptidase.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99715
Sequence Length: 904
Subcellular Location: Cell membrane
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O75077 | MKPPGSSSRQPPLAGCSLAGASCGPQRGPAGSVPASAPARTPPCRLLLVLLLLPPLAASSRPRAWGAAAPSAPHWNETAEKNLGVLADEDNTLQQNSSSNISYSNAMQKEITLPSRLIYYINQDSESPYHVLDTKARHQQKHNKAVHLAQASFQIEAFGSKFILDLILNNGLLSSDYVEIHYENGKPQYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFEDDTFVYMIEPLELVHDEKSTGRPHIIQKTLAGQYSKQMKNLTMERGDQWPFLSELQWLKRRKRAVNPSRGIFEEMKYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEQLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQRIKQHADAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGLPMAVAQVLSQSLAQNLGIQWEPSSRKPKCDCTESWGGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRPTKLFEPTECGNGYVEAGEECDCGFHVECYGLCCKKCSLSNGAHCSDGPCCNNTSCLFQPRGYECRDAVNECDITEYCTGDSGQCPPNLHKQDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLTRAPRIGQLQGEIIPTSFYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCLQIQALNMSSCPLDSKGKVCSGHGVCSNEATCICDFTWAGTDCSIRDPVRNLHPPKDEGPKGPSATNLIIGSIAGAILVAAIVLGGTGWGFKNVKKRRFDPTQQGPI | Function: May play a role in cell-cell and cell-matrix interactions. This is a non-catalytic metalloprotease-like protein.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 91926
Sequence Length: 832
Domain: A conserved motif AVN[ED]CD within the disintegrin-like domain could be involved in the binding to the integrin receptor.
Subcellular Location: Cell membrane
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Q9R160 | MVAMSEALVHARITLLQAWLRMLLFSSVWPPTWCAEYKGPPETVKPLRVIVSSKDMSLAGWMSYSLYFGGQRHIISMKSKNFLESRQLPVFTYNDQGVLFEDRPFVQNDCYYLGFVDGDLESMAALTTCFGGFQGILQINDTAYEIKPKSPSSTFEHLLYKIDSEKTQLRPMRCGLTDEEIAGQVRLQENGKSTRMQSIYGSWWSHGLYIKLALVIDHEQYLYRKKNTSLVIRDVLSIMQGINLFLLSVDINVVLLGLTIWTNGNPIPVQDIYALLPAFCTWKGTNLDSQIPYDIAHLFVNYTFSNYFGIAYVGTVCDKTFGCGIDSIAEDDFLTIGHIVAHEIGHNLGMSHDGILCTCGEESCLMSATMDSSQKLSNCSYEVLWAHMINKSCIHREPRPSDIFQLKVCGNGIVEEGEQCDCGSSENCRRNRCCMPSCTLRSKAKCDTGLCCNRKCQIQPSGTLCRARENECDLPEWCNGTSHECPEDLFVQDGTSCPGDGYCYEKRCNSHDVHCQRVFGQLAMKASDSCYKELNTRGDRFGNCGFINNEYVRCEISDILCGRIQCDKVGTLPILQNHYTIHWTHFNSVSCWSTDYHLGMKIADLGDIKDGTNCGPQHVCIARKCVNKPSWVNDCTPETCNMKGVCNNKQHCHCDVGWSPPNCQETGTGGSIDSGSPGNEVYEDEVVSKKDAPEKPNVIIWLLPIICVAVVLSVLFCLSGATKKSREAAASQPAEERVKPPYEGAEPSYETVKPPDEWANP | Cofactor: Binds 1 zinc ion per subunit.
Function: Plasma membrane protease present on mature sperm that may be involved in sperm function during epididymal maturation and/or fertilization.
PTM: The prodomain is removed during sperm passage through the caput epididymis after the protein has reached the cell surface. Not processed in the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85054
Sequence Length: 761
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Membrane
EC: 3.4.24.-
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Q9R159 | MQTTQRASSFAAAEDNIAMDKAVVYTRIPHLYLWLEILNILSSRPLTGYAQHTSLPEVVIPLRVTGNRPMWAMGWLTYSLHFGGQKHFIHIKAKKFLVSRLFSVFTYTKQGALHKDQPYVQNDCYYHGHMDGDPESMVAITTCYGGFQGILQINGTVYEIKPKNLSSTFEHLVHKMDSEETELLPMRCALTEEIARQMKLQQNENPTLMQSHYEGWWTHKSFLDLALVVERERIRYHNNNTSRVLVEVFTIINIINNIYETLDVELVLLGVEMWNERNHVQVRSIEELLDEFCMWKARSLNFRIPNDIAHIFVNHEFGIYLGLAYIGSVCVPSHNCGVDRLLGGNLFYFGRIIAHEMGHNLGMEHDSSSCTCGTKICLMAPADNGIPKFSNCSYSYYWATYATAKCMRKEKKSKGILRGKLCGDGVVDDGEQCDCGSAKSCADDPCCKPSCTLKDGAACAFGLCCLYCQIMPAGTVCRQEVNECDLPEWCNGHSHKCPNDVYLLDGSPCRDGGYCYEKRCNNRDEQCKQIFGKEARSADHSCYRELNTQGDRFGNCGVIRDAYLRCHDPDILCGRVQCENVAHIPFLRDHSTVHWTHLNGVTCWGTDYHFGMTIPDIGIVKDGTDCGPEHVCINKKCVSKSIWRSQCSPKTCNMKGVCNNLHHCHCNLGWDPPHCLKSGLGGSIDSGPPNYTENYTEKKHKKSIGLVILFWILFACFSVLFIVFLFFLRSYVELPMSEEPKVPTPENKEDTNEVMNTETE | Cofactor: Binds 1 zinc ion per subunit.
Function: Sperm surface membrane protein that may be involved in spermatogenesis and fertilization.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 86128
Sequence Length: 760
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Membrane
EC: 3.4.24.-
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Q9UKQ2 | MLQGLLPVSLLLSVAVSAIKELPGVKKYEVVYPIRLHPLHKREAKEPEQQEQFETELKYKMTINGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYYQGHILNEKVSDASISTCRGLRGYFSQGDQRYFIEPLSPIHRDGQEHALFKYNPDEKNYDSTCGMDGVLWAHDLQQNIALPATKLVKLKDRKVQEHEKYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATELAGTTVGLAFMSTMCSPYSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTICVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAPLPTDIISTPICGNQLVEMGEDCDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDDRFQVNGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNRNEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSDNLPWKGRIVTFLTCKTFDPEDTSQEIGMVANGTKCGDNKVCINAECVDIEKAYKSTNCSSKCKGHAVCDHELQCQCEEGWIPPDCDDSSVVFHFSIVVGVLFPMAVIFVVVAMVIRHQSSREKQKKDQRPLSTTGTRPHKQKRKPQMVKAVQPQEMSQMKPHVYDLPVEGNEPPASFHKDTNALPPTVFKDNPVSTPKDSNPKA | Cofactor: Binds 1 zinc ion per subunit.
Function: May play a role in the adhesive and proteolytic events that occur during lymphocyte emigration or may function in ectodomain shedding of lymphocyte surface target proteins, such as FASL and CD40L. May be involved in sperm maturation.
PTM: Pro-domain removal and maturation may be, at least in part, autocatalytic.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 87148
Sequence Length: 775
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q9UKF5 | MKMLLLLHCLGVFLSCSGHIQDEHPQYHSPPDVVIPVRITGTTRGMTPPGWLSYILPFGGQKHIIHIKVKKLLFSKHLPVFTYTDQGAILEDQPFVQNNCYYHGYVEGDPESLVSLSTCFGGFQGILQINDFAYEIKPLAFSTTFEHLVYKMDSEEKQFSTMRSGFMQNEITCRMEFEEIDNSTQKQSSYVGWWIHFRIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLIVVDDVRKSVHLYCKWKSENITPRMQHDTSHLFTTLGLRGLSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDTCRCSQPRCIMHEGNPPITKFSNCSYGDFWEYTVERTKCLLETVHTKDIFNVKRCGNGVVEEGEECDCGPLKHCAKDPCCLSNCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDDFYVEDGIPCKERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTEIPNMSDHTTVHWARFNDIMCWSTDYHLGMKGPDIGEVKDGTECGIDHICIHRHCVHITILNSNCSPAFCNKRGICNNKHHCHCNYLWDPPNCLIKGYGGSVDSGPPPKRKKKKKFCYLCILLLIVLFILLCCLYRLCKKSKPIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPPVTPS | Function: May be involved in spermatogenesis and fertilization. Seems to be a non catalytic metalloprotease-like protein.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 92759
Sequence Length: 820
Subcellular Location: Membrane
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Q811Q4 | MNMIEALLSMRVLFLTQVFGIFLCFPGLTKAGHLHYHSSIEVVIPMKVTEKTRGMNLPNWISYSLKLGGQRYIIHMKIKNLFLTRHLPVFTYSDQDSLLEDYPFVQDDCYYQGYVEGDSESLVSLSSCFGGFHGLLEINNIVYEIMPKKFSRKFEHLVYKVDINKTESRGSSLMQDNITCQVELQKSGNPILKQSSFEDWWTHTKIVELVVVVDKTLYDHYGNYTVMLSDLYSVINIVDTIYEVIGIKILLVGVEVWNKKNLIVIDDVSKSLRLYCRWKASNFLHRLKHDVSHLFIYRHLRGLSGIGSTGGICDPKRSCAVVTFIDRTLNLRAIGVAHHLGHNLGMKHDEDICKCSYSKCIMHMDSPPIPKFSNCSYNYFWSYTVKNTRCLMENMYTKDIFDRTRCGNGVVEDKEQCDCGSLRNCTNDLCCMSNCTLSTGSSCAFGLCCKNCQFLPSGTLCRKRDNICDLPEWCNGTSHECPDDAYVEDGIPCGVSAYCYEKQCNDRNEHCRQIFGQNAKTASVHCYREINTKGDRFGHCGLQGPTYIKCKSNDALCGRIQCDNVVQIPNMKDHSTIHFALVKNVSCWGTDYHTGTSLTDIGDVKDGTECEQNHICINRHCVHISTLDSNCTPAFCNYRGICNNKHHCHCNFHWDPPNCMIRGHGGSVDSGLPPKTNKKKHFFYLLLLQLIILACLLSCLLWLLFNIKGSKRKPQVQPTPVKTKKVSKKVPSQKPSPVPSPSLPQLRMPSRSASPTSSIKSTN | Function: May be involved in spermatogenesis and fertilization. Seems to be a non catalytic metalloprotease-like protein (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 86445
Sequence Length: 763
Subcellular Location: Membrane
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Q90WY4 | MICGANATNGTNATKEYTLLVALPLSIAVGLLILLIIFGNVLVIIAVFTSRALRAPQNLFLVSLASADILVATLVMPFSLANELMGMWTFGGVWCEIYLALDVLFCTASITHLCAISLDRYWSITQAIEYNLKRTPQRIKRIIFIVWIIAAVISCPPLITMKKSEGDICDINKEKWYIVSSCIGSFFLPCIIMVLVYIRIYQIAKKRTRAPPGDHRKNEVGKKENDPHEKLNGIQNAEPDDKDEINGVDMEESSSSDHKVSNPCSLKKKSSKGKTKLSQIKPGDGDKTEACQTTKASRWKGRQNREKRFTFVLAVVIGVFVICWFPFFFTYTFTAFCDCCVPETLFKFFFWFGYCNSSLNPIIYTIFNNDFRRSFKKILCRRDKRRVV | Function: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. The order of potency for this receptor is dexmedetomidine > oxymetazoline = epinephrine > norepinephrine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43997
Sequence Length: 388
Subcellular Location: Cell membrane
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P08913 | MFRQEQPLAEGSFAPMGSLQPDAGNASWNGTEAPGGGARATPYSLQVTLTLVCLAGLLMLLTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIITVWVISAVISFPPLISIEKKGGGGGPQPAEPRCEINDQKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDAVAAPPGGTERRPNGLGPERSAGPGGAEAEPLPTQLNGAPGEPAPAGPRDTDALDLEESSSSDHAERPPGPRRPERGPRGKGKARASQVKPGDSLPRRGPGATGIGTPAAGPGEERVGAAKASRWRGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLTAVGCSVPRTLFKFFFWFGYCNSSLNPVIYTIFNHDFRRAFKKILCRGDRKRIV | Function: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. The rank order of potency for agonists of this receptor is oxymetazoline > clonidine > epinephrine > norepinephrine > phenylephrine > dopamine > p-synephrine > p-tyramine > serotonin = p-octopamine. For antagonists, the rank order is yohimbine > phentolamine = mianserine > chlorpromazine = spiperone = prazosin > propanolol > alprenolol = pindolol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50647
Sequence Length: 465
Subcellular Location: Cell membrane
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P35612 | MSEETVPEAASPPPPQGQPYFDRFSEDDPEYMRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPTSSMNVSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFCLHSAIYAARPDVRCIIHLHTPATAAVSAMKWGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGVVALGDTVEEAFYKIFHLQAACEIQVSALSSAGGVENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGAPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRSMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLEMRNKIREQNRQDVKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDEDTKDDSEETVPNPFSQLTDQELEEYKKEVERKKLELDGEKETAPEEPGSPAKSAPASPVQSPAKEAETKSPLVSPSKSLEEGTKKTETSKAATTEPETTQPEGVVVNGREEEQTAEEILSKGLSQMTTSADTDVDTSKDKTESVTSGPMSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES | Function: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to the erythrocyte membrane receptor SLC2A1/GLUT1 and may therefore provide a link between the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit.
PTM: The N-terminus is blocked.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80854
Sequence Length: 726
Domain: Each subunit is comprised of three regions: a NH2-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region.
Subcellular Location: Cytoplasm
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Q8ZPL9 | MIDITLPLTDIHRHLDGNIRAQTILDLGRQFNIALPAQTLETLIPHVQVTSTEPDLVSFLTKLDWGVKVLASLDACRRVAFENIEDAARNGLHYVELRFSPGYMAMAHQLPIAGVVEAVIDGVRDGCNTFGVEARLIGIMSRTFGEAACLQELDALLAHRENITALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAQQRIGIESCLTSNIQTSTVASLADHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYHVAAPAAGLSREQIRQAQINGLEIAFLSDSEKRALREKVAEA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
Catalytic Activity: adenosine + H(+) + H2O = inosine + NH4(+)
Sequence Mass (Da): 36236
Sequence Length: 333
EC: 3.5.4.4
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Q8E8D4 | MINTSIPLVDLHRHLDGNVRVNTIWELGHQHGIALPADSLETLAPFVQIQGKETSLVAFLKKLDWMVAVLADLDAVKRIAYENVADAALSGLDYAELRFSPYYMAMNHKLPIEGVVEAVIDGVKAGLKDYQVNINLIGIMSRSFGQPACTQELEGLLAHKQHLVAMDLAGDELGFPGELFNEHFKRVRDAGLAITAHAGEAAGSQSMWQAIQELGATRIGHGVNAIHDPKLMEYLAKHRIGIESCPTSNLHTSTVSSYAEHPFRTFMDAGVLIGLNTDDPGVSAIDIKHEYRIAKFELGLSDAELAQVQRNGVEMAFLSESERKALYAAKA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
Catalytic Activity: adenosine + H(+) + H2O = inosine + NH4(+)
Sequence Mass (Da): 36175
Sequence Length: 331
EC: 3.5.4.4
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A8H819 | MNYLQLPKIDLHCHLDGSVRPQTVIDLAKLQDVTIPSFNVDDIKALMVAPASCPNLDEYLTRFALPVSVMQTEAALERISFELFEDAAKENVKYLEVRFGPQLHQKMSLNFEQIIGSVVKGMRRAEAQYDIKGNYILSIIKVLPKDDINDVIDAGAKFLNNGVVAFDLAASEEPGFCHEYIPYAKYALEKGYRITIHAGEQGVGQNVYDAISLLGAERIGHGIHINSHQQAYELVKTEAVALETCPSSNVQTKAVESIESHPFGDFYRDGLLVTINTDNRTVSDTTMTKELQLAAEKFNLTEADYFAIYKMSVDNAFTSDEVKLSLLKFID | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
Catalytic Activity: adenosine + H(+) + H2O = inosine + NH4(+)
Sequence Mass (Da): 36921
Sequence Length: 331
EC: 3.5.4.4
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B9KE87 | MKTFLQNIPKVELHLHIEGSLEPKMMFELAKRNNITLKYKSEDEIKKAYDFSNLQDFLDIYYQGANVLQTKQDFYDLTFAYMKKCKEQNVVHTEIFFDPQTHTARNIPLKDVIEGIWQALQKAKEEFGISSFLIACILRHLSEEEGLKTLDELCLYKDKIKAIGLDSSELNNPPFKFKNLFQKAKEEGFLLVMHAGEEGSSEYIKQALELGVNRIDHGVRCQEDLELVKQLAKSQIPLTICPLSNIKLKVFQNMQEHNILKLLKQNLCVCVNSDDPAYFGGYILENFIALDETFKLSKDEVKKLCINAVNASFLNINEKEKLVKQIKAYK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Catalytic Activity: adenine + H(+) + H2O = hypoxanthine + NH4(+)
Sequence Mass (Da): 38098
Sequence Length: 330
EC: 3.5.4.2
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Q59ZB1 | MAQYECSEHMENFLRELPKCEHHVHLEGTLEPSLLFKLAKRNNITLPETFPKTVEECNDRYNRFADLQDFLDHYYIGMGVLITENDFYDLAMDYFTKAHSDGCLHSEVFFDPQGHVERNIDIDVVVQGFNRACKDANTKYGTTNKLIMCLLRHLPAENGLQTIHSASKYYQDGIIHGLGLDSSEKPFPPNLFTECYAHIKDNFPEVGLTAHAGEEGDHTFVSDALNLLKVSRIDHGVNSHQSEELMQRLAEQKTLLSLCPLSNVKLQVVKDVKELPIDKFFQMNVPFSINSDDPAYFGGYILDNYKAVHTRFGFTKDQWKIIALNGIKGSWCDDQRKNELISLVEEVYKKYNIEGC | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Catalytic Activity: adenine + H(+) + H2O = hypoxanthine + NH4(+)
Sequence Mass (Da): 40782
Sequence Length: 356
Subcellular Location: Cytoplasm
EC: 3.5.4.2
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Q9A3M3 | MTDASFAPSASAEFVRGLPKAELHMHIEGSLEPELMFELAQRNGITLPFASVEEIRAAYDFSNLQDFLDIYYQGAGVLITEADFKDLALAYFQRLAADGGAHAEIFFDPQTHTDRGIAFDTVMNGLLAGMDEAEKTLGVTSKLILCFLRHLSEEAAFETLEQAKPWLAKLAGVGLDSSEVGHPPAKFARVLQASRDLGLKVVAHAGEEGPPAYVWEAIDLVKVDRIDHGNRALEDEALTARLVKDGITLTVCPLSNLKLCGVPSLDVHPLKRMLDLGLKATVNSDDPAYFGGYLLENYLATADAVGLTRDDIVTLAKNSFAGSFLTDAEKAQRIAAVEAYAAAH | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Catalytic Activity: adenine + H(+) + H2O = hypoxanthine + NH4(+)
Sequence Mass (Da): 37193
Sequence Length: 344
EC: 3.5.4.2
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B3R3T1 | MTIDAALAEQIRRTPKAELHVHIEGTLEPELIFRLAQRNQVALPYPSVDALRAAYAFTDLQSFLDIYYAGASVLLTEEDFFDMTMDYVKRAVADNVRHAEIFFDPQTHTARGVPIGVVIDGIADALAQARTEYDFSSSLILCFLRHLSEEDAFATLEAALPYRDRFVGVGLDSSEKGNPPEKFARVFARARELGLHLVAHAGEEGPAQYVADALDILKAERIDHGVRAIDDAALVERLARERVALTVCPLSNVKLKVYPDLRDHPLKRMLDAGVAITLHSDDPAYFGGYMNANWEATFDALPLDAADAHKLARNSFEAAFLPAMQKAEFLAEVDHFWSAPPKSPPATAPAA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Catalytic Activity: adenine + H(+) + H2O = hypoxanthine + NH4(+)
Sequence Mass (Da): 38700
Sequence Length: 351
EC: 3.5.4.2
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Q4IMJ1 | MCKSRVHSFLQALPKVEQHLHIEGTLEPELLFTLAEKNGIELPNDPVYESADKLRERYGRFTSLDDFLHYYYLGMSVLITENDFETLAYQYFQRAAGENVRHAEIFFDPQAHIARGVSYDTVVAGLVAAKHRAQKELGITVELIVCILRHLPVPESHALVDTLLDRGHFNDGTLTGFGMVSSEKAFPPELFTDVYARVAKTGTHLTTHAGEEAPPSFITASLEHLKVSRIDHGLAAAQDPELLKKLAANRTLLTFCPWSNVALCNLPELADAPVREFLDAGVLFSVNSDDPAYFGAYVQEVYCRVQDTFNLSVKDWAWIVRGAVEESWCSEERKKEILKEMEQVLEKYKDLDA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Catalytic Activity: adenine + H(+) + H2O = hypoxanthine + NH4(+)
Sequence Mass (Da): 39774
Sequence Length: 353
Subcellular Location: Cytoplasm
EC: 3.5.4.2
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P07754 | MSVPEVQWAQVVEKAGTPPVYKQVPVPKPGPDEILVKMRYSGVCHTDLHAMKGDWPLPSKMPLIGGHEGAGVVVAKGELVKDEDFKIGDRAGIKWLNGSCLSCEMCMQADEPLCPHASLSGYTVDGTFQQYTIGKAALASKIPDNVPLDAAAPILCAGITVYKGLKESGARPGQTVAIVGAGGGLGSLAQQYAKAMGLRTIAIDSGDEKKAMCEQLGAEVFIDFSKSADVVADVKAATPGGLGAHAVILLAVAEKPFQQATEYVRSHGSVVAIGLPANAFLKAPVFTTVVRMINIKGSYVGNRQDGVEALDFFARGLIKAPFKKAPLQDLPQIFELMGQGKIAGRYVLEIPE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 37126
Sequence Length: 352
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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Q24857 | MTMLNFTYYNPVRLIYGKGSLDEIEKQHLIPEDARIMMTYGGGSIKKNGVYEEVLKHIKPIVEFGGIEPNPSHETCIKAIKIAKENKINFLVAVGGGSIIDATKYIALGMEHTYSDDPYDICLKGGKFKVNPAQAKIGVVLTIPATGSETNCWGVISRHADKLKLPFNNESVFPTWSIVDPCFTMSLPDNQIRNGLVDSFVHCIEQYIGNYHLNPVVEAETEGVMRTIIGVSHKTLENHQDYQARITFCYAATVALNMSLLCGVTLCGGAHAVGHELTSYYGLAHGETLAITTPGVMRFNKEKNAKKLIQMGEQVFGIKNSTPEAAIEATEKWFKSIGMKTRLSEWGKGKEEFETIARKFEGNPAGAHKDIDYKGCLQILNDIY | Function: Has NADP-dependent alcohol dehydrogenase activity.
Catalytic Activity: a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH
Sequence Mass (Da): 42519
Sequence Length: 384
EC: 1.1.1.2
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P10848 | MATAGKVIKCKAAVAWEAGKPLSIEEVEVAPPQAMEVRVKILYTALCHTDVYFWEAKGQTPVFPRILGHEAGGIVESVGEGVTELVPGDHVLPVFTGECKDCAHCKSEESNLCDLLRINVDRGVMIGDGQSRFTINGKPIFHFVGTSTFSEYTVIHVGCLAKINPEAPLDKVCVLSCGLSTGLGATLNVAKPKKGSTVAIFGLGAVGLAAMEGARMAGASRIIGVDLNPAKYEQAKKFGCTDFVNPKDHTKPVQEVLVEMTNGGVDRAVECTGHIDAMIATFECVHDGWGVAVLVGVPHKEAVFKTHPMNFLNEKTLKGTFFGNYKPRTDLPEVVEMYMRKELDLEKFITHSVPFSQINTAFDLMLKGEGLRCITRTDQ | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 41011
Sequence Length: 379
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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P07246 | MLRTSTLFTRRVQPSLFSRNILRLQSTAAIPKTQKGVIFYENKGKLHYKDIPVPEPKPNEILINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVKLGSNVKGWKVGDLAGIKWLNGSCMTCEFCESGHESNCPDADLSGYTHDGSFQQFATADAIQAAKIQQGTDLAEVAPILCAGVTVYKALKEADLKAGDWVAISGAAGGLGSLAVQYATAMGYRVLGIDAGEEKEKLFKKLGGEVFIDFTKTKNMVSDIQEATKGGPHGVINVSVSEAAISLSTEYVRPCGTVVLVGLPANAYVKSEVFSHVVKSINIKGSYVGNRADTREALDFFSRGLIKSPIKIVGLSELPKVYDLMEKGKILGRYVVDTSK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 40370
Sequence Length: 375
Subcellular Location: Mitochondrion matrix
EC: 1.1.1.1
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P08319 | MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTDATVIDSKFEGLAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCRKCKFCLSPLTNLCGKISNLKSPASDQQLMEDKTSRFTCKGKPVYHFFGTSTFSQYTVVSDINLAKIDDDANLERVCLLGCGFSTGYGAAINNAKVTPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKALGATDCLNPRDLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGVAAGSKGLTIFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDALVTHTLPFDKISEAFDLMNQGKSVRTILIF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol . Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate . Also catalyzes the reduction of benzoquinones .
Catalytic Activity: all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH
Sequence Mass (Da): 40222
Sequence Length: 380
Subcellular Location: Cytoplasm
EC: 1.1.1.105
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Q9QYY9 | MGTQGKVIKCKAAIAWKTGSPLCIEEIEVSPPKACEVRIQVIATCVCPTDINATDPKKKALFPVVLGHECAGIVESVGPGVTNFKPGDKVIPFFAPQCKRCKLCLSPLTNLCGKLRNFKYPTIDQELMEDRTSRFTCKGRSIYHFMGVSSFSQYTVVSEANLARVDDEANLERVCLIGCGFSSGYGAAINTAKVTPSSTCAVFGLGCVGLSAIIGCKIAGASRIIAIDINGEKFPKAKALGATDCLNPRELDKPVQDVITELTAGGVDYSLDCAGTAQTLKAAVDCTVLGWGSCTVVGAKVDKMTIPTVDVILGRSINGTFFGGWKSVDSVPNLVSDYKNKKFDLDLLVTHALPFESINDAIDLMKEGKSIRTILTF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol . Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate . Also catalyzes the reduction of benzoquinones (By similarity).
Catalytic Activity: all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH
Sequence Mass (Da): 40211
Sequence Length: 377
Subcellular Location: Cytoplasm
EC: 1.1.1.105
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P80468 | TTEGKVIKCKAAIAWEAGKPLSVEEIEVSPPKDHEVRVKIVATGVCRTDEHAINPSFKEGVFPVILGHEGAGIVESIGQGVSKFKPGDKVIPLYMPQCGHCKFCLNPKTNLCEKISKIKTPISDQEVMSDGTSRFTCKGKPIYHFMGTSTFSEYTVVSESSLAKIDAAAPLDKVCLIGCGFSTGYGAAINTAQVEPGSTCAVFGLGGVGLSAVMGCKAAGASKIFGIDINKDKFPLAKKLGATDCLNPQDIRKPVQEIIAEMTNGGVDFAIECIGNPDVMKAAFESTTVGWGTCVIVGVAVGEQSIPFSPMQLIMGRKIKATFFGGWKSVKSVPKLVSDYMAKKFDLDALVSHTLPLDKINDAFDLMNAGKSNRTILVF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol (By similarity). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (By similarity). Also catalyzes the reduction of benzoquinones (By similarity).
Catalytic Activity: all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH
Sequence Mass (Da): 40310
Sequence Length: 379
Subcellular Location: Cytoplasm
EC: 1.1.1.105
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P10127 | MSSVTGFYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKKRLGEIALHFGASQEDPEETIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKAYEY | Cofactor: Zinc. May bind iron when zinc levels are limiting.
Function: Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 41142
Sequence Length: 382
Subcellular Location: Mitochondrion
EC: 1.1.1.1
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P28332 | MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSKTQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKW | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 39073
Sequence Length: 368
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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Q9SF85 | MASSDFDGILLGMGNPLLDVSAVVDQQFLDKYDIKLNNAILAEDKHLPMYDEMSQKFNVEYIAGGATQNSIKVAQWMLQVPGATSYMGSIGKDKYGEAMKKDATAAGVYVHYYEDEATPTGTCGVCVLGGERSLIANLSAANCYKVEHLKKPENWALVEKAKFYYIAGFFLTVSPESIQLVREHAAANNKVFTMNLSAPFICEFFKDVQEKCLPYMDYIFGNETEARTFSRVHGWETDDVEQIAIKMSQLPKASGTYKRTTVITQGADPVVVAEDGKVKKYPVIPLPKEKLVDTNGAGDAFVGGFLSQLVHGKGIEECVRAGCYASNVVIQRSGCTYPEKPDFN | Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives . Essential to sustain methyl recycling .
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 37836
Sequence Length: 344
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
EC: 2.7.1.20
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Q9LZG0 | MASSSNYDGILLGMGNPLLDISAVVDDEFLTKYDIKLNNAILAEDKHLPMYDEMSSKFNVEYIAGGATQNSIKVAQWMLQIPGATSYMGSIGKDKYGEAMKKDATAAGVNVHYYEDESAPTGTCGVCVVGGERSLIANLSAANCYKVDHLKKPENWALVEKAKFYYIAGFFLTVSPESIQLVSEHAAANNKVFTMNLSAPFICEFFKDVQEKFLPYMDFVFGNETEARTFSRVHGWETEDVEQIAIKISQLPKATGTYKRTTVITQGADPVVVAEDGKVKKYPVIPLPKEKLVDTNGAGDAFVGGFMSQLVKEKSIEECVKAGCYASNVVIQRSGCTYPEKPDFN | Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives . Essential to sustain methyl recycling .
PTM: Phosphorylated by KIN11.
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 37846
Sequence Length: 345
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.1.20
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Q54MB5 | MSNIKILCAGNPLLDLSTHVEMAILDKYELKLGNAILAEDKHLPLYGEIKSGKVEYIPGGAAQNTSRVCQWMLKDKQTVCYTGCVGTDENATILKTATESNGVVTKYQVDSSAPTGACAVLINHKERSMVTNLGAANNFKIAHFQTEEMKAIVNSAQFFYLVGYFLTVSPDSAVHLGKHAAENDKPFLYGLAAPFLIDFFFDKVSELLPYVDIVFANESEAATLGRKMNWGEDLTVIAEKLAAWEKVNTKRTRTVVFTQGPDATLVFQNGVLTKYNPIKVATEDILDLNAAGDSFCGGFLAAYSNGQEIAKCVEAGHYASWEIIRQNGATVPASEPKIQF | Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 37095
Sequence Length: 340
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
EC: 2.7.1.20
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P55263 | MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPDFH | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the phosphorylation of the purine nucleoside adenosine at the 5' position in an ATP-dependent manner. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 40545
Sequence Length: 362
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Subcellular Location: Nucleus
EC: 2.7.1.20
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O49923 | MASEGVLLGMGNPLLDISCVVDDAFLEKYGLTLNNAILAEDKHLPMYKELAANPDVEYIAGGATQNTIRIAQWMLGESNATSYFGCVGKDEYGDRMFKLASEGGVNIRYDVDEDLPTGTCGVLVVKGERSLVANLSAANKYKIDHLKKPENWAFVEKAKYIYSAGFFLTVSPESMMTVAKHAAETGKYYMINLAAPFICQFFKDPLMELFPYVDFIFGNESEARAFAQVQGWETEDTKVIAVKLAALPKAGGTHKRVAVITQGTDPTIVAEDGKVTEFPVTPIPKEKLVDTNAAGDSFVGGFLSQLVLGKDIAQCVRAGNYAASVIIQRSGCTFPSKPSFESQ | Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Can also act on the cytokinin isopentenyladenosine to produce isopentenyladenosine monophosphate.
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 37251
Sequence Length: 343
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
EC: 2.7.1.20
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O93919 | MSSYKLFCMGNPLLDLQVRDGEKLLEKYGLKSNDAILAEEKHLLLYDEIVKEHEVTYVAGGAAQNAARGAAYCLPPKSVVYTGCVGDDDLAEQLKAANKREGLDEAYLVKKGEKTGACAVIITGHDRSLVTTLRAAEKFEQSHLSSEAVAPLVDAVQFYYMEGYFVTHGLASALELAGKSAAKSKCFVLNFSAPFIPQFFMPAIQQLLPYVDIVIANESEAEAWASASGHPAPTDLAAVAKSLAMQPKTNPARPRVVIFTHGAEETVVVNSAEPGRVRTFKVDKLAEGEIVDTNGAGDAFAGGFLGALVAGRELDDSVEAGHKLAKISIQQIGPQFKWPKVQIL | Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 36940
Sequence Length: 344
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
EC: 2.7.1.20
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P78825 | MSSYILFGLENPLLDYYVGGETATLEKYGLKSNDAVLASESQMGIYKEPCVSYSAGGAAQNSCRAAQYVLPPNSTVFAGCVGQDKFADMLLESNEKAGLRSEFSVDPTTPTGVCAVVLSNNNKNRSLCTNLGAANNYKLKDLQQPNVWKFVEEAKVIYVGGFHLTVSPESMLCLAQHANENNKPYIMNLSAPFLSQFFKEQMDSVIPYCDYVIGNEAEILSYGENHGIKSTDVQEIALALSSVEKVNKKRTRVVVITQGADATIVAKDGKVTTYKPNRVPSEEIVDTNGAGDAFAGGFIAALSQGQGIDYAVTLGHWLGQECIKVSGTTLPLPKKQFPLP | Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 36709
Sequence Length: 340
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
EC: 2.7.1.20
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Q9TVW2 | MAVDSSNSATGPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLDQFNPTSLPGGSALNSVRVVQKLLRKPGSAGYMGAIGDDPRGQVLKELCDKEGLATRFMVAPGQSTGVCAVLINEKERTLCTHLGACGSFRLPEDWTTFASGALIFYATAYTLTATPKNALEVAGYAHGIPNAIFTLNLSAPFCVELYKDAMQSLLLHTNILFGNEEEFAHLAKVHNLVAAEKTALSTANKEHAVEVCTGALRLLTAGQNTGATKLVVMTRGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAGDAFVGGFLYALSQGKTVKQCIMCGNACAQDVIQHVGFSLSFTSLPC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: ATP-dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. It is a key purine metabolic enzyme in the opportunistic parasitic protozoan toxoplasma gondii as it cannot synthesize purines de novo.
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 38356
Sequence Length: 363
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
EC: 2.7.1.20
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P47143 | MTAPLVVLGNPLLDFQADVTAEYLAKYSLKENDAILVDAKSGDAKMAIFDELLQMPETKLVAGGAAQNTARGAAYVLGAGQVVYFGSVGKDKFSERLLNENEKAGVKSMYQVQNDIGTGKCAALITGHNRSLVTDLGAANFFTPDHLDKHWDLVEAAKLFYIGGFHLTVSPDAIVKLGQHAKENSKPFVLNFSAPFIPHVFKDALARVLPYATVIIANESEAEAFCDAFQLDCANTDLEAIAQRIVKDSPVEKTVIFTHGVEPTVVVSSKGTSTYPVKPLDSSKIVDTNGAGDAFAGGFMAGLTKGEDLETSIDMGQWLAALSIQEVGPSYPSEKISYSK | Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. ADO1 does not play a major role in adenine utilization in yeast. Its physiological role could primarily be to recycle adenosine produced by the methyl cycle.
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Mass (Da): 36372
Sequence Length: 340
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
EC: 2.7.1.20
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Q60813 | MSVAAAGRGFASSLSSPQIRRIALKEAKLTPHIWAALHWNLGLRLVPSVRVGILVLLIFLPSTFCDIGSVYNSSYETVIPERLPGKGGKDPGGKVSYMLLMQGQKQLLHLEVKGHYPENNFPVYSYHNGILRQEMPLLSQDCHYEGYMEGVPGSFVSVNICSGLRGVLIKEETSYGIEPMLSSKNFEHVLYTMEHQPVVSCSVTPKDSPGDTSHPPRSRKPDDLLVLTDWWSHTKYVEMFVVVNHQRFQMWGSNINETVQAVMDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQTTLRNFNFWRQEKLVGRVRHDVAHLIVGHRPGENEGQAFLRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHDHPTCTCGPKHFCLMGEKIGKDSGFSNCSSDHFLRFLHDHRGACLLDEPGRQSRMRRAANCGNGVVEDLEECDCGSDCDSHPCCSPTCTLKEGAQCSEGLCCYNCTFKKKGSLCRPAEDVCDLPEYCDGSTQECPANSYMQDGTQCDRIYYCLGGWCKNPDKQCSRIYGYPARSAPEECYISVNTKANRFGNCGHPTSANFRYETCSDEDVFCGKLVCTDVRYLPKVKPLHSLLQVPYGEDWCWSMDAYNITDVPDDGDVQSGTFCAPNKVCMEYICTGRGVLQYNCEPQEMCHGNGVCNNFKHCHCDAGFAPPDCSSPGNGGSVDSGPVGKPADRHLSLSFLAEESPDDKMEDEEVNLKVMVLVVPIFLVVLLCCLMLIAYLWSEVQEVVSPPSSSESSSSSSWSDSDSQ | Function: May be involved in sperm-egg fusion.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 87490
Sequence Length: 791
Subcellular Location: Membrane
EC: 3.4.24.-
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O22342 | MDQVQHPSVMQKVAGQLFRSSHSQDFQGYNGSFRSPALYQRRAAYGNYSNAALQHPVRAFGDLSMVPSTASAICVQAPAEKGFSSFAIDFLMGGVSAAVSKTAAAPIERVKLLIQNQDEMIKSGRLSEPYKGIGDCFKRTIKDEGFGSLWRGNTANVIRYFPTQALNFAFKDYFKRLFNFKKDRDGYWKWFAGNLASGGAAGASSLLFVYSLDYARTRLANDAKAAKKGGERQFNGLVDVYRKTLKSDGIAGLYRGFNISCVGIIVYRGLYFGMYDSLKPVLLTGSMQDSFFASFVLGWLITNGAALASYPIDTVRRRMMMTSGKAVKYKSSLDAFSQILKNEGGKSLFKGAGSNILRAIAGAGVLAGYDKLQLIVFGKKYGSGGA | Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
Catalytic Activity: ADP(in) + ATP(out) = ADP(out) + ATP(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42093
Sequence Length: 386
Domain: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. At least 2 of the odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Subcellular Location: Mitochondrion inner membrane
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P12235 | MGDHAWSFLKDFLAGGVAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQLFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFHGLGDCIIKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIFVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGAKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV | Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell . Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity . Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis (By similarity). Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A4/ANT1 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity) (By similarity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it (By similarity). Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death . It is however unclear if SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity).
PTM: Under cell death induction, transglutaminated by TGM2. Transglutamination leads to formation of covalent cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming polymers.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ADP(in) + ATP(out) = ADP(out) + ATP(in)
Sequence Mass (Da): 33064
Sequence Length: 298
Domain: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Subcellular Location: Mitochondrion inner membrane
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P48962 | MGDQALSFLKDFLAGGIAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGSSQREFNGLGDCLTKIFKSDGLKGLYQGFSVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTLDCWRKIAKDEGANAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV | Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell . Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity . Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis . Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A4/ANT1 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity) . Proton transporter activity requires free fatty acids as cofactor, but does not transport it . Probably mediates mitochondrial uncoupling in tissues that do not express UCP1 . Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death . It is however unclear if SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates it . Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 .
PTM: Under cell death induction, transglutaminated by TGM2 . Transglutamination leads to formation of covalent cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming polymers .
Location Topology: Multi-pass membrane protein
Catalytic Activity: ADP(in) + ATP(out) = ADP(out) + ATP(in)
Sequence Mass (Da): 32904
Sequence Length: 298
Domain: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Subcellular Location: Mitochondrion inner membrane
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O46373 | MSDQALSFLKDFLAGGVAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFSGLGNCLTKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQTVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWKKIAKDEGAKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV | Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity. Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis. Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A4/ANT1 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it. Probably mediates mitochondrial uncoupling in tissues that do not express UCP1. Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death. It is however unclear if SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity).
PTM: Under cell death induction, transglutaminated by TGM2. Transglutamination leads to formation of covalent cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming polymers.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ADP(in) + ATP(out) = ADP(out) + ATP(in)
Sequence Mass (Da): 32901
Sequence Length: 298
Domain: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Subcellular Location: Mitochondrion inner membrane
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Q05962 | MGDQALSFLKDFLAGGIAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGSSQREFNGLGDCLTKIFKSDGLKGLYQGFSVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGRKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV | Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity (By similarity). Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis. Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A4/ANT1 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it (By similarity). Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death (By similarity). It is however unclear if SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity).
PTM: Under cell death induction, transglutaminated by TGM2. Transglutamination leads to formation of covalent cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming polymers.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ADP(in) + ATP(out) = ADP(out) + ATP(in)
Sequence Mass (Da): 32989
Sequence Length: 298
Domain: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Subcellular Location: Mitochondrion inner membrane
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P04710 | MSHTETQTQQSHFGVDFLMGGVSAAIAKTGAAPIERVKLLMQNQEEMLKQGSLDTRYKGILDCFKRTATHEGIVSFWRGNTANVLRYFPTQALNFAFKDKIKSLLSYDRERDGYAKWFAGNLFSGGAAGGLSLLFVYSLDYARTRLAADARGSKSTSQRQFNGLLDVYKKTLKTDGLLGLYRGFVPSVLGIIVYRGLYFGLYDSFKPVLLTGALEGSFVASFLLGWVITMGASTASYPLDTVRRRMMMTSGQTIKYDGALDCLRKIVQKEGAYSLFKGCGANIFRGVAAAGVISLYDQLQLIMFGKKFK | Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell . Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
Catalytic Activity: ADP(in) + ATP(out) = ADP(out) + ATP(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34121
Sequence Length: 309
Domain: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Subcellular Location: Mitochondrion inner membrane
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Q7PQV7 | MPGLSDPVAFIKDFAAGGISAAISKTAVAPIERVKLLLQVQHISKQIAEADRYKGMVDCFVRIPREQGFSAFWRGNLANVIRYFPTQALNFAFKDKYKQVFLGGVDKNTQFTRYFIGNLASGGMAGATSLCFVYPLDFARTRLAADVGKGAEAREFKGLGDCISKIFKTDGLVGLYRGFGVSVQGIIIYRAAYFGFYDTARGMLPNPKTTPWYVSWAIAQCVTTVAGIVSYPFDTVRRRMMMQSGRAKSEIVYKGTLHCWATIAKQEGTGAFFKGAFSNVLRGTGGAFVLVLYDEIKKVL | Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
Catalytic Activity: ADP(in) + ATP(out) = ADP(out) + ATP(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32962
Sequence Length: 300
Domain: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Subcellular Location: Mitochondrion inner membrane
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Q19204 | MLLPLLISGLLFRNADAFLPFFNEDDLKYTFGVDTHAEVPNHEEIDPVPYYHQNGSLHKLEFMAFNKKYNLSLEPTLAKLLSSGVTVVKKNEKKGGSLDFGSTLDSCHYHHYGEKVYAAISNCDGRIKGTVIDDGEIIVVHPFPDHHAHRSKRATENGAHVVYKRETLAGEPKDFCGLDNVVTEESLVEDESAIFEDVFVTGQRLTQQSDLIVELAVFVDENLWRHFSSKHGGMADRKLQDYTLTLLNNIQIMYYQPTASPPLTFRVIRYEVLTRQPSALAGYLHNHGNAQMYLDRFCRYQRNLAVRDWDHAIMLTGYDIHRGAGSRSISGIARLDGMCDPWNTCTLAEGLDFTSAFIGTHELGHSVGMRHDEPYCQSKHIMSSSLGPGKVTWSTCSLRDYHQFLQRLDGRGKNCLRVSNMPNKLEISSNVKPGQIYDANLQCELMHGNGYQQVTPRQDSYDGICYMMWCGQSSFGRIITSHPALEGTFCGPSKWCQLGRCVPWTGTNEIQPTVQHVAPVVTTLPSRIDGSWSGWGATICSQCTCNGILGSVGLAIARRTCSAPYPANGGSDCVGSTSRAVLCSRQCGRASKSVDEYISDKCMEQKRLKNDRELTGKGSQLNRFPQRACKVFCDVQQHYGSQRNYRFFGDNLPDGTSCGYDRYCLDGECLALNCNNNALISRDQSCPTDTCPITDQSSSVYRGQWGTWSLWTSCTATCGGGYRKRNRACSITGQCEGNEDETEVCSSESCPSVLRVGNEWSTWTEWNHCSVSCGRGSQARYRKCLSPHRTLAFDCPEKNIEVRSCDNGPCNAIGVWGTWGGWSTCSTSCGPGTLVRQRTCNREPCDGSAHERRSCNVATCQNDGIWSLWNEWSDCSRVCGKGLRSRSRSCFGSGCMGASSEQQFCNEQACASSSANDWGTWSGWSQCSVSCGAGVKRRTRTCRTGNCPGNYKESAICNDRDCENKNAAWGGWGYWSSCSETCGDGVRKRVRKCYGSGNCDGQQYEKQYCNLRVCDFRRKF | Function: Regulates body size probably independently of the TGF beta-like dbl-1 pathway. However, may regulate some dbl-1-mediated transcription. Plays a role in cuticle collagen fibril organization. Required for embryonic development.
Sequence Mass (Da): 113527
Sequence Length: 1020
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.-
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P12857 | MADQANQPTVLHKLGGQFHLSSSFSEGVRARNICPSFSPYERRFATRNYMTQSLWGPSMSVSGGINVPVMPTPLFANAPAEKGGKNFMIDFMMGGVSAAVSKTAAAPIERVKLLIQNQDEMIKSGRLSEPYKGIADCFKRTIKDEGFSSLWRGNTANVIRYFPTQALNFAFKDYFKRLFNFKKDRDGYWKWFAGNLASGGAAGASSLFFVYSLDYARTRLANDAKAAKGGGDRQFNGLVDVYRKTLKSDGIAGLYRGFNISCVGIIVYRGLYFGLYDSIKPVVLTGSLQDNFFASFALGWLITNGAGLASYPIDTVRRRMMMTSGEAVKYKSSLDAFQQILKKEGPKSLFKGAGANILRAIAGAGVLSGYDQLQILFFGKKYGSGGA | Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
Catalytic Activity: ADP(in) + ATP(out) = ADP(out) + ATP(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42333
Sequence Length: 387
Domain: The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. At least 2 of the odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue.
Subcellular Location: Mitochondrion inner membrane
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Q9ZN78 | MAKQARAVQTWRSIVDAAASVFDDYGYERAAISEILRRAKVTKGALYFHFASKEAIAQAIMDEQTSTVEFEQEGSPLQSLVDGGQQFAFALRHNSMARAGTRLSIEGVFLGGPHPWGDWIDATARMLELGQERGEVFPQIDPMVSAKIIVASFTGIQLVSEADSGRADLRGQVAEMWRHILPSIAHPGVIAHIKPEGRVDLAAQAREKAEREEQEARIAAEAKGAGSDAATDSGSRSGGSGLRGGGSGRGPRAGGAGDEGDEEPAGAGVAAGGVVA | Function: Represses adpA expression by binding to the promoter region in the absence of A-factor, causing repression of streptomycin production and of sporulation.
Sequence Mass (Da): 28950
Sequence Length: 276
Domain: Binds DNA through its N-terminal H-T-H motif and binds A-factor via its C-terminal region.
Subcellular Location: Cytoplasm
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Q8LAW2 | MAEQETTSNINTINDQAEEETRTKSQPLISGLPNDIAELCLLRLPYPYHALYRSVSSSWNKTITNPRFLFSKQSLSISSPYLFVFAFNKSTARIQWQSLDLASGRWFVLPPMPNSFTKISSPHALSCASMPRQGKLFVLGGGDVNRSAVVYTALTNRWSCISPMMSPRTYFVSGNVNGKIMAVGGSVGGNGEATTEVESYDPDNDTWTVVKKLPMVLAKYDSAVIGKEMCVTEGWAWPFMFPPMGQVYDSDEGTWREMSGGMKEGWTGVSVVIRDRLFVISEHGDFPMKVYCSDDDTWRYVSGEKLQGEKMRRPFAVTGADDRVFVVASGINVAEGRVSEGQNGDFSVEWRMVSSPKSSIQFSPASCHVLYV | Function: Component of SCF (ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Part of the phyA-mediated signaling transduction pathway leading to the regulation of gene expression and hypocotyls elongation in response to red and far-red light exposure.
Sequence Mass (Da): 41278
Sequence Length: 372
Domain: The kelch repeats form a beta-propeller structure involved in protein-protein interaction.
Pathway: Protein modification; protein ubiquitination.
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Q2I8V6 | MNRWGLIGASTIAREWVIGAIRATGGEVVSMMSTSAERGAAYATENGIGKSVTSVEELVGDPDVDAVYVSTTNELHREQTLAAIRAGKHVLCEKPLAMTLEDAREMVVAAREAGVVLGTNHHLRNAAAHRAMRDAIAEGRIGRPIAARVFHAVYLPPHLQGWRLERPEAGGGVILDITVHDADTLRFVLNDDPAEAVAISHSAGMGKEGVEDGVMGGVRFQSGVIAQFHDAFTTKFAETGFEVHGTEGSLIGRNVMTQKPVGTVTLRNAEGESQLPLDPANLYETALAAFHSAIEGHGQPSATGEDGVWSLATGLAVVKAAATGQAAEIETGL | Function: Catalyzes the NADPH-specific reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-D-mannitol. Also shows some activity against structurally related compounds such as 3-keto-1,5-anhydro-D-fructose, D-glucosone and D-xylosone. The enzyme cannot use NADH as cosubstrate.
Catalytic Activity: 1,5-anhydro-D-mannitol + NADP(+) = 1,5-anhydro-D-fructose + H(+) + NADPH
Sequence Mass (Da): 35010
Sequence Length: 333
EC: 1.1.1.292
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Q84LB2 | MEFRVHLQADNEQKIFQNQMKPEPEASYLINQRRSANYKPNIWKNDFLDQSLISKYDGDEYRKLSEKLIEEVKIYISAETMDLVAKLELIDSVRKLGLANLFEKEIKEALDSIAAIESDNLGTRDDLYGTALHFKILRQHGYKVSQDIFGRFMDEKGTLENHHFAHLKGMLELFEASNLGFEGEDILDEAKASLTLALRDSGHICYPDSNLSRDVVHSLELPSHRRVQWFDVKWQINAYEKDICRVNATLLELAKLNFNVVQAQLQKNLREASRWWANLGIADNLKFARDRLVECFACAVGVAFEPEHSSFRICLTKVINLVLIIDDVYDIYGSEEELKHFTNAVDRWDSRETEQLPECMKMCFQVLYNTTCEIAREIEEENGWNQVLPQLTKVWADFCKALLVEAEWYNKSHIPTLEEYLRNGCISSSVSVLLVHSFFSITHEGTKEMADFLHKNEDLLYNISLIVRLNNDLGTSAAEQERGDSPSSIVCYMREVNASEETARKNIKGMIDNAWKKVNGKCFTTNQVPFLSSFMNNATNMARVAHSLYKDGDGFGDQEKGPRTHILSLLFQPLVN | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Sesquiterpene synthase catalyzing the production of (E,E)-alpha-farnesene, the predominant terpene produced during storage of fruits. Produces all six isomers (E,E)-alpha-farnesene, (Z,E)-alpha-farnesene, (E,Z)-alpha-farnesene, (Z,Z)-alpha-farnesene, (E)-beta-farnesene and (Z)-beta-farnesene from a mix of isomeric forms of the farnesyl diphosphate precursor. Able to convert geranyl diphosphate to the monoterpenes (E)-beta-ocimene, linalool and beta-myrcene. Has also a prenyltransferase activity producing alpha-farnesene directly from geranyl diphosphate and isoprenyl diphosphate.
Catalytic Activity: (2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene + diphosphate
Sequence Mass (Da): 66183
Sequence Length: 576
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Subcellular Location: Cytoplasm
EC: 4.2.3.46
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G4FEF4 | MEIFGKTFREGRFVLKEKNFTVEFAVEKIHLGWKISGRVKGSPGRLEVLRTKAPEKVLVNNWQSWGPCRVVDAFSFKPPEIDPNWRYTASVVPDVLERNLQSDYFVAEEGKVYGFLSSKIAHPFFAVEDGELVAYLEYFDVEFDDFVPLEPLVVLEDPNTPLLLEKYAELVGMENNARVPKHTPTGWCSWYHYFLDLTWEETLKNLKLAKNFPFEVFQIDDAYEKDIGDWLVTRGDFPSVEEMAKVIAENGFIPGIWTAPFSVSETSDVFNEHPDWVVKENGEPKMAYRNWNKKIYALDLSKDEVLNWLFDLFSSLRKMGYRYFKIDFLFAGAVPGERKKNITPIQAFRKGIETIRKAVGEDSFILGCGSPLLPAVGCVDGMRIGPDTAPFWGEHIEDNGAPAARWALRNAITRYFMHDRFWLNDPDCLILREEKTDLTQKEKELYSYTCGVLDNMIIESDDLSLVRDHGKKVLKETLELLGGRPRVQNIMSEDLRYEIVSSGTLSGNVKIVVDLNSREYHLEKEGKSSLKKRVVKREDGRNFYFYEEGERE | Function: Hydrolyzes the short-chain alpha-galactosaccharides raffinose, melibiose and stachyose.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
Sequence Mass (Da): 63657
Sequence Length: 552
EC: 3.2.1.22
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Q9UPQ3 | MNYQQQLANSAAIRAEIQRFESVHPNIYSIYELLERVEEPVLQNQIREHVIAIEDAFVNSQEWTLSRSVPELKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPPEAQFAMWVDAVIFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDVAQKIVATRKKQQLSIGPCKSLPNSPSHSSVCSAQVSAVHISQTSNGGGSLSDYSSSVPSTPSTSQKELRIDVPPTANTPTPVRKQSKRRSNLFTSRKGSDPDKEKKGLESRADSIGSGRAIPIKQGMLLKRSGKSLNKEWKKKYVTLCDNGVLTYHPSLHDYMQNVHGKEIDLLRTTVKVPGKRPPRATSACAPISSPKTNGLSKDMSSLHISPNSGNVTSASGSQMASGISLVSFNSRPDGMHQRSYSVSSADQWSEATVIANSAISSDTGLGDSVCSSPSISSTTSPKLDPPPSPHANRKKHRRKKSTSNFKADGLSGTAEEQEENFEFIIVSLTGQTWHFEATTYEERDAWVQAIESQILASLQSCESSKNKSRLTSQSEAMALQSIRNMRGNSHCVDCETQNPNWASLNLGALMCIECSGIHRNLGTHLSRVRSLDLDDWPVELIKVMSSIGNELANSVWEESSQGRTKPSVDSTREEKERWIRAKYEQKLFLAPLPCTELSLGQHLLRATADEDLRTAILLLAHGSRDEVNETCGEGDGRTALHLACRKGNVVLAQLLIWYGVDVTARDAHGNTALAYARQASSQECIDVLLQYGCPDERFVLMATPNLSRRNNNRNNSSGRVPTII | Function: GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system.
PTM: Phosphorylated on tyrosines.
Sequence Mass (Da): 94470
Sequence Length: 857
Domain: The PH domain mediates AP-3 binding.
Subcellular Location: Cytoplasm
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Q8BXK8 | MNYQQQLANSAAIRAEIQRFESVHPNIYSIYELLERVEEPVLQNQIREHVIAIEDAFVNSQEWTLSRSVPELKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPPEAQFAMWVDAVIFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSTNPRVIDDVRARKLSNDLKRCTYYETCATYGLNVERVFQDVAQKIVATRKKQQLSIGPCKSLPNSPSHSSVCSAQVSAVHISQTSNGGGSLSDYSSSVPSTPSTSQKELRIDVPPTANTPTPVRKQSKRRSNLFTSRKGSDPDKEKKGLESRADSIGSGRAIPIKQGMLLKRSGKSLNKEWKKKYVTLCDNGVLTYHPSLHDYMQNVHGKEIDLLRTTVKVPGKRPPRATSACAPISSPKTNGLAKDMSSLHISPNSGNVTSASGSQMASGISLVSFNSRPDGMHQRSYSVSSADQWSDATVIANSAISSDTGLGDSVCSSPSISSSTSPKLDPPPSPHANRKKHRRKKSTSNFKADGLSGTAEEQEENLEFIIVSLTGQTWHFEATTYEERDAWVQAIESQILASLQSCESSKNKSRLTSQSEAMALQSIRNMRGNSHCVDCDTQNPNWASLNLGALMCIECSGIHRNLGTHLSRVRSLDLDDWPMELIKVMSSIGNELANSVWEEGSQGRTKPSLDSTREEKERWIRAKYEQKLFLAPLPCTEFSLGQQLLRATAEEDLRTVILLLAHGSRDEVNETCGEGDGRTALHLACRKGNVVLAQLLIWYGVDVMARDAHGNTALAYARQASSQECIDVLLQYGCPDERFVLMATPNLSRKSNSRNNSSGRAPSVI | Function: GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system (By similarity).
PTM: Phosphorylated on tyrosines.
Sequence Mass (Da): 94411
Sequence Length: 857
Domain: The PH domain mediates AP-3 binding.
Subcellular Location: Cytoplasm
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P13734 | MLKVIPWLLVTSSLVAIPTYIHATTEVVVNLNVKHSVEGKSEFERKNHIKLHSTLNDNDWQGEEDKLKYMMEELDVYFGRDNGGTVWNFNQAIEDPANIGYADPQNIIARGQAQRETNWGQNKSALHQYDGRGDLMIGGQPRAHYLGNTSPCCGGSAWQAKGGDAVGDFLGQYVNEFFRSAGDPVTKGHLAPVYFEVLNEPLYQVTDAPHELGLEQPIPPIDIFTFHNDVADAFRQHNTHIKIGGFTVAFPIFEQREFARWEERMKLFIDTSGSHMDVYSTHFYDLEDDNRFKGSRLEATLDMIDQYSLLALGETKPHVISEYGGRNRPMENAPWSALRDWWFLKTASPMLMQFLSRPDSVLTSIPFVPIKALWGTAADGTPYNWRLLRQQKEAPNETGENWVFTEMVKFYQLWSDVKGTRVDTFSTNSDFLIDSYVQNDKAYVLISNLTEQAEKIVVHKYGAPASSQPTTRIKHLYLKGAAPRLMKQVMRQISKKSRLLLKRLW | Catalytic Activity: Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
Sequence Mass (Da): 57617
Sequence Length: 505
Subcellular Location: Secreted
EC: 3.2.1.81
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P07883 | MVNRRDLIKWSAVALGAGAGLAGPAPAAHAADLEWEQYPVPAAPGGNRSWQLLPSHSDDFNYTGKPQTFRGRWLDQHKDGWSGPANSLYSARHSWVADGNLIVEGRRAPDGRVYCGYVTSRTPVEYPLYTEVLMRVSGLKLSSNFWLLSRDDVNEIDVIECYGNESLHGKHMNTAYHIFQRNPFTELARSQKGYFADGSYGYNGETGQVFGDGAGQPLLRNGFHRYGVHWISATEFDFYFNGRLVRRLNRSNDLRDPRSRFFDQPMHLILNTESHQWRVDRGIEPTDAELADPSINNIYYRWVRTYQAV | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
Sequence Mass (Da): 35164
Sequence Length: 309
Subcellular Location: Secreted
EC: 3.2.1.81
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Q8U3D2 | MKAKVVINLVKINKKIIPDKIYVYRLFNDPEEELQKEGYSIYRLAYENVGIVIDPENLIIATTKELEYEGEFIPEGEISFSELRNDYQSKLVLRLLKENGIGEYELSKLLRKFRKPKTFGDYKVIPSVEMSVIKHDEDFYLVIHIIHQIQSMKTLWELVNKDPKELEEFLMTHKENLMLKDIASPLKTVYKPCFEEYTKKPKLDHNQEIVKYWYNYHIERYWNTPEAKLEFYRKFGQVDLKQPAILAKFASKIKKNKNYKIYLLPQLVVPTYNAEQLESDVAKEILEYTKLMPEERKELLENILAEVDSDIIDKSLSEIEVEKIAQELENKIRVRDDKGNSVPISQLNVQKSQLLLWTNYSRKYPVILPYEVPEKFRKIREIPMFIILDSGLLADIQNFATNEFRELVKSMYYSLAKKYNSLAKKARSTNEIGLPFLDFRGKEKVITEDLNSDKGIIEVVEQVSSFMKGKELGLAFIAARNKLSSEKFEEIKRRLFNLNVISQVVNEDTLKNKRDKYDRNRLDLFVRHNLLFQVLSKLGVKYYVLDYRFNYDYIIGIDVAPMKRSEGYIGGSAVMFDSQGYIRKIVPIKIGEQRGESVDMNEFFKEMVDKFKEFNIKLDNKKILLLRDGRITNNEEEGLKYISEMFDIEVVTMDVIKNHPVRAFANMKMYFNLGGAIYLIPHKLKQAKGTPIPIKLAKKRIIKNGKVEKQSITRQDVLDIFILTRLNYGSISADMRLPAPVHYAHKFANAIRNEWKIKEEFLAEGFLYFV | Cofactor: Probably binds 2 Mn(2+) per subunit; only 1 is seen in the structure (By similarity). Mn(2+) is the preferred cation for cleavage, Co(2+) can be used but not Mg(2+), Ca(2+), Cu(2+), Fe(2+) or Ni(2+) .
Function: A DNA-guided ssDNA endonuclease that may play a role in defense against invading mobile genetic elements. Uses short 5'-phospho-ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in cleavage of the target DNA (tDNA). Endonucleolytically cleaves DNA in short dsDNA (the gDNA indicates where to cleave on the tDNA). Efficient guide-dependent target DNA cleavage requires a minimal gDNA length of 15 nucleotides (nt) and works up to at least 31 nt. Overexpression decreases plasmid transformation efficiency. Has no appreciable activity with gRNA or on target RNA. Also has guide-independent activity on plasmid DNA called 'chopping' . The cleavage site is 10 nucleotides (nt) downstream of the target residue base-paired with the 5'-end of the gDNA, cleavage is insensitive to adenine methylation. DNA cleavage produces 5'-phosphomonoesters (as it can be ligated by T4 DNA ligase) .
Sequence Mass (Da): 90390
Sequence Length: 770
Domain: Has 4 domains; N-terminal, PAZ, Mid and PIWI. The N-terminal, Mid and PIWI domains form a crescent-shaped base with a stalk rising from the end of the N-terminal domain that holds the PAZ domain above the cresent. A groove is present in the center of the crescent closed off by the PAZ domain, in which the putative active sites are found. The PIWI domain assumes an RNase H fold and has the catalytic residues.
EC: 3.1.24.-
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Q31N05 | MDLLSNLRRSSIVLNRFYVKSLSQSDLTAYEYRCIFKKTPELGDEKRLLASICYKLGAIAVRIGSNIITKEAVRPEKLQGHDWQLVQMGTKQLDCRNDAHRCALETFERKFLERDLSASSQTEVRKAAEGGLIWWVVGAKGIEKSGNGWEVHRGRRIDVSLDAEGNLYLEIDIHHRFYTPWTVHQWLEQYPEIPLSYVRNNYLDERHGFINWQYGRFTQERPQDILLDCLGMSLAEYHLNKGATEEEVQQSYVVYVKPISWRKGKLTAHLSRRLSPSLTMEMLAKVAEDSTVCDREKREIRAVFKSIKQSINQRLQEAQKTASWILTKTYGISSPAIALSCDGYLLPAAKLLAANKQPVSKTADIRNKGCAKIGETSFGYLNLYNNQLQYPLEVHKCLLEIANKNNLQLSLDQRRVLSDYPQDDLDQQMFWQTWSSQGIKTVLVVMPWDSHHDKQKIRIQAIQAGIATQFMVPLPKADKYKALNVTLGLLCKAGWQPIQLESVDHPEVADLIIGFDTGTNRELYYGTSAFAVLADGQSLGWELPAVQRGETFSGQAIWQTVSKLIIKFYQICQRYPQKLLLMRDGLVQEGEFQQTIELLKERKIAVDVISVRKSGAGRMGQEIYENGQLVYRDAAIGSVILQPAERSFIMVTSQPVSKTIGSIRPLRIVHEYGSTDLELLALQTYHLTQLHPASGFRSCRLPWVLHLADRSSKEFQRIGQISVLQNISRDKLIAV | Cofactor: Cleavage is more efficient in Mn(2+), has weak cleavage activity with Mg(2+) . Cleavage probaby requires 2 divalent metal cations (By similarity).
Function: A DNA-guided ssDNA endonuclease that might play a role in defense against invading mobile genetic elements. Uses short ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in cleavage of the target DNA (tDNA). The cleavage site is 10 nucleotides (nt) downstream of the target residue base-paired with the 5'-end of the gDNA. Both 5'-P and 5'-OH gDNAs confer activity; a 5'-OH guide cleaves between nt 10-11 and nt 11-12. Guide DNA mismatches in the seed (nt 2-9) can enhance activity, mismatches 1-5 nt after the cleavage site block activity. Has no appreciable activity with guide RNA or on target RNA. In situ binds to 5'-phosphorylated DNA 14-20 nt in length; small DNA maps over the chromosome and plasmid with some preference for the replication origin and the probable termination site. Also has weak guide-independent nuclease activity on DNA called 'chopping'. Overexpression of wild-type or catalytically inactive mutant has no visible effect during growth under continuous high light for up to a month.
Sequence Mass (Da): 83748
Sequence Length: 735
Domain: Has 4 domains (N-terminal, PAZ, Mid and PIWI). The N-terminal and PAZ domains are joined by linker L1, the PAZ and Mid domains are joined by linker L2. The domains assemble in 2 lobes; the PAZ lobe consists of the N-terminal, L1, PAZ and L2 domains, while the PIWI lobe has the Mid and PIWI domains. The PIWI domain assumes an RNase H fold and has the catalytic residues. gDNA lies between the 2 lobes, with its unpaired 5'-end anchored in the Mid lobe.
EC: 3.1.24.-
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Q746M7 | MNHLGKTEVFLNRFALRPLNPEELRPWRLEVVLDPPPGREEVYPLLAQVARRAGGVTVRMGDGLASWSPPEVLVLEGTLARMGQTYAYRLYPKGRRPLDPKDPGERSVLSALARRLLQERLRRLEGVWVEGLAVYRREHARGPGWRVLGGAVLDLWVSDSGAFLLEVDPAYRILCEMSLEAWLAQGHPLPKRVRNAYDRRTWELLRLGEEDPKELPLPGGLSLLDYHASKGRLQGREGGRVAWVADPKDPRKPIPHLTGLLVPVLTLEDLHEEEGSLALSLPWEERRRRTREIASWIGRRLGLGTPEAVRAQAYRLSIPKLMGRRAVSKPADALRVGFYRAQETALALLRLDGAQGWPEFLRRALLRAFGASGASLRLHTLHAHPSQGLAFREALRKAKEEGVQAVLVLTPPMAWEDRNRLKALLLREGLPSQILNVPLREEERHRWENALLGLLAKAGLQVVALSGAYPAELAVGFDAGGRESFRFGGAACAVGGDGGHLLWTLPEAQAGERIPQEVVWDLLEETLWAFRRKAGRLPSRVLLLRDGRVPQDEFALALEALAREGIAYDLVSVRKSGGGRVYPVQGRLADGLYVPLEDKTFLLLTVHRDFRGTPRPLKLVHEAGDTPLEALAHQIFHLTRLYPASGFAFPRLPAPLHLADRLVKEVGRLGIRHLKEVDREKLFFV | Cofactor: Binds 3 Mn(2+) per subunit (Probable). Target RNA cleavage occurs in the presence of Mn(2+) . Prefers Mn(2+) over Mg(2+) for tDNA cleavage . tDNA cleavage occurs in the presence of Mn(2+) or Mg(2+) with a slight preference for Mn(2+), no cleavage occurs in the presence of Ca(2+) .
Function: A DNA-guided ssDNA endonuclease. Uses short ssDNA sequences as guides (gDNA, also called small interfering DNA, siDNA) to bind complementary DNA target strands, resulting in cleavage of the target DNA (tDNA). The cleavage site is 10 nucleotides (nt) downstream of the target residue base-paired with the 5'-end of the gDNA . Plays a role in completion of DNA replication, participates in decatenating replicated DNA and plasmid. In situ purifies with 5'-phosphorylated long DNA (about 1160 nt, maps to the whole chromosome and plasmid), 25-35 nt RNAs that map to the whole chromosome and 15-18 nt DNA that maps to the replication terminus region (ter) on the chromosome and plasmid. Most short DNA starts with dC . Has been shown to have guide sequence-independent dsDNase activity called 'chopping', which requires unstable DNA (high AT-content, multiple mismatches or low salt conditions), and could be used to generate gDNA. Preferentially binds tDNA with dC at its 3'-terminus . Has also been shown to have no detectable guide sequence-independent dsDNase activity . The latter study proposes TtAgo may acquire gDNA from nicked dsDNA, by binding to 5'-phosphorylated-dC nicks, then cleaving 10 nt away on the opposite strand; subsequently an exonuclease (maybe AddA-AddB helicase/nuclease) trims the ends to generate the gDNA (Probable).
Sequence Mass (Da): 76611
Sequence Length: 685
Domain: Has 4 domains (N-terminal, PAZ, Mid and PIWI). The N-terminal and PAZ domains are joined by linker L1, the PAZ and Mid domains are joined by linker L2. The domains assemble in 2 lobes; the PAZ lobe consists of the N-terminal, L1, PAZ and L2 domains, while the PIWI lobe has the Mid and PIWI domains. The PIWI domain assumes an RNase H fold and has the catalytic residues. gDNA lies between the 2 lobes, with its unpaired 5'-end anchored in the Mid lobe while the 3'-end anchors in the PAZ domain in the absence of target or if target nucleic acid has not fully base-paired with the gDNA. The N-terminal, Mid and PAZ domains alter position upon binding different length gDNA, forming and closing DNA-binding channels . The 2 lobes and gDNA move considerably upon formation of the ternary gDNA:target RNA:TtAgo complex to accomodate and base pair the target RNA . Deletions of the N-terminus (residues 1-106 or 1-177) have lost catalytic activity . Upon release of the 3'-end of the gDNA from the PAZ domain during nucleic acid duplex formation, Glu-512 moves about 13 Angstroms to complete the active site .
EC: 3.1.24.-
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Q9M0S4 | MASKSVVVLLFLALIASSAIAQAPGPAPTRSPLPSPAQPPRTAAPTPSITPTPTPTPSATPTAAPVSPPAGSPLPSSASPPAPPTSLTPDGAPVAGPTGSTPVDNNNAATLAAGSLAGFVFVASLLL | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline residues are glycosylated with arabinogalactan.
Location Topology: Lipid-anchor
Sequence Mass (Da): 12071
Sequence Length: 127
Subcellular Location: Cell membrane
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Q9FVE0 | MARLFVVVALLALAVGTVFAADAPSAAPTASPTKSPTKAPAAAPKSSAAAPKASSPVAEEPTPEDDYSAASPSDSAEAPTVSSPPAPTPEADGPSSDGPSSDGPAAAESPKSGATTNVKLSIAGTVAAAGFFIFSL | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on the hydroxyproline residues.
Location Topology: Lipid-anchor
Sequence Mass (Da): 12992
Sequence Length: 136
Subcellular Location: Cell membrane
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Q9LJD9 | MESMKMKLIVVLMVAIVAFSAVGNVAAQTEAPAPSPTSDAAMFVPALFASVAALASGFLF | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: Contains 4-hydroxyproline; hydroxylated on Pro-32, Pro-34 and Pro-36.
Location Topology: Lipid-anchor
Sequence Mass (Da): 6089
Sequence Length: 60
Subcellular Location: Cell membrane
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Q9STQ3 | MEAMKMRLFVAVLVAAMAFSAVQQAAAVEAPAPSPTSDASLAIPAFFASVATLAFGFLF | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: Contains 4-hydroxyproline; hydroxylated on Pro-31, Pro-33 and Pro-35.
Location Topology: Lipid-anchor
Sequence Mass (Da): 6052
Sequence Length: 59
Subcellular Location: Cell membrane
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Q9LVC0 | MEAMKMKLYVVVLVAVIAFSTVHQTVAAVDAPAPSPTSDASSFIPTFFASVAVMAFGFFF | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death (Probable). Involved in the regulation of root hair elongation .
PTM: Contains 4-hydroxyproline; hydroxylated on Pro-32, Pro-34 and Pro-36.
Location Topology: Lipid-anchor
Sequence Mass (Da): 6363
Sequence Length: 60
Subcellular Location: Cell membrane
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Q9LYF6 | MAISKASIVVLMMVIISVVASAQSEAPAPSPTSGSSAISASFVSAGVAAVAALVFGSALRI | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: Contains 4-hydroxyproline; hydroxylated on Pro-27, Pro-29 and Pro-31.
Location Topology: Lipid-anchor
Sequence Mass (Da): 5849
Sequence Length: 61
Subcellular Location: Cell membrane
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O82337 | MASRNSVTGFALFSFVFAVILSLAGAQSLAPAPAPTSDGTSIDQGIAYLLMVVALVLTYLIHPLDASSSYSFF | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: Contains 4-hydroxyproline; hydroxylated on Pro-31, Pro-33 and Pro-35.
Location Topology: Lipid-anchor
Sequence Mass (Da): 7602
Sequence Length: 73
Subcellular Location: Cell membrane
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O22194 | MTRNILLTVTLICIVFITVGGQSPATAPIHSPSTSPHKPKPTSPAISPAAPTPESTEAPAKTPVEAPVEAPPSPTPASTPQISPPAPSPEADTPSAPEIAPSADVPAPALTKHKKKTKKHKTAPAPGPASELLSPPAPPGEAPGPGPSDAFSPAADDQSGAQRISVVIQMVGAAAIAWSLLVLAF | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on the hydroxyproline residues.
Location Topology: Lipid-anchor
Sequence Mass (Da): 18481
Sequence Length: 185
Subcellular Location: Cell membrane
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Q9FPR2 | MDRNFLLTVTLICIVVAGVGGQSPISSPTKSPTTPSAPTTSPTKSPAVTSPTTAPAKTPTASASSPVESPKSPAPVSESSPPPTPVPESSPPVPAPMVSSPVSSPPVPAPVADSPPAPVAAPVADVPAPAPSKHKKTTKKSKKHQAAPAPAPELLGPPAPPTESPGPNSDAFSPGPSADDQSGAASTRVLRNVAVGAVATAWAVLVMAF | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on the hydroxyproline residues.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20489
Sequence Length: 209
Subcellular Location: Cell membrane
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Q9S740 | MESNSIIWSLLLASALISSFSVNAQGPAASPVTSTTTAPPPTTAAPPTTAAPPPTTTTPPVSAAQPPASPVTPPPAVTPTSPPAPKVAPVISPATPPPQPPQSPPASAPTVSPPPVSPPPAPTSPPPTPASPPPAPASPPPAPASPPPAPVSPPPVQAPSPISLPPAPAPAPTKHKRKHKHKRHHHAPAPAPIPPSPPSPPVLTDPQDTAPAPSPNTNGGNALNQLKGRAVMWLNTGLVILFLLAMTA | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on the hydroxyproline residues.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24484
Sequence Length: 248
Subcellular Location: Cell membrane
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Q8LCN5 | MAFSKSLVFVLLAALLISSAVAQSPAPAPSNVGGRRISPAPSPKKMTAPAPAPEVSPSPSPAAALTPESSASPPSPPLADSPTADSPALSPSAISDSPTEAPGPAQGGAVSNKFASFGSVAVMLTAAVLVI | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on the hydroxyproline residues.
Location Topology: Lipid-anchor
Sequence Mass (Da): 12637
Sequence Length: 131
Subcellular Location: Cell membrane
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Q6Z232 | MARLHLVVVAMAALFAAAAVAQGPSASPTPAPKAQPPVATPPTRPPAVAPVSPPAAQPPVTTPPPVSAPAPVPAPSAAATPSPQASAPTAEPPVLSPPAPAPGSISQSPTEAPTSPPPPSAASGVSPSAAAVVAAWAAVAAVAAFY | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: O-glycosylated on hydroxyprolines; noncontiguous hydroxylproline residues are glycosylated with arabinogalactan.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13703
Sequence Length: 146
Subcellular Location: Vacuole
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P25376 | MSSSKSLYELKDLKNSSTEIHATGQDNEIEYFETGSNDRPSSQPHLGYEQHNTSAVRRFFDSFKRADQGPQDEVEATQMNDLTSAISPSSRQAQELEKNESSDNIGANTGHKSDSLKKTIQPRHVLMIALGTGIGTGLLVGNGTALVHAGPAGLLIGYAIMGSILYCIIQACGEMALVYSNLTGGYNAYPSFLVDDGFGFAVAWVYCLQWLCVCPLELVTASMTIKYWTTSVNPDVFVIIFYVLVITINIFGARGYAEAEFFFNCCKILMMTGFFILGIIIDVGGAGNDGFIGGKYWHDPGAFNGKHAIDRFKGVAATLVTAAFAFGGSEFIAITTAEQSNPRKAIPGAAKQMIYRILFLFLATIILLGFLVPYNSDQLLGSTGGGTKASPYVIAVASHGVRVVPHFINAVILLSVLSMANSSFYSSARLFLTLSEQGYAPKVFSYIDRAGRPLIAMGVSALFAVIAFCAASPKEEQVFTWLLAISGLSQLFTWTAICLSHLRFRRAMKVQGRSLGELGFKSQTGVWGSAYACIMMILILIAQFWVAIAPIGEGKLDAQAFFENYLAMPILIALYVGYKVWHKDWKLFIRADKIDLDSHRQIFDEELIKQEDEEYRERLRNGPYWKRVVAFWC | Function: Broad substrate range permease which transports asparagine and glutamine with intermediate specificity. Also transports Ala, Cys, Gly, Ile, Leu, Met, Phe, Ser, Thr, Tyr and Val. Important for the utilization of amino acids as a nitrogen source.
PTM: Palmitoylated by PFA4.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69671
Sequence Length: 633
Subcellular Location: Cell membrane
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Q9M373 | MASRNSVAVIALFAFVFAVISPFAGAQSLAPAPSPTSDGTSIDQGIAYLLMVVALVLTYLIHPLDASSSSYTFF | Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
PTM: Contains 4-hydroxyproline; hydroxylated on Pro-31, Pro-33 and Pro-35.
Location Topology: Lipid-anchor
Sequence Mass (Da): 7699
Sequence Length: 74
Subcellular Location: Cell membrane
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Q17QF0 | MTGAWGHLLRSLHLKTLSLWIPKTCFSLKARAFWTSVTRCGLHTKPSMPPCDFTPERYQSLAYSRVLEIHKQHLSPVHTAYFPEPLLLHQGHVEWLFDHEGNRYLDFFSGIVTVSVGHCHPKVNAAAQRQLGRLWHTSSVFFHPLIHEYAEKLSALLPEPLKVVFLVNSGSEANDLAMLMARAHSNSTDIISFRGAYHGCSPYTLGLTNVGIYKMDLPHGMGCQPTMCPDIFHGPWGGSHCRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPKGFLKEAFELVRERGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAAVVTTPDIAKSLTKRMLHFNTFGGNPMACAVGSAVLEVIKEENLQENSQEVGTYMLLKLAKLRDEFEIVGDVRGKGLMIGIEMVKDKESRQPLPREEVNQIHHDCKCMGLLIGRGGLFSQTFRIAPSMCITKPEVDFAVEVFRSALIQHMERRAK | Function: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure (By similarity).
Catalytic Activity: glyoxylate + L-alanine = glycine + pyruvate
Sequence Mass (Da): 57226
Sequence Length: 514
Subcellular Location: Mitochondrion
EC: 2.6.1.44
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Q9BYV1 | MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQSLGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCHPKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLMARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSHCRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPKGFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAAVITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAKLRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQTFRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK | Function: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure.
Catalytic Activity: glyoxylate + L-alanine = glycine + pyruvate
Sequence Mass (Da): 57156
Sequence Length: 514
Subcellular Location: Mitochondrion
EC: 2.6.1.44
|
Q3UEG6 | MSLAWRNLQKPFYLETSLRILQMRPSLSLGASRIAVPKLTLHTKHSMPPCDFSPEKYQSLAYSRVLAIHKQHLSPVDTAYFRKPLLLHQGHMEWLFDSEGNRYLDFFSGIVTVSVGHCHPKVSAVAKKQIDRLWHTSSVFFHSPMHEYAEKLSALLPEPLKVIFLVNSGSEANDLAMVMARAHSNHTDIISFRGAYHGCSPYTLGLTNVGIYKMEVPGGIGCQSTMCPDVFRGPWGGIHCRDSPVQTVRDCSCAPDCCQAKERYIEQFKDTLNTSVATSIAGFFAEPIQGVNGVVQYPKEFLKEAFALVRERGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAAVVTTPEIAKSLAKRLLHFSTFGGNPLACAIGSAVLEVIEEENLQRNSQEVGTYMLLKFAKLRDEFDIVGDVRGKGLMVGIEMVQDKISRQPLPKTEVNQIHEDCKDMGLLVGRGGNFSQTFRIVPPMCVTKMEVDFAYEVFRAALIQHMERRAK | Function: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure.
Catalytic Activity: glyoxylate + L-alanine = glycine + pyruvate
Sequence Mass (Da): 57115
Sequence Length: 513
Subcellular Location: Mitochondrion
EC: 2.6.1.44
|
Q54RP0 | MEKKVEYIKENDKIVLMCNYGFRDMTLNLLKCFEKLSIDKSRYILYCMDDKAYQFFAEFKGIECQRFSRDDIINSSTSSTQLFHDNNTNDNKGIYSENAESYGDIGFRAICNEKPLVVLDVLKKGYNVLWTDTDIVWKRDPFIHFYQDINQENQFTNDDDIDLYVQQDDDDICAGFYFIRSNQRTIKFIQDSINFLNPCIDDQIAMRLFLKSQGINIKSKNILLSLSENDKKDKIRYRLLDKKLFPNGTNYFNLKITQRDNITPFIIHNNCIIGHRSKKDRFIEYGLWYINDDEIDINSNINNDDENNKEIKLFKNVLKNHTDIITSINSSDDGKLFTTSIDKSIKIWKFENTSGNDTDNGIFKVLKSKYIHKRGGIWSTFIFSSNNNNNNDYGFENLLTSSHDKTIQYWDNNLQVIQTFIGHTGIINQLIVIPNSSYFFTCSDDNTIRQFDLNNINFKRVFIGHNGWVSSIAINKNLNTLYSCSNDGTIRFWDINSGRCLNIIKGNQGGWIRKIIYNDNLNQLISGGNDGTIKIWSCDNLNNFNDNQYLLKINTNENSSINDLQFDSDTNLIYCAFENGSLKSFKLTSNNNNNNNNNNNNNNNTINYSLDKVYQGHLNSSINCIHISKSLNLLFSGGFDKQIKSWDL | Cofactor: Divalent metal cations. Mn(2+) is 4-fold better than Mg(2+).
Function: Specifically catalyzes the transfer of a galactosyl residue to the hydroxyproline-linked saccharide on Skp1 protein (fpaA/fpaB). Catalyzes the formation of a Gal-alpha-1,3-Fuc linkage, leading to Gal-Fuc-Gal-GlcNAc-HyPro143-Skp1.
Catalytic Activity: an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl derivative + H(+) + UDP
Sequence Mass (Da): 75244
Sequence Length: 648
Domain: Consists of two domains: an N-terminal catalytic domain and a C-terminal domain, not required for activity, that is predicted to form a beta-propeller-like protein-protein interaction domain.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cytoplasm
EC: 2.4.1.37
|
P79785 | MVPNYSTEETVKRIHVDCPVSGRHSYIYIMVPTVYSIIFIIGIFGNSLVVIVIYCYMKLKTVASIFLLNLALADLCFLITLPLWAAYTAMEYQWPFGNCLCKLASAGISFNLYASVFLLTCLSIDRYLAIVHPVKSRIRRTMFVARVTCIVIWLLAGVASLPVIIHRNIFFAENLNMTVCGFRYDNNNTTLRVGLGLSKNLLGFLIPFLIILTSYTLIWKTLKKAYQIQRNKTRNDDIFKMIVAIVFFFFFSWIPHQVFTFLDVLIQLHVITDCKITDIVDTAMPFTICIAYFNNCLNPFFYVFFGKNFKKYFLQLIKYIPPNVSTHPSLTTKMSSLSYRPPENIRLPTKKTAGSFDAE | Function: Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C.
PTM: C-terminal Ser or Thr residues may be phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41220
Sequence Length: 359
Subcellular Location: Cell membrane
|
P30556 | MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE | Function: Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney . The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C .
PTM: C-terminal Ser or Thr residues may be phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41061
Sequence Length: 359
Subcellular Location: Cell membrane
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Q8LPN5 | MDGREAMAFPGSHSQYYLQRGAFTNLAPSQVASGLHAPPPHTGLRPMSNPNIHHPQANNPGPPFSDFGHTIHMGVVSSASDADVQPPPPPPPPEEPMVKRKRGRPRKYGEPMVSNKSRDSSPMSDPNEPKRARGRPPGTGRKQRLANLGEWMNTSAGLAFAPHVISIGAGEDIAAKVLSFSQQRPRALCIMSGTGTISSVTLCKPGSTDRHLTYEGPFEIISFGGSYLVNEEGGSRSRTGGLSVSLSRPDGSIIAGGVDMLIAANLVQVVACSFVYGARAKTHNNNNKTIRQEKEPNEEDNNSEMETTPGSAAEPAASAGQQTPQNFSSQGIRGWPGSGSGSGRSLDICRNPLTDFDLTRG | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 38312
Sequence Length: 361
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
Q940I0 | MDSREIHHQQQQQQQQQQQQQQQQQHLQQQQQPPPGMLMSHHNSYNRNPNAAAAVLMGHNTSTSQAMHQRLPFGGSMSPHQPQQHQYHHPQPQQQIDQKTLESLGFDGSPSSVAATQQHSMRFGIDHQQVKKKRGRPRKYAADGGGGGGGGSNIALGLAPTSPLPSASNSYGGGNEGGGGGDSAGANANSSDPPAKRNRGRPPGSGKKQLDALGGTGGVGFTPHVIEVKTGEDIATKILAFTNQGPRAICILSATGAVTNVMLRQANNSNPTGTVKYEGRFEIISLSGSFLNSESNGTVTKTGNLSVSLAGHEGRIVGGCVDGMLVAGSQVQVIVGSFVPDGRKQKQSAGRAQNTPEPASAPANMLSFGGVGGPGSPRSQGQQHSSESSEENESNSPLHRRSNNNNSNNHGIFGNSTPQPLHQIPMQMYQNLWPGNSPQ | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 46277
Sequence Length: 439
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
A1L4X7 | MDPNESHHHHQQQQLHHLHQQQQQQQQQQRLTSPYFHHQLQHHHHLPTTVATTASTGNAVPSSNNGLFPPQPQPQHQPNDGSSSLAVYPHSVPSSAVTAPMEPVKRKRGRPRKYVTPEQALAAKKLASSASSSSAKQRRELAAVTGGTVSTNSGSSKKSQLGSVGKTGQCFTPHIVNIAPGEDVVQKIMMFANQSKHELCVLSASGTISNASLRQPAPSGGNLPYEGQYEILSLSGSYIRTEQGGKSGGLSVSLSASDGQIIGGAIGSHLTAAGPVQVILGTFQLDRKKDAAGSGGKGDASNSGSRLTSPVSSGQLLGMGFPPGMESTGRNPMRGNDEQHDHHHHQAGLGGPHHFMMQAPQGIHMTHSRPSEWRGGGNSGHDGRGGGGYDLSGRIGHESSENGDYEQQIPD | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 43446
Sequence Length: 411
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
Q9M2S3 | MANPWWVGNVAIGGVESPVTSSAPSLHHRNSNNNNPPTMTRSDPRLDHDFTTNNSGSPNTQTQSQEEQNSRDEQPAVEPGSGSGSTGRRPRGRPPGSKNKPKSPVVVTKESPNSLQSHVLEIATGADVAESLNAFARRRGRGVSVLSGSGLVTNVTLRQPAASGGVVSLRGQFEILSMCGAFLPTSGSPAAAAGLTIYLAGAQGQVVGGGVAGPLIASGPVIVIAATFCNATYERLPIEEEQQQEQPLQLEDGKKQKEENDDNESGNNGNEGSMQPPMYNMPPNFIPNGHQMAQHDVYWGGPPPRAPPSY | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Binds the DNA sequence GNFEI (GA-negative feedback element I) in the GA3OX1 promoter . Negatively regulates plant innate immunity (PTI) to pathogens through the down-regulation of the PAMP-triggered FRK1 expression .
Sequence Mass (Da): 32603
Sequence Length: 310
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
Q9SJG4 | MAGGTALTPTSVGSKSVPMRNHEATERGNTNNNLRALPKAVQPVSSIEGEMAKRPRGRPAGSKNKPKPPIIVTHDSPNSLRANAVEISSGCDICETLSDFARRKQRGLCILSANGCVTNVTLRQPASSGAIVTLHGRYEILSLLGSILPPPAPLGITGLTIYLAGPQGQVVGGGVVGGLIASGPVVLMAASFMNAVFDRLPMDDDEAASMQNQQYYQNGRSRPLDDIHGLPQNLLTNGNSASDIYSWGPAQRVMSKP | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) . Encodes a nuclear matrix protein that acts in the maintenance of genomic integrity by silencing TEs and repeat-containing genes through epigenetic machinery. Acts as a chromatin remodeling factor that modifies the architecture of FLC and FWA chromatin by modulating both H3 acetylation and methylation leading to the regulation of FLC and FWA expression . Negatively regulates floral repressors including MAF4 and MAF5 . Plays a transcription activation role in anther development. Regulates the expression of arabinogalactan proteins (AGPs) involved in the formation of the nexine layer of the pollen wall . Binds AGP6, AGP11, AGP23 and AGP40 promoters .
Sequence Mass (Da): 27004
Sequence Length: 257
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
Q9LTA2 | MKGEYREQKSNEMFSKLPHHQQQQQQQQQQHSLTSHFHLSSTVTPTVDDSSIEVVRRPRGRPPGSKNKPKPPVFVTRDTDPPMSPYILEVPSGNDVVEAINRFCRRKSIGVCVLSGSGSVANVTLRQPSPAALGSTITFHGKFDLLSVSATFLPPPPRTSLSPPVSNFFTVSLAGPQGQIIGGFVAGPLISAGTVYVIAASFNNPSYHRLPAEEEQKHSAGTGEREGQSPPVSGGGEESGQMAGSGGESCGVSMYSCHMGGSDVIWAPTARAPPPY | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 29390
Sequence Length: 276
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
Q9LZX7 | MDEVSRSHTPQFLSSDHQHYHHQNAGRQKRGREEEGVEPNNIGEDLATFPSGEENIKKRRPRGRPAGSKNKPKAPIIVTRDSANAFRCHVMEITNACDVMESLAVFARRRQRGVCVLTGNGAVTNVTVRQPGGGVVSLHGRFEILSLSGSFLPPPAPPAASGLKVYLAGGQGQVIGGSVVGPLTASSPVVVMAASFGNASYERLPLEEEEETEREIDGNAARAIGTQTQKQLMQDATSFIGSPSNLINSVSLPGEAYWGTQRPSF | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Acts redundantly with AHL22, AHL27 and AHL29 in the regulation of flowering and regulation of the hypocotyl elongation .
Sequence Mass (Da): 28412
Sequence Length: 265
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
Q9SR17 | MANPWWTGQVNLSGLETTPPGSSQLKKPDLHISMNMAMDSGHNNHHHHQEVDNNNNDDDRDNLSGDDHEPREGAVEAPTRRPRGRPAGSKNKPKPPIFVTRDSPNALKSHVMEIASGTDVIETLATFARRRQRGICILSGNGTVANVTLRQPSTAAVAAAPGGAAVLALQGRFEILSLTGSFLPGPAPPGSTGLTIYLAGGQGQVVGGSVVGPLMAAGPVMLIAATFSNATYERLPLEEEEAAERGGGGGSGGVVPGQLGGGGSPLSSGAGGGDGNQGLPVYNMPGNLVSNGGSGGGGQMSGQEAYGWAQARSGF | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Negatively regulates plant innate immunity (PTI) to pathogens through the down-regulation of the PAMP-triggered FRK1 expression . Positively regulates defense against fungal Verticillium infection .
Sequence Mass (Da): 32038
Sequence Length: 315
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
Q8VYJ2 | MVLNMESTGEAVRSTTGNDGGITVVRSDAPSDFHVAQRSESSNQSPTSVTPPPPQPSSHHTAPPPLQISTVTTTTTTAAMEGISGGLMKKKRGRPRKYGPDGTVVALSPKPISSAPAPSHLPPPSSHVIDFSASEKRSKVKPTNSFNRTKYHHQVENLGEWAPCSVGGNFTPHIITVNTGEDVTMKIISFSQQGPRSICVLSANGVISSVTLRQPDSSGGTLTYEGRFEILSLSGSFMPNDSGGTRSRTGGMSVSLASPDGRVVGGGLAGLLVAASPVQVVVGSFLAGTDHQDQKPKKNKHDFMLSSPTAAIPISSAADHRTIHSVSSLPVNNNTWQTSLASDPRNKHTDINVNVT | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). May play a function in the positioning of chromatin fibers within the nucleus.
Sequence Mass (Da): 37312
Sequence Length: 356
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
Q8GWQ2 | MANPWWTNQSGLAGMVDHSVSSGHHQNHHHQSLLTKGDLGIAMNQSQDNDQDEEDDPREGAVEVVNRRPRGRPPGSKNKPKAPIFVTRDSPNALRSHVLEISDGSDVADTIAHFSRRRQRGVCVLSGTGSVANVTLRQAAAPGGVVSLQGRFEILSLTGAFLPGPSPPGSTGLTVYLAGVQGQVVGGSVVGPLLAIGSVMVIAATFSNATYERLPMEEEEDGGGSRQIHGGGDSPPRIGSNLPDLSGMAGPGYNMPPHLIPNGAGQLGHEPYTWVHARPPY | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Negatively regulates plant innate immunity (PTI) to pathogens through the down-regulation of the PAMP-triggered NHO1 and FRK1 expression .
Sequence Mass (Da): 29540
Sequence Length: 281
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
O82166 | MAGLDLGTTSRYVHNVDGGGGGQFTTDNHHEDDGGAGGNHHHHHHNHNHHQGLDLIASNDNSGLGGGGGGGSGDLVMRRPRGRPAGSKNKPKPPVIVTRESANTLRAHILEVGSGCDVFECISTYARRRQRGICVLSGTGTVTNVSIRQPTAAGAVVTLRGTFEILSLSGSFLPPPAPPGATSLTIFLAGAQGQVVGGNVVGELMAAGPVMVMAASFTNVAYERLPLDEHEEHLQSGGGGGGGNMYSEATGGGGGLPFFNLPMSMPQIGVESWQGNHAGAGRAPF | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). Binds to the MARs present in the ETTIN (ETT) promoter leading to a negative regulation of its gene expression. Functions as a molecular node downstream of the homeotic protein AGAMOUS (AG), regulating patterning and differentiation of reproductive organs. Acts as a chromatin remodeling factor that modifies the architecture of ETTIN (ETT) chromatin by modulating H3 methylation leading to the regulation of ETT expression. Seems to be involved in the regulation of a set of reproductives genes including CRABS CLAW (CRC), JAGGED (JAG) and KNUCKLES (KNU).
Sequence Mass (Da): 29144
Sequence Length: 285
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
O22130 | MDQVSRSLPPPFLSRDLHLHPHHQFQHQQQQQQQNHGHDIDQHRIGGLKRDRDADIDPNEHSSAGKDQSTPGSGGESGGGGGGDNHITRRPRGRPAGSKNKPKPPIIITRDSANALKSHVMEVANGCDVMESVTVFARRRQRGICVLSGNGAVTNVTIRQPASVPGGGSSVVNLHGRFEILSLSGSFLPPPAPPAASGLTIYLAGGQGQVVGGSVVGPLMASGPVVIMAASFGNAAYERLPLEEDDQEEQTAGAVANNIDGNATMGGGTQTQTQTQQQQQQQLMQDPTSFIQGLPPNLMNSVQLPAEAYWGTPRPSF | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). Binds an AT-rich DNA sequences in the FLOWERING LOCUS T (FT) promoter . Acts redundantly with AHL18, AHL27 and AHL29 in the regulation of flowering and regulation of the hypocotyl elongation. Plays a role in both photo- and skotomorphogenesis . Acts as a chromatin remodeling factor that modifies the architecture of FLOWERING LOCUS T (FT) chromatin by modulating both H3 acetylation and methylation leading to the regulation of FT expression during flowering induction .
Sequence Mass (Da): 33519
Sequence Length: 317
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
O23620 | MAGLDLGTAFRYVNHQLHRPDLHLHHNSSSDDVTPGAGMGHFTVDDEDNNNNHQGLDLASGGGSGSSGGGGGHGGGGDVVGRRPRGRPPGSKNKPKPPVIITRESANTLRAHILEVTNGCDVFDCVATYARRRQRGICVLSGSGTVTNVSIRQPSAAGAVVTLQGTFEILSLSGSFLPPPAPPGATSLTIFLAGGQGQVVGGSVVGELTAAGPVIVIAASFTNVAYERLPLEEDEQQQQLGGGSNGGGNLFPEVAAGGGGGLPFFNLPMNMQPNVQLPVEGWPGNSGGRGPF | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 29724
Sequence Length: 292
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
O49662 | MDPVQSHGSQSSLPPPFHARDFQLHLQQQQQEFFLHHHQQQRNQTDGDQQGGSGGNRQIKMDREETSDNIDNIANNSGSEGKDIDIHGGSGEGGGGSGGDHQMTRRPRGRPAGSKNKPKPPIIITRDSANALRTHVMEIGDGCDLVESVATFARRRQRGVCVMSGTGNVTNVTIRQPGSHPSPGSVVSLHGRFEILSLSGSFLPPPAPPTATGLSVYLAGGQGQVVGGSVVGPLLCAGPVVVMAASFSNAAYERLPLEEDEMQTPVHGGGGGGSLESPPMMGQQLQHQQQAMSGHQGLPPNLLGSVQLQQQHDQSYWSTGRPPY | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 34339
Sequence Length: 324
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
Q6DBQ1 | MSSYMHPLLGQELHLQRPEDSRTPPDQNNMELNRSEADEAKAETTPTGGATSSATASGSSSGRRPRGRPAGSKNKPKPPTIITRDSPNVLRSHVLEVTSGSDISEAVSTYATRRGCGVCIISGTGAVTNVTIRQPAAPAGGGVITLHGRFDILSLTGTALPPPAPPGAGGLTVYLAGGQGQVVGGNVAGSLIASGPVVLMAASFANAVYDRLPIEEEETPPPRTTGVQQQQPEASQSSEVTGSGAQACESNLQGGNGGGGVAFYNLGMNMNNFQFSGGDIYGMSGGSGGGGGGATRPAF | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Binds the DNA sequence GNFEI (GA-negative feedback element I) in the GA3OX1 promoter. Binding to GNFEI sequence is required for GA-negative feedback regulation of GA3OX1.
Sequence Mass (Da): 30148
Sequence Length: 299
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
|
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