ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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F4I9E1 | MRPRIRDVSDKLRPNRASFDDGETKFHRKHLPPLRTMFGRWRKWTVLVAAIWIQASTGTNFDFSAYSSHLKSVLGISQVRLNYLAVASDLGKAFGWSSGIALGYFPLSVVLFAAAAMGFVGYGVQWLVITNIITLPYSLVFLCCLLAGLSICWFNTACFILCIRHFPNNRALALSLTVSFNGISAALYSLAFNAINPSSSNLYLLLNSLVPLVVSFAALYPVLTKPSLDTTPDYDSRRHDSHVFTILNVLAVITSFHLLLSSSSTSSARLNFIGAVVLLVFPLCAPLLVYARDYFLPVINARLNHESSGYVMLNIDELKNQKTSVSSKTGYEHMGTAKEGNTVRLGDEHSFRLLISRLEFWLYYIAYFCGGTIGLVYSNNLGQIAQSLGQNSTTLVTIYSSFSFFGRLLSAAPDFMHKRFRLTRTGWFAIALLPTPIAFFLLAVSSSQQTALQTATALIGLSSGFIFAAAVSITSDLFGPNSVGVNHNILITNIPIGSLLYGYIAASIYEANASPDITPIVSDSIVCIGRDCYFKTFVFWGCLSILGVVSSLSLYIRTKPVYHRLEQDKVSLTSSYKDLDPL | Function: Required for karyogamy during female gametophyte development, when the two polar nuclei fuse to form the diploid central cell nucleus .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64060
Sequence Length: 582
Subcellular Location: Membrane
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Q68AP4 | MTQMRDLMIINANVRTVDARNSCAQAVLVSGGRIAIVGTETEVRGAAAPDAEVLDVSGKTVVPGFIDAHNHLSVAAFAPDSVDCSTPPLATLDEVLEVIERHCRNIPPGQWVRGINFHASHIREQRNPTRYELDEVAPNNPFFLIDASCHAGFANSAALDLVGIGAHTPEPWGGEIERDLSGKPTGTLLEAAANLLHSASWNDYAERDWDRAVELLHSKMNDYLAVGLTGVGDAMVTAKSAELYRRADAAGKMPFTLQQLHGGDHFFSMQDLGRSDTVDRIMEPESYLLRGGAMKIFVDRAYPSPAIDQIHDGCKTHVGANFYSKSEVHDLAVRASKLGINLAIHGMGNCAIDIVLDAYEAVRRQSNADTVLRLEHAFIAETGQGQRMADLGIDLVANPGLAFGWGEVFNMWRGENQEHLKLFPVRSMLDAGVRVSLASDHPCGTYSPAEIMWTAVARETMAGAPLEPDEAVTADEALRMYTINPAHASGRGSEEGSIEAGKRANLLVLDRDPVDCATGELRELQVLRTYVDGVLRYERTGS | Function: Hydrolyzes N-substituted formamides, but not amides. N-benzylformamide is the preferred substrate, while N-butylformamide is hydrolyzed at a much lower rate. Has very low activity towards allylformamide, N-(2-cyclohex-1-enylethyl)formamide and N-(alpha-methylbenzyl)formamide.
Catalytic Activity: H2O + N-benzylformamide = benzylamine + formate
Sequence Mass (Da): 58828
Sequence Length: 542
EC: 3.5.1.91
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Q16621 | MSPCPPQQSRNRVIQLSTSELGEMELTWQEIMSITELQGLNAPSEPSFEPQAPAPYLGPPPPTTYCPCSIHPDSGFPLPPPPYELPASTSHVPDPPYSYGNMAIPVSKPLSLSGLLSEPLQDPLALLDIGLPAGPPKPQEDPESDSGLSLNYSDAESLELEGTEAGRRRSEYVEMYPVEYPYSLMPNSLAHSNYTLPAAETPLALEPSSGPVRAKPTARGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLARYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLTNERERLLRARGEADRTLEVMRQQLTELYRDIFQHLRDESGNSYSPEEYALQQAADGTIFLVPRGTKMEATD | Function: Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron.
PTM: Phosphorylated on serine residues. In undifferentiated erythrocytes, phosphorylated by MAPK8 which then leads to ubiquitination and protein degradation.
Sequence Mass (Da): 41473
Sequence Length: 373
Domain: The PXY motifs are required for binding WW domains. PXY1 is required to promote transactivation of beta-globin and for hyperacetylation of histone H3, but not for binding to the HS2 promoter site (By similarity).
Subcellular Location: Nucleus
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Q6AYT2 | MPPCPPQPNRNRLPQLPTGELGEMELTWQEIMSITELQGLNVPSEPSFEPQAPTPYPGPLPPPTYCPCSIHPDAGFTLPPPPYELPASTPHAPDLPYSYGNIAIPVSKPLTLSGLLNEPLPDPLALLDIGLPVGQPKPQEDPESDSGLSLNYSDAESLELEGTEAGRRRSEYVDMYPVEYPYSLMPNSLAHPNYTLPPTETPLVLESSSGPVRAKPAVRGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLAQYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLGSERERLLRARGEADRTLEVMRQQLTELYHDIFQHLRDESGNSYSPEEYVLQQAADGAIFLVPRGTKMEATD | Function: Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron (By similarity).
PTM: Phosphorylated on serine residues. In undifferentiated erythrocytes, phosphorylated by MAPK8 which then leads to ubiquitination and protein degradation.
Sequence Mass (Da): 41496
Sequence Length: 373
Domain: The PXY motifs are required for binding WW domains. PXY1 is required to promote transactivation of beta-globin and for hyperacetylation of histone H3, but not for binding to the HS2 promoter site.
Subcellular Location: Nucleus
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Q86UQ8 | MPRVVCWHTLKSLNGYKNLSSGAETREGLRSSSPVDLPLRPRKQATAAGQRKLLSLQLLLCACTSVTDLTYWGPAGHGATAPHRSLLAIHLHLVPASSAAMKATGPHNAQTQVNPQGHAPSAEDPTGTWTVSGPCKDHPHPFLSQSNPPTRISSALPLKTDSALEQTPQQLPSLHLSQG | Function: Functions as part of the SSP (stage selector protein) complex, a complex that contributes to the preferential expression of the gamma-gene in fetal erythroid cells by facilitating the interaction of the gamma-globin genes with enhancer elements contained in the locus control region (LCR). The complex binds to the stage selector element (SSE) in the proximal gamma-globin promoter. In contrast, isoform 2 acts as a repressor of gamma-globin gene expression by preventing NFE2 and RNA polymerase II recruitment to the promoter.
PTM: Acetylation at Lys-43 prolongs the protein half-life by preventing ubiquitin-mediated degradation and reduces the interaction between NF-E4 and HDAC1, potentially maximizing the activating ability of the factor at the gamma-promoter.
Sequence Mass (Da): 19019
Sequence Length: 179
Subcellular Location: Nucleus
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O32077 | MELFGVPIQTMYLYTLIIAGSLTLLFLFFGDVFSGLSEGIPFLNPTLVLSFFTCFSAGGYIGELVLPLSSLLIALLSCILSIMLVVLLHIFVLVPLSSAEESLAYREDDLRGRLGKVITAVPVDGFGEVVIEGIGGTISKSAVSFDNQQISYGTTVLVVDINNGVLSVTPHEPI | Function: Plays a role in assembly of FloT membrane rafts, probably recruited to rafts by FloT.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18604
Sequence Length: 174
Subcellular Location: Cell membrane
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P12037 | MRGAVLRLGAARGQLRLEQEHLLEDIAHVRQRLDDEARQRQEAEAAARALARFAQEAEAARVELQKKAQALQEECGYLRRHHQEEAQAEARDALKCDVTSALREIRAQLEGHAVQSTLQQEEWFRVRLDRLSEAAKVNTDAM | Function: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. NEFH has an important function in mature axons that is not subserved by the two smaller NF proteins. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity).
PTM: There are a number of repeats of the tripeptide K-S-P, NFH is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFH results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.
Sequence Mass (Da): 16204
Sequence Length: 142
Subcellular Location: Cytoplasm
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Q54X04 | MNRSILKFVKNGIISSSSRINNNGFINKNNNNRWFATLPQPNRGIAGEKQPIYLDMQSTTPIDPRVLDAMLPLYTENYGNPHSKTHAYGWTSNDLVEDAREKVSKIIGADSKEIIFTSGATESGNIAIKGVARFYKEKKNHIITTVTEHKCILDSCRHLEMEGFKVTYLPVGENGLVDLELLKNTITPQTSLVTIMAVNNEIGVVQPIKEIGKICRENGVFFHTDAAQAVGKIPIDVNDMNIDLLSISGHKIYGPKGVGALFVRRRPRVRIEPITTGGGQERGIRSGTVPSTLAVGLGAACDIALKEMNHDAAWVKYLYDRLLKGITDNIPNVKVNGDLNARYYGNLNISFSYVEGESLLMAIKDVACSSGSACTSSSLEPSYVLRSLGVEEDMAHSSIRFGIGRFTTEQEIDYTIEILKKNVQRLRDMSPLWEMVQEGIDIKTIEWSQI | Function: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters (By similarity).
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 49853
Sequence Length: 450
Subcellular Location: Mitochondrion
EC: 2.8.1.7
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Q8SQS2 | MIGGLKSCIEQPSLPKPSTLLPQDKACDTGGKRIFLDVQSTTPVDPRVLDAMLPFYTTVFGNPHSRTHRYGWQAEAAVEKARSQVASLIGCDPKEIIFTSGATESNNLALKGVSGFKLKEGKAAHIITLQTEHKCILDTCRNLEENGVEVTYLPVGNDGVVDIDDVKKSIKENTVLVSIGAVNSEIGTVQPLKEIGMLCKERGVLFHTDAAQGVGKIQIDVNEMNIDLLSMCAHKIYGPKGIGALYVRRRPRVRMVPLINGGGQERGLRSGTVASPLVVGFGKAAEICSKEMKRDFEHIKELSKKLKNMFKKNIEGVIINGSEKGFPGCVNVSFPFVEGESLLMHLKDIALSSGSACTSASLEPSYVLRALGRDDELAHSSIRFGIGRFTMAKEIDIVANKTVEAVQKLREMSPLYEMVKEGIDLSKISWTS | Function: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters in mitosomes.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 47016
Sequence Length: 432
Subcellular Location: Mitosome
EC: 2.8.1.7
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Q9Y697 | MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH | Function: Cysteine desulfurase, of the core iron-sulfur cluster (ISC) assembly complex, that catalyzes the desulfuration of L-cysteine to L-alanine, as component of the cysteine desulfurase complex, leading to the formation of a cysteine persulfide intermediate at the active site cysteine residue and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU . The persulfide is then transferred on the flexible Cys loop from the catalytic site of NFS1 to the surface of NFS1 . After the NFS1-linked persulfide sulfur is transferred to one of the conserved Cys residues of the scaffold, a reaction assisted by FXN (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity).
PTM: N-gluconoylated.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 50196
Sequence Length: 457
Subcellular Location: Mitochondrion
EC: 2.8.1.7
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O74351 | MSKMGSLMLSRARCLLELRSALFFVKRESQDINNVRQSLGVYGRSFMTSSRMDKPSMSNKPREQMYGLGNMTAVQEPIPENSLKTVTLDQAQTAASTVTGLHPIYMDFQATSPLDYRVLDSMLPFFTGIYGNPHSRTHAYGWEAEKAVENARQEIASVINADPREIIFTSGATESNNAILKGVARFYKSRKKHLVSVQTEHKCVLDSLRALQEEGFEVTFLPVQTNGLINLDELRDAIRPDTVCVSVMAVNNEIGVCQPLEEIGKICRQKKVFFHSDAAQGYGKIDIDVNRMNIDLMSISAHKIYGPKGIGAAYVRRRPRVRLEPLISGGGQERGLRSGTLAPSQVVGFGTAARICKEEMKYDYAHISKLSQRLIDGLLAIPYTSLNGDPKSRYPGCVNISFNYVEGESLLMGLKNIALSSGSACTSASLEPSYVLRAIGQSDENAHSSIRFGIGRFTTEAEIDYAIENVSRQVSFLRNMSPLWDLVQEGVDLSTIEWSQH | Function: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Plays a role in both tRNA-processing and mitochondrial metabolism. Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 55543
Sequence Length: 501
Subcellular Location: Mitochondrion
EC: 2.8.1.7
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B0YLW6 | MPLPNQIATSNVETKNFASLKRSDEPIAIAQASRTPAKIYFDFQATTPVDPRVLDAMLPYFTKKYGNPHSRTHSFGWESEKAVETARKQVADLIGAHEKEIIFTSGATESNNLAIKGAVDWKAQDGNPVHVITTQVEHKCVLDSMRFLEEKGARVTYMKVNKDGVIDLEELKRSISDDTVLVSIMGVNNEIGTVQPLEEIGKICKERNVLFHCDAAQMFGKLKIDVNKMNIDLLSISGHKIYGPKGVGALYVRRRPRVRLVPLFSGGGQERGLRSGTLPTPLIVGLGKAAAVCQEEMQRDLSWIESLSKKLYTCLKENIPNVIKNGSLQTNPLRWFPGCLNLSFPHVEGEGLLMALKNIALSSGSACTSASLEPSYVLRALGNDDELAHSSIRFGIGRFTTPCEIKEVAKQTTSAVKKLRDMSPLYEMEQEGIDLKTIKWT | Function: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters in mitosomes.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 48744
Sequence Length: 441
Subcellular Location: Mitosome
EC: 2.8.1.7
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P25374 | MLKSTATRSITRLSQVYNVPAATYRACLVSRRFYSPPAAGVKLDDNFSLETHTDIQAAAKAQASARASASGTTPDAVVASGSTAMSHAYQENTGFGTRPIYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLKGVPRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKEIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERGLRSGTLAPPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGCVNVSFAYVEGESLLMALRDIALSSGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELSPLWEMVQEGIDLNSIKWSGH | Function: Catalyzes the removal of elemental sulfur from cysteine to produce alanine . It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters . Plays a role in both tRNA-processing and mitochondrial metabolism . Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs .
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Mass (Da): 54467
Sequence Length: 497
Domain: the N-terminal beta-strand formed by residues 99-104 is essential for the function.
Subcellular Location: Mitochondrion
EC: 2.8.1.7
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P17117 | MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR | Cofactor: Binds 1 FMN per monomer.
Function: Catalyzes the reduction of nitroaromatic compounds using NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major oxygen-insensitive nitroreductase in E.coli.
Sequence Mass (Da): 26801
Sequence Length: 240
EC: 1.-.-.-
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P38489 | MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV | Function: Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.
Catalytic Activity: 5,6,7,8-tetrahydropteridine + NAD(+) = 6,7-dihydropteridine + H(+) + NADH
Sequence Mass (Da): 23905
Sequence Length: 217
EC: 1.-.-.-
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A1DN30 | MEVWEHSRPIADDTIKKTPSFTTLPIRINKQNDVADAATRRALRDWDYYLHDGLAERALISISELGNLGAFAYPEVPPERLAIVTYLTDLGILHDDGYEAMDMDQARTEHREFGALFDPHEQLPSRRGTRAAKLKKLVSQILLEAIRIDRDMGMYMFDMYNKGWLSVAGGEGKVPQFKSVEEYQAYRRDDFGIRAFWPMVEFGMAMRLSDEDKKLIEPVMEPIDKAIIWTNDYWSFDREYHESITNGSRLTNVVEVVRQIENKSIDEAKAAVRQLLVNLEQQYLERKRAIYAQNPSIPSHLRKWIEVVGITVAGTHFWASCSPRHHAWRNNSRNGLKPANHVAAPTLITPSNNLNSSKGSEEQMQDSDNGTRTQMCPANDHEVMQLNAKLSLGKQDGGHAMRAALALLSRAAEQCESLFDGMEHERARLLQSGEEKARLSWEGRSKGSQELEHSWYKPAKTALQAPIHYICSMPSKGVRSRMIEAFNYWLEVDETSLTKIRRLVDLLHNASLILDDIEDHSPKRRGRPATHTIFGHSQAINSANFMFVQAVQVARQFRNPNAVDILLEELENLYLGQSWDLDWKYKLRCPSPSEYLNMVDNKTGGLFRLLLRLMQAERKGTTEVDLDGLTVLFGRFFQIRDDYMNLRSGLYTEQKGFCEDLDEGKFSYPIVVCVANHADFRDLIDGVFRQRPTAITSGMQPLAPEIKRYVVEYLNTSGTFQHCREFLMQLESLIESEIDRIEKVTNEANPMLRLLLEKLSVKEN | Function: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of sesterfisheric acid . The bifunctional terpene synthase NfSS converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into sesterfisherol . The C-terminal prenyltransferase (PT) domain of NfSS catalyzes formation of geranylfarnesyl pyrophosphate (GFPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP to sesterfisherol . The cyotochrome P450 monooxygenase NfP450 then catalyzes oxidative modifications of sesterfisherol into sesterfisheric acid .
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate
Sequence Mass (Da): 87565
Sequence Length: 764
Domain: The conserved DDXXD motifs as well as the NSE/DTE motif are important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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Q06204 | MTIESTLARELESLILPADSIVNVVDQFQEELLSRLQTNTISMLPQCLVPDKRSRWNPEDKILTIDFGGTRLKFAIISLPQIVIEYNDAFELTYNIVDSNFFNQIIYTICTRLAANGYIKKKNESSEASKFFVSVTFSFPLNPEGEVVAMGKGFVMTDTLQGSTVKQLIQSSFHRIISENIEEFFCTMNVCHVINDAIAVSLTSKFICENDSISLIIGTGTNACFEVPYGYLPPFKRDALRETLPSSYNKETLNFKHVLINSEIGFIGKNVIALQPFDIHGAISYEMPLECVTSGKWLPLSLKNILLQYNIIPKNFPVEFNGELVCQLAEDCTNAWFENEHYALICQIARLLIKRAAFYVAAIVQAIDIITGCKNYNFIHIGYVGSFLHNSNFYREQIKYYSSIHIKLQFLNHSNLLGAAIATYLNKSDNQVQ | Function: N-acetylglucosamine (GlcNAc) kinase that transfers a phosphate onto GlcNAc to generate GlcNAc-6-phosphate, which can be a precursor for glycan synthesis . Can utilize a broad range of NTPs, namely ATP, CTP, GTP, ITP, and UTP, as phosphoryl donors . Shows only low glucose phosphorylation activity . NGK1 may play a role under a certain condition as an alternative supply pathway GlcNAc-6-P as a precursor of UDP-GlcNAc (Probable).
Catalytic Activity: ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 48969
Sequence Length: 433
EC: 2.7.1.59
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Q03264 | MTQDKEVKVVAPDVAPDQEVEINKSVKDAKHQTNDDSLLQHKKKGKKGKKSKPIVTPEHIAKVRAEREVMRKAKRDAMLAQGVDPDCPPELHFIRRPFLSLHEAEPVTGFRFKLMTYNCLAQALIRRKLFPDSGDALKWYRRSKVLLNEFKYYNSDVICLQEIDHIQFQSFWKDEFSKLGYDGQYYRNATKNHGVAIMWRRELFHQVDKMLIDYDKESSESISTRTTTNNVGLVLALKFSEKVLSNLGKKSSKKCGILIGTTHLFWHPFGTYERTRQCYIVLKKMKEFMHRVNVLQNENDGDLSHWFPFFCGDFNSQPFDTPYLSMTSKPVHYRNRAKTVIGCSTSYKFSKVRDGEEGADDEEGGNIEKYGKDQPESPVPEKFHANEEQSELVDKMAQLHNSLDMRAISLYSVGYKNVHPENAGLDNDRGEPEISNWANTWRGLLDYLFYVKKWDPQSNCQEVETLGDFEKENKVKCRGFLRMPPGNEMTKHGQPHVGEYASDHLSMVCDLELQL | Function: Involved in pre-rRNA processing. Required for the final stage of 3'-end maturation of 5.8S rRNA at site E.
Sequence Mass (Da): 59540
Sequence Length: 515
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q9TW67 | MPVTEVGSLPELNNILERSDANRLIIIDFFANWCGPCRMISPIFEQFSAEYGNATFLKVNCDVARDIVQRYNISAMPTFIFLKNRQQVDMVRGANQQAIAEKIRQHYSPTPANPNAASDSEKRFLEQFVKCSNVPRSYQDEVFKALARSVMPEELVGRAMTEGPRDEKAILKDLLHWFKTQFFTWFDRPTCPKCTLKCSTDGLQGTPTREEQKEGGASRVEVYICDGCNTEMRFPRYNNPAKLLQTRTGRCGEWANCFGLLLAALNLESRFIYDTTDHVWNEVYLLAEQRWCHVDPCENTMDRPLLYTRGWGKTLGYCIGYGSDHVVDVTWRYIWDSKKLVTQRNEVRQPVFENFLSKLNSRQAEGQTEPRKRELAVRRVCELMEMMAQEAKNHKIGWEKIGDDLGGRITGSEEWRRERGELGESGPKLLAEPIKLAPPTGPAQNYLEFNYDVITDTYSQPPEIGFSAQAFELENVQRVEETDWNMTYLCRKRGDAPGNISWHFDLKSLKKSIEKIEIRMAGIQKFEKGKAMAIACLGDSCMRLPIDCSALTIEDPKNAEILKITATLSGGEGAIGFQQAQIFRTELKRGGGARTESFSVKIWMKN | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation . Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp . Prefers proteins containing high-mannose over those bearing complex type oligosaccharides . Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins . Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins . Also displays oxidoreductase (thioredoxin) activity . Involved in regulating the expression of proteasomal subunits such as rpt-3 in order to confer resistance to proteasomal dysfunction .
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 69148
Sequence Length: 606
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q5ZJM3 | MAGSAGLSSSPSSPAVRELCKNARDTFLEASRLLLTYADNILRNPYEEKYRSIRNGNPAFSTRLLPVRGAVECLFEMGFQEGETHMVFPKEASIEQLRKVRDLIAVERSSRLNESNQVHRSASSETVAITQAIAHQPSRPAGSVPTPDHQQPEPSLLQSLKMAADILTTLQSKCDHLILAYESTSLQQKALALIPLQQLKEKAQRKLAQATRLDKGEHVNEEDFLLLELLNWFKNDFFHWVDNLPCSRCGGQTEGKRDYLSPTDDDLRWNADRVENHYCSQCQFCNRFPRYNNPEKLLETRRGRCGEWANCFTLCCRAVGFEARYVRDWTDHVWTEVYSASQKRWLHCDPCENVCDKPLLYEIGWGKKLSYVIAFSKDEVVDVTWRYSCKHQEVLTRRTALSEAKLRETINAINKKKQQSLSEGRRKELLERTIVELAEFISPKTPKPGEFGGRTSGSMAWRIARGETGSEERKEVIFIPSEKEKASKLFHLMYNVVEDSYTRISNNNEQITGWGTGIWKAESIARKVETDWKMVYLARKEGSSSASISWKFECKSVGLKIDNISIRTSSQTFHSGRIKWRLYSPTAEVILVGDNSLSSYSDFCGATEVTLEATLSGGDGKAAWQHTQLFRNSLAGCGENCLEMIIKLADL | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 73903
Sequence Length: 651
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q503I8 | MPGSQGVLALCENTTEVFLDVSKLLITYADNILRNPNEEKYRSIRIGNPTFSTKLLPVKGAVECLFEMGFEEAETHLVFPRSASVEKLRQVRETIAAERDQRLGASNTASSPQNASVPPVPAPPPSLSSTASAGPAAAAVPTPAPASIPFTSSSATFQRTVQSNFQHVLVYEDPELQQKALECIPHELLRSRAKERLKQANDADAACSLGEEDMLVLDLLQWFKSDFFSWVDNLPCIQCGGKTQPSGSLSPSSDDLHWDAGRVENHFCHTCQLSTRFPRYNNPEKLLETRKGRCGEWANCFTLLCRALGLEARYIWDSTDHVWTEVYSQSQRRWIHCDPCENACDKPLLYEVGWGKKLSYILAFSKDQVADVTWRYSCKHPEVLSRRTQVQETWLLHMLNKLNAERQQFLGAERKQQLLQRLLVELVEFISPKSPQPGELGGRMSGSLAWRAARGETGASNAKEDTQENVFTPSESEKESKRFHICYNVTKDCYYRVSNGQETIQGWQKGAWRTENMFRKEEHDWQMVYLARTEGASFGRMSWKFNCAPAGMKMKSASVRVFSQTFHSGTVRWSLSTNETTTEFPGDGELHSFSNVSGGTELIVEAELTGGDGSTSWQHAQLFRQSLKDTEKVLFEVMVEMEKS | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 72489
Sequence Length: 644
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q7KRR5 | MVDINLECVHQIEPKTRSAGQQQQERGLKEAYLEAVRILLVLLENILAQPENSMFRTIRQENKAIKEKLLSLPGCERLLEAIGFVRAPSSNAYTLPTEVSLQQVKKYRDALSERRTAWLNGTVSKSPPQQSTTSTTPLFIKPSVEYRHRIAFPRVLRTNNNFLQSLELYSDAVMQYEDNLLLATGRTLIPVEELTEMASEKLIDIQDQIASGERQEKEPCVRDLLLVELVNWFNTQFFQWVNNIPCRVCGSEESRLRRTEREGDIRVEVTVCCGQESKFYRYNDISQLLVSRKGRCGEYANCFTFLCRALDYDARIVHSHFDHVWTEVYSEAQMRWLHVDPSENVIDSPLMYQHGWKRHIDYILAYSRDDIQDVTWRYTNDHQKILHLRKLCGEKEMVQTLDAIRAKRRQNCTADRKLFLSQRNMYEVIGLTLERKPTENELKGRSSGSLSWRQSRGEHTFTNIFVFNLSATELQKRQLNVRYSCATDTYERYAKEGEHITILDSYKTWQKAQFSSKNIFRKVERDWKMAYLARLEDTDCGEIAWTFDFSKTNLKVKSYNLVFETKTFGDGKISVTVDATDGSASVENATGFKIVAKLTGGKGDVAWQHTQLFRQSLNSRDYPFDLQVQLH | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 73316
Sequence Length: 631
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q96IV0 | MAAAALGSSSGSASPAVAELCQNTPETFLEASKLLLTYADNILRNPNDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIERSSRLDGSNKSHKVKSSQQPAASTQLPTTPSSNPSGLNQHTRNRQGQSSDPPSASTVAADSAILEVLQSNIQHVLVYENPALQEKALACIPVQELKRKSQEKLSRARKLDKGINISDEDFLLLELLHWFKEEFFHWVNNVLCSKCGGQTRSRDRSLLPSDDELKWGAKEVEDHYCDACQFSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRAVGFEARYVWDYTDHVWTEVYSPSQQRWLHCDACEDVCDKPLLYEIGWGKKLSYVIAFSKDEVVDVTWRYSCKHEEVIARRTKVKEALLRDTINGLNKQRQLFLSENRRKELLQRIIVELVEFISPKTPKPGELGGRISGSVAWRVARGEMGLQRKETLFIPCENEKISKQLHLCYNIVKDRYVRVSNNNQTISGWENGVWKMESIFRKVETDWHMVYLARKEGSSFAYISWKFECGSVGLKVDSISIRTSSQTFQTGTVEWKLRSDTAQVELTGDNSLHSYADFSGATEVILEAELSRGDGDVAWQHTQLFRQSLNDHEENCLEIIIKFSDL | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 74390
Sequence Length: 654
Domain: The PUB domain mediates the interaction with VCP.
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q9JI78 | MASATLGSSSSSASPAVAELCQNTPETFLEASKLLLTYADNILRNPSDEKYRSIRIGNTAFSTRLLPVRGAVECLFEMGFEEGETHLIFPKKASVEQLQKIRDLIAIERSSRLDGSSKKVQFSQHPAAAKLPLEQSEDPAGLIRHSGNQTGQLPSLPSAPMVVGDSTILKVLQSNIQHVQLYENPVLQEKALTCIPVSELKRKAQEKLFRARKLDKGTNVSDEDFLLLELLHWFKEEFFRWVNNIVCSKCGGETRSRDEALLPNDDELKWGAKNVENHYCDACQLSNRFPRYNNPEKLLETRCGRCGEWANCFTLCCRALGFEARYVWDYTDHVWTEVYSPSQQRWLHCDACEDVCDKPLLYEIGWGKKLSYIIAFSKDEVVDVTWRYSCKHDEVMSRRTKVKEELLRETINGLNKQRQLSLSESRRKELLQRIIVELVEFISPKTPRPGELGGRVSGSLAWRVARGETGLERKEILFIPSENEKISKQFHLRYDIVRDRYIRVSDNNINISGWENGVWKMESIFRKVEKDWNMVYLARKEGSSFAYISWKFECGSAGLKVDTVSIRTSSQSFESGSVRWKLRSETAQVNLLGDKNLRSYNDFSGATEVTLEAELSRGDGDVAWQHTQLFRQSLNDSGENGLEIIITFNDL | Cofactor: Binds 1 zinc ion per subunit.
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins.
Catalytic Activity: Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.
Sequence Mass (Da): 74275
Sequence Length: 651
Domain: The PUB domain mediates the interaction with VCP.
Subcellular Location: Cytoplasm
EC: 3.5.1.52
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Q2NVY9 | MIAASLRRMITHPAAGGVLLFAAALAAIVMANTDARALYNAIIYFPAQSASATPSHLSLLVLVNDGLMAVFFLAVGLEVKYELLQGALNSRVRAAFPAIAALGGMVAPAVIYSLMTAGTPALRAGWAIPAATDIAFAVGVLALLGTRVPVSLKVFMLALAIIDDLGAIVIIALFYNTALEPLALAAAGAVIGIMALMNRANVRFLSLYLLLGAVLWGCILLSGIHATLAGVVVGGLIPLTLPSTEVSPARALEHWLQPWVVYLILPLFAFANAGISLQGVAPGHLISFLPLGIAAGLVVGKPLGIVLFTAVAVKLRLARLPAGIAFRHIAAAAMLCGIGFTMSIFIANLAFGHDDPETIVLAKVGILSGSVIAALLGYLLLRAILPQPQGSGSVPVGG | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40831
Sequence Length: 398
Subcellular Location: Cell inner membrane
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Q1GVK1 | MARSFPPPSALRDFLESESAGGILLIFAAILAMIVANSPLATLYHDLIHAVTGPVLTDKLGPMTVHLWINDGLMAVFFLLVGLEIKREFVDGRLASWDRRRLPFIAAAAGMAVPAALYMFFVGDEPGLAQGWAIPAATDIAFAMGVLALLGRRAPTSLKLFLVTVAIVDDMGAVAIIALFYTAKINLLALGAAAAILGIMFACNRGGVKNLLVYMALFLLLWYAMLLSGVHATIAGVLAAMAIPFERTPGAPDSQTSPLHRLEHALHPTVAFAIVPLFGFANAGVDVRALGLDQLFAPLPLGIAAGLFLGKQIGIFGSVWLAVKLGIAGRLRGATWLQVYAVSMLCGIGFTMSLFIGSLAFPGNALLIEEAKIGILMGSLASALVGFAVLRLAPLHPEHNAVESASKGEIAVDGDVRDTSEAAR | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44573
Sequence Length: 424
Subcellular Location: Cell inner membrane
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Q93F90 | MAAPRTPNTARKVLGRLSLPERTFVADALRTETVGGVLLLVATVTALVWANIPALQHSYEAVSHFHFGPSALGLNLSVAHWAADGLLAVFFFVAGIELKRELVAGDLRDPRAAVLPVVAALCGMAVPALVYTLTNLTGHGSTQGWAVPTATDIAFALAVLAVIGTSLPSALRAFLLTLAVVDDLFAILIIAIFFTERINFAALGGAVAGLAVFWLLLRKGVRGWYVYVPLAVVVWALMYNSGVHATIAGVAMGLMLRCTTREGEEHSPGEHIEHLVRPLSAGLAVPLFALFSAGVVVSGGALGDVFTEPETLGVVLGLVVGKTLGIFGSTWLTARFTHAELSEDLEWADIFAVASLAGIGFTVSLLIGELAFAGDTLLTDEVKAAVLTGSLIAALCATVLLKIRNARYRGLCEDEERDEDRDGIPDVYEQDDPAYHLRMADIFERKAAEHRRIAAEKAAAARHGGAEVPGGAGEEDGRPA | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50682
Sequence Length: 480
Subcellular Location: Cell membrane
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Q82EL6 | MAAPRTSTRKFLGRLSLPERNFVAEALRTETVGGVLLLLAAITALIWANVPALHHSYESVSHFHFGPAPLGLDLSVQHWAADGLLAVFFFVAGIELKRELVAGDLKDPKAAALPVAAALCGMAVPALVYTLTNLTGGGSLRGWAVPTATDIAFALAVLAVIGTSLPSALRAFLLTLAVVDDLFAILIIAVFFTADLNFAALAGAVIGLAVFWLLLRKGVRGWYVYVPLALVIWGLMYNSGIHATIAGVAMGLMLRCHRHQGEEHAPGEHIEHLVRPLSAGLAVPLFALFSAGVVISGGALGDVFTRPETLGVVLGLVVGKAIGIFGGTWLTARFTRASLSDDLAWPDVFAVASLAGIGFTVSLLIGELAFDGDPVLTDEVKAAVLTGSLLAALIATTLLKLRNAKYRALCEDEERDEDSDGIPDIYEQDNPAYHLRMAEIYERKAAEHRRLAEVTGGAGAENDGPA | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49235
Sequence Length: 466
Subcellular Location: Cell membrane
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Q30PM3 | MKLYAPWQRAFEKIATPFEQFLHAQTTTGLMLMLMTVVALLLANSPLSDEYLHIFHTNIDIFVGNYGFSKSIHHWINDGLMAIFFFIIGLEIKRNILVGELSNIKVAMLPILAAIGGMALPALIYYAINYGDIGEAGWGIPMATDIAFAISALVLLGRRVSASLVTFLVALAIVDDLGAVVVIALFYTQEINMLPLLFAFISFLVLVSFNRFGIHAILPYFVVGFIMWLFMLESGIHATVAGVIAAMAIPSRPKYTPMDFTKSVKSRLDEYDNYPIEDNYMLHEQQKAILQNVKDKIDAISSPSARLEHSLHLPVSLVVIPLFALANAGVSINFSSAYDTLLQPISLGVMAGLVFGKVFGIAGISYLAIKLGIAKLPEGSTMSQVFGVAFLGGIGFTMSIFIAELAFAGNSELVFQAKIGILAASLFAGIFGFIWLRFIAKSAN | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48397
Sequence Length: 444
Subcellular Location: Cell inner membrane
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A0LLE6 | MGRSSARDGQMPLRDIMDKKKRKNEYALERLFGRILSPFEAFLKRTTAGGIVLMGTTVLTLIAANSAWGDAFLRFWEQRVRFGIGSLQLEMSLHDLINDGLMSLFFLVVGLELKREMKVGELSSWRDAALPVFAAAGGMVVPALVYFAVNPHGTAAAGWGIPMATDIAFAVGILVLLSWRIPPGLIIFLTALAIADDLGAVLVIALFYTHEISLGAIGFASAVLFLLLLLNRGGIRHAIPYGVLGVLLWMALHHSGVHSTLAGVLLAFTIPARPARAPAEFEQRLVELQNAFHAEAAAPDFVDQPLSNPRMATIAETLERNSRAVQSPLQRMEHRLGPWVTFIVIPLFALNNVGIDFEKIALLQGLCEPVTMGVCLGLVFGKFTGISVFSWIAVRLGIGRLPSEVRWRHLLGVAWLGGIGFTMSLFISQLAFDDRLLQEQAKLGILTASLLSAMIGMTWLYFGGTRARPNPE | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51493
Sequence Length: 472
Subcellular Location: Cell inner membrane
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Q9JJ40 | MASTFNPRECKLSKKEGQNYGFFLRIEKDTDGHLVRVIEEGSPAEKAGLLDGDRVLRINGVFVDKEEHAQVVDLVRKSGNSVTLLVLDGDSYEKAVKHQVDLKELDQSPREPALNEKKPDLGMNGGVETCAQPRLCYLVKEGNSFGFSLKTIQGKKGVFLTDITPQGVAMKAGVLADDHLIEVNGENVENASHEEVVEKVTKSGSRIMFLLVDKETARCHSEQKTPFKRETASLKLLPHQPRVVVIKKGSNGYGFYLRAGPEQKGQIIKDIEPGSPAEAAGLKNNDLVVAVNGESVEALDHDGVVEMIRNGGDQTTLLVLDKEADRIYSLARFSPLLYCQSQELPNGSVKEAPAPISAPLEAPGSATTEDVGDHKPKLCRLIKEDDSYGFHLNAIRGQPGSFVKEVQQGGPADKAGLENEDIIIEVNGENVQDEPYDRVVERIKSSGEHVTLLVCGKVAYSYFQAKKIPILSSLADPLVAGPDAKGETEHDSAESTKDSSHPARDRTLSAASHSSSNSEDTVM | Function: A scaffold protein that connects plasma membrane proteins and regulatory components, regulating their surface expression in epithelial cells apical domains. May be involved in the coordination of a diverse range of regulatory processes for ion transport and second messenger cascades. In complex with NHERF1, may cluster proteins that are functionally dependent in a mutual fashion and modulate the trafficking and the activity of the associated membrane proteins. May play a role in the cellular mechanisms associated with multidrug resistance through its interaction with ABCC2 and PDZK1IP1. May potentiate the CFTR chloride channel activity (By similarity). Required for normal cell-surface expression of SCARB1. Plays a role in maintaining normal plasma cholesterol levels via its effects on SCARB1. Plays a role in the normal localization and function of the chloride-anion exchanger SLC26A6 to the plasma membrane in the brush border of the proximal tubule of the kidney. May be involved in the regulation of proximal tubular Na(+)-dependent inorganic phosphate cotransport therefore playing an important role in tubule function (By similarity). Component of a complex, composed of PDZK1, SYNGAP1, KLHL17 and NMDA receptors. Interacts (via PDZ1 domain) directly with KLHL17; the interaction is important for integrity of actin cytoskeleton structures in neurons.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56800
Sequence Length: 523
Domain: The PDZ 2 and 3 domains seem to be involved in the interaction with SLC26A3.
Subcellular Location: Membrane
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Q86UT5 | MVTPSPPGNHSLSLEAPRLHTASDLLGNHSLGLPLITALVGSRDRRGRVFSPVPVPLPTNPTTQHPTRQKLPSTLSGHRVCQAHGEPVLGLCPLLPLFCCPPHPPDPWSLERPRFCLLSKEEGKSFGFHLQQELGRAGHVVCRVDPGTSAQRQGLQEGDRILAVNNDVVEHEDYAVVVRRIRASSPRVLLTVLARHAHDVARAQLGEDAHLCPTLGPGVRPRLCHIVKDEGGFGFSVTHGNQGPFWLVLSTGGAAERAGVPPGARLLEVNGVSVEKFTHNQLTRKLWQSGQQVTLLVAGPEVEEQCRQLGLPLAAPLAEGWALPTKPRCLHLEKGPQGFGFLLREEKGLDGRPGQFLWEVDPGLPAKKAGMQAGDRLVAVAGESVEGLGHEETVSRIQGQGSCVSLTVVDPEADRFFSMVRLSPLLFLENTEAPASPRGSSSASLVETEDPSLEDTSVPSVPLGSRQCFLYPGPGGSYGFRLSCVASGPRLFISQVTPGGSAARAGLQVGDVILEVNGYPVGGQNDLERLQQLPEAEPPLCLKLAARSLRGLEAWIPPGAAEDWALASDLL | Function: Acts as a regulatory protein that associates with GUCY2C and negatively modulates its heat-stable enterotoxin-mediated activation . Stimulates SLC9A3 activity in the presence of elevated calcium ions .
PTM: Phosphorylation at Ser-395 negatively regulates its interaction with SLC26A3.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 61032
Sequence Length: 571
Subcellular Location: Cell membrane
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Q99MJ6 | MEAAADLRDTALLTLKFKFNPRLGIDNPVLSLAEDQDQSDPWNLHRPRFCLLSKEEEKTFGFHLQQHLGKADHVVCRVDPGTSAQRQGLREGDRILAVNNNIVAHEDHAVVVRYIRASGPRVLLTVLAQHVHDVARVLQGSDAFLCPTLPSGVRPRLCHVVKDEGGFGFSVTHGSRGPFWLVLSAGGAAERAGVPPGARLLEVNGASVEKLTYNQLNRKLWQSGDQVTLLVAGLEVEEQCHQLGMPLAAPLAEGWALPAKPRCLNIEKGPEGFGFLLREEKGLDGRLGQFLWDVDPGLPADKAGMKAGDRLVAVAGESVDGLGHEETVSRIRAQGSCVSLIVVDPEADRFFSMVRLSPLLFLENTEIAAPPLAETKDLPVEDTVEPSGLAGSCQCFLYPGPGGGYGFRLCCVASGPCLFISQVTPGGSTARAGLQVGDTVLEVNGYPVGGDSELDRLQQLTEAEPPLCLKLGARNPQGLEAWISLESGEDWTLASELL | Function: Acts as a regulatory protein that associates with GUCY2C and negatively modulates its heat-stable enterotoxin-mediated activation (By similarity). Stimulates SLC9A3 activity in the presence of elevated calcium ions (By similarity).
PTM: Phosphorylation at Ser-329 negatively regulates its interaction with SLC26A3.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53525
Sequence Length: 498
Subcellular Location: Cell membrane
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Q68KI4 | MLDSLVSKLPSLSTSDHASVVALNLFVALLCACIVLGHLLEENRWMNESITALLIGLGTGVTILLISKGKSSHLLVFSEDLFFIYLLPPIIFNAGFQVKKKQFFRNFVTIMLFGAVGTIISCTIISLGVTQFFKKLDIGTFDLGDYLAIGAIFAATDSVCTLQVLNQDETPLLYSLVFGEGVVNDATSVVVFNAIQSFDLTHLNHEAAFHLLGNFLYLFLLSTLLGAATGLISAYVIKKLYFGRHSTDREVALMMLMAYLSYMLAELFDLSGILTVFFCGIVMSHYTWHNVTESSRITTKHTFATLSFLAETFIFLYVGMDALDIDKWRSVSDTPGTSIAVSSILMGLVMVGRAAFVFPLSFLSNLAKKNQSEKINFNMQVVIWWSGLMRGAVSMALAYNKFTRAGHTDVRGNAIMITSTITVCLFSTVVFGMLTKPLISYLLPHQNATTSMLSDDNTPKSIHIPLLDQDSFIEPSGNHNVPRPDSIRGFLTRPTRTVHYYWRQFDDSFMRPVFGGRGFVPFVPGSPTERNPPDLSKA | Function: Acts in low affinity electroneutral exchange of protons for cations such as Na(+) or K(+) across membranes. Can also exchange Li(+) and Cs(+) with a lower affinity. Involved in vacuolar ion compartmentalization necessary for cell volume regulation and cytoplasmic Na(+) detoxification. Required during leaves expansion, probably to stimulate epidermal cell expansion. Confers competence to grow in high salinity conditions.
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59513
Sequence Length: 538
Subcellular Location: Vacuole membrane
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Q9SXJ8 | MGMEVAAARLGALYTTSDYASVVSINLFVALLCACIVLGHLLEENRWVNESITALIIGLCTGVVILLMTKGKSSHLFVFSEDLFFIYLLPPIIFNAGFQVKKKQFFRNFMTITLFGAVGTMISFFTISIAAIAIFSRMNIGTLDVGDFLAIGAIFSATDSVCTLQVLNQDETPFLYSLVFGEGVVNDATSIVLFNALQNFDLVHIDAAVVLKFLGNFFYLFLSSTFLGVFAGLLSAYIIKKLYIGRHSTDREVALMMLMAYLSYMLAELLDLSGILTVFFCGIVMSHYTWHNVTESSRVTTKHAFATLSFIAETFLFLYVGMDALDIEKWEFASDRPGKSIGISSILLGLVLIGRAAFVFPLSFLSNLTKKAPNEKITWRQQVVIWWAGLMRGAVSIALAYNKFTRSGHTQLHGNAIMITSTITVVLFSTMVFGMMTKPLIRLLLPASGHPVTSEPSSPKSLHSPLLTSMQGSDLESTTNIVRPSSLRMLLTKPTHTVHYYWRKFDDALMRPMFGGRGFVPFSPGSPTEQSHGGR | Function: Vacuolar antiporter that acts in low affinity electroneutral exchange of protons H(+) for cations such as Na(+) or K(+) across membranes . Plays important roles in the transport of Na(+) and K(+) accumulated in the cytoplasm into vacuoles, and is involved in salt stress tolerance .
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59070
Sequence Length: 535
Subcellular Location: Vacuole membrane
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Q04121 | MLSKVLLNIAFKVLLTTAKRAVDPDDDDELLPSPDLPGSDDPIAGDPDVDLNPVTEEMFSSWALFIMLLLLISALWSSYYLTQKRIRAVHETVLSIFYGMVIGLIIRMSPGHYIQDTVTFNSSYFFNVLLPPIILNSGYELNQVNFFNNMLSILIFAIPGTFISAVVIGIILYIWTFLGLESIDISFADAMSVGATLSATDPVTILSIFNAYKVDPKLYTIIFGESLLNDAISIVMFETCQKFHGQPATFSSVFEGAGLFLMTFSVSLLIGVLIGILVALLLKHTHIRRYPQIESCLILLIAYESYFFSNGCHMSGIVSLLFCGITLKHYAYYNMSRRSQITIKYIFQLLARLSENFIFIYLGLELFTEVELVYKPLLIIVAAISICVARWCAVFPLSQFVNWIYRVKTIRSMSGITGENISVPDEIPYNYQMMTFWAGLRGAVGVALALGIQGEYKFTLLATVLVVVVLTVIIFGGTTAGMLEVLNIKTGCISEEDTSDDEFDIEAPRAINLLNGSSIQTDLGPYSDNNSPDISIDQFAVSSNKNLPNNISTTGGNTFGGLNETENTSPNPARSSMDKRNLRDKLGTIFNSDSQWFQNFDEQVLKPVFLDNVSPSLQDSATQSPADFSSQNH | Function: Endosomal/prevacuolar electroneutral Na(+)/H(+) exchanger which mediates intracellular sequestration of Na(+) cations, regulates vacuolar pH and contributes to osmotolerance following sudden exposure to hyperosmotic media. Contributes also to the postdiauxic/stationary phase resistance to osmotic stress and allows for the continued growth of cells until the acquired osmotolerance response can occur. Involved in hygromycin resistance probably through its influence on the electrochemical proton gradient affecting secondarily the entrance of hygromycin. Mediates pH-dependent vesicle trafficking out of the endosome. Contributes to K(+) sequestration and homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70148
Sequence Length: 633
Subcellular Location: Endosome membrane
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Q8T5S1 | MSLLRRPWVLVVGLLLIMSYVGAECEEEEKEYPSRYPIAYFEWENVKIPMTICLWLIGASIAKIIFNLIPHLNELFPDSALLIMIGLIIGIIFKLIGVNKNAFFLESEVFMLYLLPPLVFDAGYFMPARQFFDNFGSILCFAMIGTSFNIVAIALSLWAISLTGLFSVETPLMHMLLFGSVAADVDPVAVIVIFEELKVNEVLFIAVFGESLLNDGVAVVLYRMFLTFSEIGTENLITSDYINGGVSFLVVAFGGIGIGLLFAFLTSLVTRFARDEEVKVLNSVFILILPYTCYLCGELFGLSSIMAIVFCGAAMRQYCRENVDPDTVKATESFIKVLSLASETVIFVFLGLSTVSSNHHWDTSFIVLTVVFCLIYRTLGVVVMCYFLNKYRLNKYTKVDQFIMAYGGLRGAIAYGLVVAIPDFIPGKNMFVTSCIIVIYFTVFLQGITLKPIAEFLQVEKKNVHSKNMIEHIYSELIDTTMAGMEDIAGFKGHHWIRDSWNALNNNYLRPILVNKNNMKEMDKTKLVRKYKHLVDEDAKKIARGDLNSNMVFTKALIEHTRSRTNTMIDGVSSTSKIDFTKHMKENFGVTVYDDHSTVPMTPTHLFQETTEVEYSVRSEINDNDGFENDGYESDESGSFHERV | Function: Na(+)/H(+) antiporter that promotes normal di- or tripeptide transporter function, recovery following the peptide-induced acidification of the intestinal cytoplasm and maintenance of the peptide-dependent intestinal pH homeostasis. Regulator of free fatty acid uptake from the diet together with the dipeptide transporter pept-1. May play a timekeeper role in defecation cycle but is not necessary for pbo-4-dependent proton release. May play a role in the regulation of lifespan independent of the stress response pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72611
Sequence Length: 644
Subcellular Location: Apical cell membrane
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Q84WG1 | MVIGLSTMLEKTEALFASDHASVVSMNLFVALLCACIVLGHLLEETRWMNESITALIIGSCTGIVILLISGGKSSRILVFSEDLFFIYLLPPIIFNAGFQVKKKQFFRNFMTIMLFGAIGTLISFVIISFGAKHLFEKMNIGDLTIADYLAIGAIFSATDSVCTLQVLNQDETPLLYSLVFGEGVVNDATSVVLFNAIQRFDLTNINSAIALEFAGNFFYLFILSTALGVAAGLLSAFVIKKLYIGRHSTDREVALMMLLAYLSYMLAELFHLSSILTVFFCGIVMSHYTWHNVTDKSKVTTKHTFAAMSFLAEIFIFLYVGMDALDIEKWDVVRNSPGQSIGVSSILLGLILLGRAAFVFPLSFLSNLTKSSPDEKIDLKKQVTIWWAGLMRGAVSMALAYNQFTTSGHTKVLGNAIMITSTITVVLFSTVVFGLLTKPLVKHLQPSSKQSSTTALQITLRSSFHDPILHEPLLSTQGQSEYDPEQHVSFRMFWKSPSRFTH | Function: May act in low affinity electroneutral exchange of protons for cations such as Na(+) or K(+) across membranes. May also exchange Li(+) and Cs(+) with a lower affinity.
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55606
Sequence Length: 503
Subcellular Location: Vacuole membrane
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O16452 | MLSKLFVFLLICYATADEVDKKEAKHGFQLFHWNWDHIHKVYVITTWLLVASLAKILFNLMKPLSKWLPDSSLLIIVGLGLGYFLNQTTLSGVHLDSHAFFLYLLPPIIFDAGYFMPNRALFKNFDSVLVFSVLGTLWNTFAIGGSLLIMSKYQLFTMPFTTFEILVFSALISAVDPVAVIAIFEEIHVNEFLFINVFGEALFNDGVTVVLYQMFKSFALIGSENLSPWDYATGGLSFFVVALGGAAIGIIFAIATSLATKYTQGIKILAPVFIFLLPYMAYLTAEMVSLSSIIAIAVCGMLMKQYIKGNITEAATNSVKYFTKMLAQCSETVIFMFLGLSTLTSEHHVDFIFIGATLVFCLIYRAIGIIVQCFILNKFRAKKFEVVDQFILSYGGLRGAIAYGLVVSIPASIQAKPMFITTTICVIYFTVFLQGITIRPLVNCLNVKKKEHREATMVESVYNKYLDYMMSGVEDIAGQRGHYSFIENFERFNAKVIKPVLMRHEKRQSFDATSIIRAYEKITLEDAIKLTKVKSTLQNKRLEKVKSEVRVAPEQTTVTPKDVQLARFMQSGENIDQLYTLFSDLLDKKLNELKVQADKVDKANDDDIQDDYMAEMGSHSNLGFMHHSADQLDSDSVFQRRGRRLSTGDLKGHCGTSRKPKHSMFELRHV | Function: Plays a role in epithelial membrane transport processes.
PTM: Phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75546
Sequence Length: 670
Subcellular Location: Endomembrane system
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Q8S397 | MSIGLTEFVTNKLAAEHPQVIPISVFIAILCLCLVIGHLLEENRWVNESITAILVGAASGTVILLISKGKSSHILVFDEELFFIYLLPPIIFNAGFQVKKKKFFHNFLTIMSFGVIGVFISTVIISFGTWWLFPKLGFKGLSARDYLAIGTIFSSTDTVCTLQILHQDETPLLYSLVFGEGVVNDATSVVLFNAVQKIQFESLTGWTALQVFGNFLYLFSTSTLLGIGVGLITSFVLKTLYFGRHSTTRELAIMVLMAYLSYMLAELFSLSGILTVFFCGVLMSHYASYNVTESSRITSRHVFAMLSFIAETFIFLYVGTDALDFTKWKTSSLSFGGTLGVSGVITALVLLGRAAFVFPLSVLTNFMNRHTERNESITFKHQVIIWWAGLMRGAVSIALAFKQFTYSGVTLDPVNAAMVTNTTIVVLFTTLVFGFLTKPLVNYLLPQDASHNTGNRGKRTEPGSPKEDATLPLLSFDESASTNFNRAKDSISLLMEQPVYTIHRYWRKFDDTYMRPIFGGPRRENQPEC | Function: May act in low affinity electroneutral exchange of protons for cations such as Na(+) or K(+) across membranes. May also exchange Li(+) and Cs(+) with a lower affinity.
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58872
Sequence Length: 529
Subcellular Location: Vacuole membrane
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Q8RWU6 | MSSELQISPAIHDPQGQEKQQQAAGVGILLQIMMLVLSFVLGHVLRRHKFYYLPEASASLLIGLIVGGLANISNTETSIRTWFNFHDEFFFLFLLPPIIFQSGFSLQPKPFFSNFGAIVTFSVLGTFVASMVTGLLVYLGGVMFLMYRLPFVECLMFGSLISATDPVTVLSIFQELGSDVNLYALVFGESVLNDAMAISLYRTMSLVRSHSSGQNFFMVIVRFLETFVGSMSAGVGVGFTSALLFKYAGLDVDNLQNLECCLFVLFPYFSYMLAEGLSLSGIVSILFTGIVMKHYTYSNLSANSQRFVSAFFHLISSLAETFVFIYMGFDIAMEKHSWSHLGFIFFSILFIVIARAANVFGCGYLVNLARPAHRKIPMTHQKALWYSGLRGAMAFALALQSVHDLPEGHGQTIFTATTAIVVLTVLLIGGSTGTMLEALEVVGDSHDTSLGDGFEVVNSRYMTSYDDEDTPPGSGFRTKLREFHKSAASFTELDRNYLTPFFTSNNGDYDDEGNMEQHHEERIPFTRRGNLNNRG | Function: Involved in trafficking to the vacuole . Required for cell proliferation and cell expansion, but not for cell differentiation . Acts in low affinity electroneutral exchange of protons for cations such as Na(+) or K(+) across membranes (By similarity). May also exchange Li(+) and Cs(+) with a lower affinity (By similarity).
Catalytic Activity: H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59314
Sequence Length: 535
Subcellular Location: Endosome membrane
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Q9APC2 | IDGNEAVAQVVYQINEVIAIYPITPSSPMAEWADAWASEGKPNIWGTVPTVVQMQSEGGVAGAVHGALQTGSLTTTFTASQGLLLMIPNMYKIAGELTPTVFHIAARSLAAQALSIFGDHSDVMATRGTGFAMLCAASVQEAHDFALISTRTTLESRIPFLHFFDGFRTSHEINKIELLTTENLQTFIPNELVIAHRSRAFTPDNSFTRGTGQNPDVYFQGEEGTVIYYIACQASLKSMDEFAQMTGRQYQLFEYHGDSTAERVIVLMGSGCETVHETVDYLNTLGEKVGVIKVRLYHPFDSQRFIAALPPTTRSIAVLDRTKEPGASGEPLYLDVVAALYEAGEQLPKVVGGRYGLSSKEFTPGMVKAVFDNLAATIPKNHFTIGINDDVSHTSLDYDPDFNI | Function: Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase.
Catalytic Activity: CoA + 2 H(+) + oxidized [flavodoxin] + pyruvate = acetyl-CoA + CO2 + reduced [flavodoxin]
Sequence Mass (Da): 44044
Sequence Length: 404
EC: 1.2.7.-
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P33594 | MTLLNISGLSHHYAHGGFNGKHQHQAVLNNVSLTLKSGETVALLGRSGCGKSTLARLLVGLESPAQGNISWRGEPLAKLNRAQRKAFRRDIQMVFQDSISAVNPRKTVREILREPMRHLLSLKKSEQLARASEMLKAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQVVGEKLTFSSDAGRVLQNAVLPAFPVRRRTTEKV | Function: Part of the ABC transporter complex NikABCDE involved in nickel import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + Ni(2+)(out) = ADP + H(+) + Ni(2+)(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29722
Sequence Length: 268
Subcellular Location: Cell inner membrane
EC: 7.2.2.11
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Q88HL0 | MSLLHVHHVGHRYRTGGLLRKRGWLQVLDGIDLQLHAGESIGLLGSSGSGKSTLARLLLGLEKPAQGQVSFAGQDVSQLKGEQARAFQRTVQLVFQDAPGAFNPQRSIGWSIAEPLRHLTDMDEAARQARTLALLEEMGLRAEHAQRLPQQLSGGQLQRANIARALAASPQLVVLDEALSNLDRLLQLQILQQLEALRQRSGTAFVLISHDLSLVQYFCQRVVLLHGGRIVEERPVTHDLCFAHPVGRQLQAAVLPVRPQRRPSPQGLPTAAH | Function: Part of the ABC transporter complex NikABCDE involved in nickel import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + Ni(2+)(out) = ADP + H(+) + Ni(2+)(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29974
Sequence Length: 273
Subcellular Location: Cell inner membrane
EC: 7.2.2.11
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Q99UA3 | MIELKHVTFGYNKKQMVLQDINITIPDGENVGILGESGCGKSTLASLVLGLFKPVKGEIYLSDNAVLTIFQHPLTSFNPDWTIETSLKEALYYYRGLTDNTAQDQLLLQHLSTFELNAQLLTKLPSEVSGGQLQRFNVMRSLLAQPRVLICDEITSNLDVIAEQNVINILKAQTITNLNHFIVISHDLSVLQRLVNRIIVLKDGMIVDDFAIEELFNVDRHPYTKELVQTFSY | Function: Part of the ABC transporter complex NikABCDE (Opp2) involved in nickel import. Probably responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + Ni(2+)(out) = ADP + H(+) + Ni(2+)(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26291
Sequence Length: 233
Subcellular Location: Cell membrane
EC: 7.2.2.11
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Q9JHE8 | MESDREIIHLQHRHSTPGGNQRHINLNHYATKKSVAESMLDVALFMSNAMRLKSVLEQGPFSQYYTTLLTLISASLLLQVVIGILLVVIARLNLNEVENQWRLNQLNNAATTLVFITVVINIFITAFGAHKTGSVAARTSSNPI | Function: Homophilic cell adhesion molecule that promotes axonal growth. May play a role in nerve regeneration and in the formation and function of other tissues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15996
Sequence Length: 144
Subcellular Location: Membrane
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P12669 | MIKSWKPQELSISYHQFTVFQKDSTPPVMDWTDEAIEKGYAAADGAISFEAQRNTKAFILFRLNSSETVNSYEKKVTVPFHVTENGIHIESIMSKRLSFDLPKGDYQLTCWTVPAEMSDLHADTYIIDAVSV | Function: Plays a role in the competence of cells to be transformed. It inhibits the activity of the DNA-entry nuclease.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 14997
Sequence Length: 132
Subcellular Location: Cell membrane
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Q8VZW1 | MADISGNGYGNAREEVVMVNLKDEVEHQQEMEDIHNPRPLKKQDSLLSVSVPFLQKLIAEFLGTYFLVFTGCASVVVNMQNDNVVTLPGIAIVWGLTIMVLIYSLGHISGAHINPAVTIAFASCGRFPLKQVPAYVISQVIGSTLAAATLRLLFGLDHDVCSGKHDVFIGSSPVGSDLQAFTMEFIVTFYLMFIISGVATDNRAIGELAGLAIGSTVLLNVLIAAPVSSASMNPGRSLGPALVYGCYKGIWIYLVAPTLGAIAGAWVYNTVRYTDKPLREITKSGSFLKTVRIGST | Function: Water channel probably required to promote glycerol permeability and water transport across cell membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31715
Sequence Length: 296
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala/Gly (NPA).
Subcellular Location: Membrane
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Q40746 | MAGGDNNSQTTNGGSGHEQRAMEEGRKQEEFAADGQGCGLAFSVPFIQKIIAEIFGTYFLIFAGCGAVTINQSKNGQITFPGVAIVWGLAVMVMVYAVGHISGAHFNPAVTLAFATCRRFPWRQVPAYAAAQMLGATLAAGTLRLMFGGRHEHFPGTLPAGSDVQSLVLEFIITFYLMFVISGVATDNRAIGELAGLAVGATILLNVLIAGPISGASMNPARSLGPAMIGGEYRSIWVYIVGPVAGAVAGAWAYNIIRFTNKPLREITKSGSFLKSMNRMNSST | Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29973
Sequence Length: 284
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Membrane
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Q0DK16 | MAGGEHGVNGQHEETRAMEEGSRDHQARCENSEQDGGSKSSSNNHPMFSVQFAQKVIAEILGTFFLIFAGCAAVAVNKRTGGTVTFPGICITWGLAVMVMVYSVGHISGAHLNPAVTLAFATCGRFPWRRVPAYAAAQVAGSAAASAALRALFGGAPEHFFGTAPAGSDVQSLAMEFIITFYLMFVVSGVATDNRAIGELAGLAVGATVLVNVLFAGPISGASMNPARTIGPAIILGRYTGIWVYIAGPVFGAVAGAWAYNLIRFTDKPLREITMTASFIRSTRRN | Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30022
Sequence Length: 286
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Membrane
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Q5Z9E2 | MARREVDDSYTNGSVVEVVSIEEGSKMDKEDDHQNPQAPDGGDVVVCGMPMSFTFLQMLLAEFLATFFLMFAGLGAITVEEKKGAVTFPGVAVAWGAAVMAMVYAVGHVSGAHLNPAVTLGFAVAGRFPWRRAPAYALAQTAAATAASVVLRLMFGGRHAPVPATLPGGAHAQSLVIEFVITFYLMFVIMAVATDDQAVGHMAGVAVGGTIMLNVLFAGPVSGASMNPARSIGPALVGSKYTALWVYILGPFAGAAAGAWAYSLIRLTGDRTD | Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28402
Sequence Length: 273
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Membrane
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Q8GT75 | MASSRFQSGFCPISSCPSLENFIERIKDACRFTLSAVLGTILSAVLTFFFALVGTLLGALTGALIGQETESGFIRGAAVGAISGAVFSIEVFESSLVLWKSNESRFGCLLYLIDVIVSLISGRLVRERIGPAMLSAVQSQMGAVDSTFEELSSIFDTGGSKGLTGDLVDKIPKIKITGKNNLDASGNKDSCSVCLQDFQLGETVRSLPHCHHMFHLPCIDNWLFRHGSCPMCRRDL | Function: Intrinsic thylakoid membrane protein that fixes RPOT2 on the stromal side of the thylakoid membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25451
Sequence Length: 236
Subcellular Location: Plastid
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Q8W037 | MDDISVSKSNHGNVVVLNIKASSLADTSLPSNKHESSSPPLLSVHFLQKLLAELVGTYYLIFAGCAAIAVNAQHNHVVTLVGIAVVWGIVIMVLVYCLGHLSAHFNPAVTLALASSQRFPLNQVPAYITVQVIGSTLASATLRLLFDLNNDVCSKKHDVFLGSSPSGSDLQAFVMEFIITGFLMLVVCAVTTTKRTTEELEGLIIGATVTLNVIFAGEVSGASMNPARSIGPALVWGCYKGIWIYLLAPTLGAVSGALIHKMLPSIQNAEPEFSKTGSSHKRVTDLPL | Function: Low water transport activity in yeast cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30581
Sequence Length: 288
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Subcellular Location: Endoplasmic reticulum membrane
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P42580 | MLAWQDVGAKAAPSHHKISFSVLDILDPQKFTRAALPPVRLAALEAKKSLEEVEAGQDACSGNPIGSQETPDAVGRGIDPGSPVEGSEAEEEEEAEDAGRAHQPERWQGVHEGSPEARAVAVGTEESGAEGLPASPGSPGSPRPRRRRAESSCAKPRRARTAFTYEQLVALENKFRATRYLSVCERLNLALSLSLTETQVKIWFQNRRTKWKKQNPGADGAVQAGGGAPQPGTPGAVAGGGGSATGSSPGPPVPGALPYQTFPTYPATNVLFPAASFPLTTAANGSPFTPFLGPSYLTPFYAPHL | Function: May function in cell specification, particularly in the CNS.
PTM: Phosphorylated by HIPK2 in vitro.
Sequence Mass (Da): 32013
Sequence Length: 305
Subcellular Location: Nucleus
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P50220 | MSMSPKHTTPFSVSDILSPLEESYKKVGMEGGGLGAPLAAYRQGQAAPPAAAMQQHAVGHHGAVTAAYHMTAAGVPQLSHSAVGGYCNGNLGNMSELPPYQDTMRNSASGPGWYGANPDPRFPAISRFMGPASGMNMSGMGGLGSLGDVSKNMAPLPSAPRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQQLQQDSGGGGGGGGGAGCPQQQQAQQQSPRRVAVPVLVKDGKPCQAGAPAPGAASLQSHAQQQAQQQAQAAQAAAAAISVGSGGAGLGAHPGHQPGSAGQSPDLAHHAASPAGLQGQVSSLSHLNSSGSDYGAMSCSTLLYGRTW | Function: Transcription factor that binds and activates the promoter of thyroid specific genes such as thyroglobulin, thyroperoxidase, and thyrotropin receptor. Crucial in the maintenance of the thyroid differentiation phenotype. May play a role in lung development and surfactant homeostasis. Forms a regulatory loop with GRHL2 that coordinates lung epithelial cell morphogenesis and differentiation . Activates the transcription of GNRHR and plays a role in enhancing the circadian oscillation of its gene expression. Represses the transcription of the circadian transcriptional repressor NR1D1 .
PTM: Phosphorylated on serine residues by STK3/MST2.
Sequence Mass (Da): 38570
Sequence Length: 372
Subcellular Location: Nucleus
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P43697 | MSLTNTKTGFSVKDILDLPDTNDEEGSVAEGPEEESEGPEPAKRAGPLGQGALDAVHSLPLKSPFYDSSDNPYTRWLASTEGLQYSLHGLAASAPPQDSSSKSPEPSADESPDNDKETPGGGGDAGKKRKRRVLFSKAQTYELERRFRQQRYLSAPEREHLASLIRLTPTQVKIWFQNHRYKMKRARAEKGMEVTPLPSPRCVAVPVLVRDGKPCHALKAQDLAAATFQAGIPFSAYSAQSLQHMQYNAQYSSASTPQYPTAHPLVQAQQWTW | Function: Transcriptional activator involved in the development of insulin-producting beta cells in the endocrine pancreas (By similarity). May also be involved in specifying diencephalic neuromeric boundaries, and in controlling the expression of genes that play a role in axonal guidance. Binds to elements within the NEUROD1 promoter (By similarity).
Sequence Mass (Da): 30065
Sequence Length: 273
Domain: The homeodomain is essential for interaction with OLIG2.
Subcellular Location: Nucleus
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P42586 | MSLTNTKTGFSVKDILDLPDTNDEDGSVAEGPEEESEGPEPAKRAGPLGQGALDAVQSLPLKSPFYDSSDNPYTRWLASTEGLQYSLHGLAASAPPQDSSSKSPEPSADESPDNDKETQGGGGDAGKKRKRRVLFSKAQTYELERRFRQQRYLSAPEREHLASLIRLTPTQVKIWFQNHRYKMKRARAEKGMEVTPLPSPRRVAVPVLVRDGKPCHALKAQDLAAATFQAGIPFSAYSAQSLQHMQYNAQYSSASTPQYPTAHPLVQAQQWTW | Function: Transcriptional activator involved in the development of insulin-producting beta cells in the endocrine pancreas . May also be involved in specifying diencephalic neuromeric boundaries, and in controlling the expression of genes that play a role in axonal guidance. Binds to elements within the NEUROD1 promoter .
Sequence Mass (Da): 30126
Sequence Length: 273
Domain: The homeodomain is essential for interaction with OLIG2.
Subcellular Location: Nucleus
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Q90788 | MFPSPVTTTPFSVKDILNLEQQQQGGLAPMELSSPSCMLATFKQEAFGSEPPALPELPEPPPAKPPAAFPGPYYVKSYGEMDTAKDSKADKKELCALHKSLEQEKRELEDPERPRQRKRRKPRVLFSQAQVYELERRFKQQKYLSAPERDHLANVLKLTSTQVKIWFQNRRYKCKRQRQDQTLEMVGIPPPRRIAVPVLVRDGKPCLGESSPYSSPYNVSINPYSYNAYPAYPNYNSPACNANYNCSYPAVQPVQPSAAGNNFMNFSVGDLNSVQPPIPQGNAGISTLHGIRAW | Function: Transcription factor required for the development of the heart and the spleen. Implicated in commitment to and/or differentiation of the myocardial lineage. Binds to the core DNA motif of promoter.
Sequence Mass (Da): 33073
Sequence Length: 294
Domain: The homeobox domain binds to double-stranded DNA.
Subcellular Location: Nucleus
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P52952 | MFPSPALTPTPFSVKDILNLEQQQRSLAAAGELSARLEATLAPSSCMLAAFKPEAYAGPEAAAPGLPELRAELGRAPSPAKCASAFPAAPAFYPRAYSDPDPAKDPRAEKKELCALQKAVELEKTEADNAERPRARRRRKPRVLFSQAQVYELERRFKQQRYLSAPERDQLASVLKLTSTQVKIWFQNRRYKCKRQRQDQTLELVGLPPPPPPPARRIAVPVLVRDGKPCLGDSAPYAPAYGVGLNPYGYNAYPAYPGYGGAACSPGYSCTAAYPAGPSPAQPATAAANNNFVNFGVGDLNAVQSPGIPQSNSGVSTLHGIRAW | Function: Transcription factor required for the development of the heart and the spleen . During heart development, acts as a transcriptional activator of NPPA/ANF in cooperation with GATA4 (By similarity). May cooperate with TBX2 to negatively modulate expression of NPPA/ANF in the atrioventricular canal (By similarity). Binds to the core DNA motif of NPPA promoter . Together with PBX1, required for spleen development through a mechanism that involves CDKN2B repression . Positively regulates transcription of genes such as COL3A1 and MMP2, resulting in increased pulmonary endothelial fibrosis in response to hypoxia .
Sequence Mass (Da): 34918
Sequence Length: 324
Domain: The homeobox domain binds to double-stranded DNA .
Subcellular Location: Nucleus
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P42583 | MFASPVTSTPFSVKDILNLEQHQSGLSPMDITSRLENSSCMLSTFKQESYPGTPCLSELTEEMSQRDTAKGPSSFPGSFFVKNYLEMDSKDPKDHKKDICPLQKTLEHDKREAEDPERPRQRKRRKPRVLFSQAQVYELERRFKQQKYLSAPERDHLANVLKLTSTQVKIWFQNRRYKCKRQRQDQTLEMVGLPPPRRIAVPVLVRDGKPCLGESSPYNSPYNVSINPYSYNTYPAYSNYSNPACSGSYNCSYSSMPSMQPTSAGNNFMNFSVGDLNTVQTPIQQASSVSALHHGIRAW | Function: Transcription factor required for the development of the heart and the spleen. Implicated in commitment to and/or differentiation of the myocardial lineage. May regulate the expression of genes involved in cardiogenesis and play a role in the formation of gut and the pharyngeal region. Binds to the core DNA motif of promoter.
Sequence Mass (Da): 34097
Sequence Length: 299
Domain: The homeobox domain binds to double-stranded DNA.
Subcellular Location: Nucleus
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Q75D90 | MTIQAHKRTLSEVSTSSVGQLKRREGYTEDYTDEGSDIDMPEYVTDSANNQQWQDTISRVVQSVVSVHFAQVAPFDCESALVSEATGFVVDAKLGIILTNRHVVGAGPFSGYAVFDNHEECDVIPIYRDPVHDFGFLKFDPSTIKYMNVQALELKPALAKVGSEIRVVGNDAGEKLSILAGFISRVDRNAPDYGELTYNDFNTEYIQAAAAASGGSSGSPVVNIDGYAVALQAGGSTEASTDFFLPLDRILRALRCIQGSQPITRGTIQTQWLLKPYDECRRMGLSPESEAKAREQFPGKIGLLVAETILREGPADKSIKEGDILISINGQMICSFIQVDAILDENVGKPITLVVQRSGIDITVECTVGDLHAITPSRYVEVCGATFNELSYQMARYYAIPVRAVFLSSATGSFCFDTKEKLGWIVDEVNNQPTPTLDTFIEVMSTIPDCSRVTVQYHHLVDQHSPHVTTVYIDRHWCNEFRIFERNDETGIWDYKNLADPIPALPLKPQTAKFIDLPISNPKLARLARMLVMVSTIGPVPLDSVDPEPRKAAGLVLDAKQGYVIVSRRIVPHDCMDVFVTIAESVLVPASVVFLHPTQNYVIVKYDPAQVQAAVETPILSTERLKRGDKVQFVGYTHNFRSVSSETTVTDISSLSIPSNMVPRYRATNLEAISIESSVGSRCHSGILADDDGTVRALWLSFLGEKQDEKDKIYLMGLDLVDIGEVVEVLKKGKIPRVNIVDSGFGSISVLQARLRGVPEEWIKRMESESENRLQFITVTRVSYTDEEQKLVSGDIILSVNDQLVKQMRDLEGIVTTTDVPAVQQVLRFKIVRKGSIMDLDIKTIEVEETSKIVIFAGCILQAPHHAVRQAMLNIPSGVYCTFRGQSSPAIQYGISSTNFITHVNEIETPDLDRFLEVVRTIPDNTYCKIRLVTFDNVPFAISLKTNYHYFPTSELSRNSDTGRWIEHLCNATPAKN | Function: Nuclear serine protease which mediates apoptosis.
Sequence Mass (Da): 108313
Sequence Length: 977
Subcellular Location: Nucleus
EC: 3.4.21.-
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Q4L4T4 | MWYNNQLTQSLNIQYPIIQAGMAGSTTAELVATVSNKGGLGCIGAGYFTTKKLEQEIQKVQGLTSQPFGVNLFVPSHQSYTNEQVEHMNAWLKPYRKALNLEEPVVNISEEQQFKSAIQTVIKYRVPVCCFTFGIPSKEIIEQLKGAKITLIGTATTVDEAIANEHAGMDIVVAQGSEAGGHRGSFLTTNNQREPLIGTMSLIPQIVDHVSIPVVAAGGVMDGRGILASQILGAQGVQMGTAFLTTEESGANQLVKQAVLHSKETDTIVTDVFSGKSARGINNEFVETMKQYEGNIPPYPVQNQLTNSIRKTAASTGHREWTHMWSGQSPRLATSQHVNQLMDRLVEQVKTLLTVVR | Cofactor: Binds 1 FMN per subunit.
Function: Nitronate monooxygenase that uses molecular oxygen to catalyze the oxidative denitrification of alkyl nitronates. Acts on propionate 3-nitronate (P3N), the presumed physiological substrate. Probably functions in the detoxification of P3N, a metabolic poison produced by plants and fungi as a defense mechanism.
Catalytic Activity: H2O + 3 O2 + 3 propionate 3-nitronate = 3 3-oxopropanoate + 3 H(+) + H2O2 + 2 nitrate + nitrite
Sequence Mass (Da): 38909
Sequence Length: 357
EC: 1.13.12.-
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A1L3G9 | MAGEVEGRGCGFSLGVLVTLLVLPLPSLCTLSTEKELHVIKLYEGRMVRYNESRNFCYQRTYEPKWSDVWTKIQIRINSTKMIRVTQVDNEEKLKEMETFNMFDFFSSFLKEKLNDTFIYVNLYSNKTCVKVHLTDTDTYYSVALSRGFDPRLFFVFLCGLLLFFYGDTLSRSQLFFYSTGITVGMLASMLILVFMLSKLMPKKSPFFALLLGGWSVSIYVIQLVFRNLQAICSEYWQYLIVYLGIVGFVSFAFCYIYGPLENERSINILNWTLQLIGLLLMYVSVQIQHIAVTIVVIAFCTKQIEYPVQWIYILYRKIKLKRAKPGPPRLLTEEEYRKQADVETRKALEELRECCSSPDFAAWKTISRIQSPKRFADFVEGSSHLTPNEVSVHEHEYGLGGSFLEDELFGEDSDVEEEMEIEPPLYPIPRSVF | Function: In concert with ran, required for proper eye development . May be involved in the expression of early eye marker genes . Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity).
PTM: Phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50327
Sequence Length: 434
Domain: The transmembrane domains are required and sufficient for its oligomerization.
Subcellular Location: Nucleus inner membrane
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P47482 | MKQKIIIFGGSFDPIHNAHLYIAKHAIKKIKAQKLFFVPTYNGIFKNNFHASNKDRIAMLKLAIKSVNNALVSNFDIKTKNAFSINTVNHFKSCYPTSEIYFLIGSDKLNELEKWDHIQQLKDLCTFVCYERKPYPFNKKIANQFNVKYLAKCPLEIASSKLLNQPRKKLIPLAVLNYINTNHLYLIPTLKAMVDDKRFQHCLRVGKLAKQLAIANKLDAKRAFVAGAYHDLAKQLPVDQLVNIATSELKITNYPSWKVLHSYVGAYILKNWFGVKDKMIINAIKNHTIPPKQVSKLDMIVYLADKLEPNRKQEQWSGGIEIDQLVKLAKSNLKQAYLITLKYVQNLVKD | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 40217
Sequence Length: 350
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
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Q9PQ21 | MKIILFCGAFDMVHNAHIAMAKQAMKLVNADKLIFLPSNFKFFKAINKNDNLEYEKTKLTPGHHRIAMLKIATKNLVNIEVSDYELKQINKSYTINTIEHFKQIYGSEHEYYFIMGSDNLERFKQWKDWERILKEVKIICFKRGDVCVKKSCPQKSCECESFNFFEHEILLVNDFNYNISSTEIKKRHNLTSGIDPAVLDYINEHGLYALWLLEKHLISYDNFNNLEKKVARINHCRRVAQMCVDLMNVYDKKLIDQAYCAGIYHDILKCLDEQESVAYFNEHKSELNIGDDFISWRILHSYLGAHLLQTQYGFKNQLILNAIRRHTRPFDFIKDYSELTTLDKILYCADKLEPNRREEIDQINIDYYRKLVFEDLDKAFIEVYQYQQRQRK | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 46645
Sequence Length: 392
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
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Q03NP0 | MSKAITIAEAQRYDAHATNVIGIPAMVLMERAALATFNNLLNDDFDLDRVVVVAATGNNGGDGIAVARLLKIRGIDVTIYLLGDPENATPQTSQQLKIANYYNIPVTADLNQIVNATLIVDAIFGVGLTRDVTGKFADAINAINAADAKTVAIDVPSGINADTGAVMGVAVVADSTTTMAYNKIGLLTTVGKQHAGTIHVADIGIYAQDRVEHAR | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 22530
Sequence Length: 215
EC: 5.1.99.6
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A5VML0 | MTDKIVTAEEMRHYDFYTINTIGIPSLVLMERAALAVRDEILHAFPIALKDVVVVAGSGNNGGDGIAIARLLHIAGVHVTILNIGNPQHASAEHQTQEKIAQYYQIPETSDLAVLNKATLIVDAMFGIGIDRAVKGAYADAINAINNTDAVVVAVDMPSGVNTDTGEVMGTAVRATTTVTFAYNKVGLTKNDGKDYAGNVVVANDMGTYAVD | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 22430
Sequence Length: 212
EC: 5.1.99.6
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E8N877 | MADPRRDPAAESKDRPSTERVAAYTADAVRAAEAPLLAEGRPLMRTAARALADIAAAEVRTTPGAVLVLAGAGDNGGDALFAAADLASSAERVDVVLVRDRVHREALDAAVAAGARVVSVSDASAGVADYALVLDGILGIGRLADRRLRGSARALVERLLALAHRPRVLAVDVPSGLDPDDGTADAVILPADVTVTFGALKAGLVRGRGPELSGRVHLVDLGLEPYLRRAHPAVTAAIDVVRETPRAAETDRAQRA | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 26451
Sequence Length: 256
EC: 5.1.99.6
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F7FIH8 | MSGLRTLLGLGLLVSSSRFPRVVARGGPRCPGPAWWAARPMHLGDSTMAGGTVKYLSQEEAQAVDEELFNEYKFSVDQLMELAGLSCATAIAKAYPLSSFGSNPPAVLVICGPGNNGGDGLVCARHLKLFGYEPKIHYPKKPNKPLFDALVTQCQKMDIPFLPEVPPEPMLIDELYELVVDAIFGFSFKGAVREPFGTILSIMNGLTVPIASIDIPSGWDVEKGNPEGIRPDLLISLTAPKKAATLFKGRHHYLGGRFVPSDLEKKYQLNLPPYPGTDCVLQLQ | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (By similarity).
PTM: Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 30838
Sequence Length: 284
Subcellular Location: Mitochondrion
EC: 5.1.99.6
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Q8K4Z3 | MSGLRTLLGLGLLVAGSRLPRVISQQSVCRARPIWWGTQRRGSETMAGAAVKYLSQEEAQAVDQELFNEYQFSVDQLMELAGLSCATAIAKAYPPTSMSKSPPTVLVICGPGNNGGDGLVCARHLKLFGYQPTIYYPKRPNKPLFTGLVTQCQKMDIPFLGEMPPEPMMVDELYELVVDAIFGFSFKGDVREPFHSILSVLSGLTVPIASIDIPSGWDVEKGNPSGIQPDLLISLTAPKKSATHFTGRYHYLGGRFVPPALEKKYQLNLPSYPDTECVYRLQ | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (By similarity).
PTM: Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 30973
Sequence Length: 282
Subcellular Location: Mitochondrion
EC: 5.1.99.6
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Q7SGL3 | MALKTLSAKAAAALDRELMSTGAFSIDQLMELAGLSVSQAVARVHPTKQGRRVLVAVGPGNNGGDGLVAARHLFHYGYQPAIYYPKRPKNDLYQRLVKQCEDLEIPFVDDFFAALESTDHVVDAIFGFSFSGEVREPFPAVINAMAETKVPVTSVDAPSSWDINEGPPKSGVGSNFHPNVLVSLTAPKPLVKYFKGRHFVGGRFVAPSIAKKYDFDVPKYEGIDQIVEITDNQVKI | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 25735
Sequence Length: 236
Subcellular Location: Cytoplasm
EC: 5.1.99.6
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A9A432 | MEITVDQMYNIENKGHDMGFLKKFMMENAGAAAVKRLVEKLGNVDSKNILIFVGMGNNGGDGLVMARHLAGYNAKVTVMLLGNPENIKTEESNWNWSILEKMPSVKLMTGGTTNFDFKPDVIVDGILGTGISGEIREPYASAINYINQTDCYKFAVDVPSGLDPQTGETANIFTKCDMTVTFHKMKQGIPKRKDLTGELFAEKIGIPPEAEEGIL | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 23584
Sequence Length: 215
EC: 5.1.99.6
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Q04HC3 | MTTIYISSKQAHNFDDYTINKIGVPSSVLMERAALAVCQRLLESRNFNLKKVLVVAGIGNNGGDGIAVARMLYLKQVPVKIYLLGDREKISKDSRIQLKIAENYGVPFVSNIDDLSSYTTIVDAVFGVGLSRDVTGEIAGIVDFINNSPASVMAVDMPTGLNADNGNIMGTAVKAAETVTMSYNKLGLISETGRKFAGVVTVADIGIYEP | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 22498
Sequence Length: 210
EC: 5.1.99.6
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A0E3W6 | MQQLNKISYLNQIQSQQFDVELMSEEVGFTLDQLMELAGQSIANTVVQLNKEGKSYNKILVLCGPGNNGGDGIVSARHLKQFGLQPEIALFREVKNPFFNRLLNQCKYNLIPIHYELQDLEKYDLLIDAILGFSFKPPLREPYDKPIQQLKTTKTPILSVDIPSGWDVEQGNAQDFFTPQYLISLTLPKLGVKSFKGRHFIGGRFIPLKLQEKYNFIVPEYQGSDTILELSNL | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 26540
Sequence Length: 233
EC: 5.1.99.6
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E0V9D8 | MVRYLSQQEAIDIDQELFNVYKYSVDQLMELAGLSCSIAIYKCYSKLKKILVCCGPGNNGGDGLVAARHLKLFGFEPSVYYPKRTEKPLYQNLTHQCLAMKIDFLNDIPDAKEMSNNYELIVDALFGFSFKPPVRPEFEKVMNVLGKSKVPICSIDIPSGWDVENGCPENGILPDMLISLTAPKKCAKFFNGRFHYLGGRFVPPDLERKYDLKINSEYSGTECCVQLK | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 25777
Sequence Length: 228
EC: 5.1.99.6
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D2QYP6 | MDLQRIYDRRKSRLVDELAIAKYGMLGLMLMENAGRNVAYELLARTPCRRVVIVVGKGNNGGDGWVIARHLDAAGVDVIVLLTTAPNEFRGDAAVNYAIANLAKIKIIDLSRTPTAEAIATHFAEADWLVDAMLGTGATGEPRGAMRLAIEAINQSSVRTLAVDLPTGIDCDSGGAATVAVRADVTCTFVTLKPCCQVAACRSYLGEVRVIDIGVPRALLEEIDAMP | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 24224
Sequence Length: 227
EC: 5.1.99.6
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Q8IKN4 | MITNLFIKSFTFSRSLKNFYVLSLLNYFKLKIYNKIYVPTLGVSLKRKRRSYSLNVRKMEITYLSQDLSQKIDNELMSDEVGYTTEQLMELAGLSISQIIFKEYKPCEFKKILICCGPGNNGGDGLVAARHLKQFGYNVVVLYPKVNDKTLFKRLLKLLEHYEINVLMSLRASDLDNYDLIIDSIFGFSFKGEPRKPFDEIIQMINNSNKVVVSVDVPSGINIDSGLSTNSLFINSDMNISLMLPKQGLKNYKKKHYLGGRFIPISIIKKYNLKVPCFSDDNPYVML | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 32960
Sequence Length: 287
EC: 5.1.99.6
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Q9Y239 | MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICF | Function: Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and thus participates in both innate and adaptive immune responses . Specifically recognizes and binds gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP), a dipeptide present in peptidoglycan of Gram-negative bacteria . Preferentially binds iE-DAP in tripeptide-containing muropeptides (MurNAc-TriDAP or TriDAP) . Ligand binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 . Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling . This in turn leads to the transcriptional activation of hundreds of genes involved in immune response . Also acts as a regulator of antiviral response elicited by dsRNA and the expression of RLR pathway members by targeting IFIH1 and TRAF3 to modulate the formation of IFIH1-MAVS and TRAF3-MAVS complexes leading to increased transcription of type I IFNs . Also acts as a regulator of autophagy via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (By similarity). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling . In addition, plays a role in insulin trafficking in beta cells in a cell-autonomous manner (By similarity). Mechanistically, upon recognizing cognate ligands, NOD1 and RIPK2 localize to insulin vesicles where they recruit RAB1A to direct insulin trafficking through the cytoplasm (By similarity).
PTM: Palmitoylated. Palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection.
Location Topology: Lipid-anchor
Sequence Mass (Da): 107691
Sequence Length: 953
Domain: The LRR repeats recognize and bind gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).
Subcellular Location: Cell membrane
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Q8BHB0 | MEEHGHHEMEGTPLGCHSHIKLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYVDLRLWLSEIGFSPSQLIRTKTIVNTDPVSRYTQQLRHQLGRDSKFMLCYAQKEDLLLEETYMDTLMELVGFNNENLGSLGGLDCLLDHSTGVLNEHGETVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFSCFKESDMLSLQDLLFKHFCYPEQDPEEVFSFLLRFPHTALFTFDGLDELHSDFDLSRVPDSCCPWEPAHPLVLLANLLSGRLLKGAGKLLTARTGVEVPRQLLRKKVLLRGFSPSHLRAYARRMFPERTAQEHLLQQLDANPNLCSLCGVPLFCWIIFRCFQHFQTVFEGSSSQLPDCAVTLTDVFLLVTEVHLNRPQPSSLVQRNTRSPAETLRAGWRTLHALGEVAHRGTDKSLFVFGQEEVQASKLQEGDLQLGFLRALPDVGPEQGQSYEFFHLTLQAFFTAFFLVADDKVSTRELLRFFREWTSPGEATSSSCHSSFFSFQCLGGRSRLGPDPFRNKDHFQFTNLFLCGLLAKARQKLLRQLVPKAILRRKRKALWAHLFASLRSYLKSLPRVQSGGFNQVHAMPTFLWMLRCIYETQSQKVGRLAARGISADYLKLAFCNACSADCSALSFVLHHFHRQLALDLDNNNLNDYGVQELQPCFSRLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLYNNQITDIGARYVAQILDECRGLKHLKLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEICLNGNLIKPEEAKVFENEKRIICF | Function: Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and thus participates in both innate and adaptive immune responses . Specifically recognizes and binds gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP), a dipeptide present in peptidoglycan of Gram-negative bacteria . Preferentially binds iE-DAP in tetrapeptide-containing muropeptides (MurNAc-TetraDAP or TetraDAP) . Ligand binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 (By similarity). Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (By similarity). This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (By similarity). Also acts as a regulator of antiviral response elicited by dsRNA and the expression of RLR pathway members by targeting IFIH1 and TRAF3 to modulate the formation of IFIH1-MAVS and TRAF3-MAVS complexes leading to increased transcription of type I IFNs (By similarity). Also acts as a regulator of autophagy via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry . Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling . In addition, plays a role in insulin trafficking in beta cells in a cell-autonomous manner . Mechanistically, upon recognizing cognate ligands, NOD1 and RIPK2 localize to insulin vesicles where they recruit RAB1A to direct insulin trafficking through the cytoplasm .
PTM: Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF34 promotes proteasomal degradation and thereby negatively regulates NOD1 for instance in NF-kappa-B activation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 107740
Sequence Length: 953
Subcellular Location: Cell membrane
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Q91620 | MASLGVILFFVIASLIHGKPIHSERKAAKIPLEGSNLGYKKPNNIYGSRLSQGMRYPPSMMQLYQTLILGNDTDLSILEYPVLQESDAVLSLIAKSCVVVGNRWTLSFDMSSISSSNELKLAELRIRLPSFERSQDVTVEIYHTKEGQENLFMGSFKTNPSVAMGSSWKIFNLTRMLQYYLHQGEPFTNVEYIEVKNMHERAKPHVIKRGVRAEVEEGLQRNKDNTPASSFPTERVVLVVFTRDKPTASHFGSPSLIHTVESSKYVMSENTVRVTDTRRPRRNQKTKNTIVMNTIPSRSVGKTLCRRVDMIVDFEKIEWGDRIVYPKRFNAYRCEGACPIPLNETFKPTNHAYIKSLVKLYDQEKVECSSCVPVKMSPLSMLLYEDGEVVLKHHEDMIVDECGCN | Function: Cooperation and regulatory loops of multiple nodals are essential for mesendoderm patterning in early embryos. Essential for mesoderm formation and axial patterning during embryonic development. Activates the activin-like signaling pathway to induce dorsal and ventral mesoderm in animal cap ectoderm. In addition, also dorsalizes ventral marginal zone (VMZ) tissues during gastrulation. Induces muscle actin. Appears to act as both a short-range and long-range morphogen. The unprocessed protein inhibits bmp- and wnt-signaling.
Sequence Mass (Da): 46067
Sequence Length: 405
Domain: The pro-region is necessary but not sufficient for wnt-inhibitory activity. The central region is required for muscle induction activity.
Subcellular Location: Secreted
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Q8K3Z0 | MRSSCCDMCSQEEFQAQRSQLVALLISGSLEGFESILDWLLSWDVLSREDYEGLSLPGQPLSHSARRLLDTVWNKGVWGCQKLLEAVQEAQANSHTFELYGSWDTHSLHPTRDLQSHRPAIVRRLYNHVEAMLELAREGGFLSQYECEEIRLPIFTSSQRARRLLDLAAVKANGLAAFLLQHVRELPAPLPLPYEAAECQKFISKLRTMVLTQSRFLSTYDGSENLCLEDIYTENILELQTEVGTAGALQKSPAILGLEDLFDTHGHLNRDADTILVVGEAGSGKSTLLQRLHLLWATGRSFQEFLFIFPFSCRQLQCVAKPLSLRTLLFEHCCWPDVAQDDVFQFLLDHPDRVLLTFDGLDEFKFRFTDRERHCSPIDPTSVQTLLFNLLQGNLLKNACKVLTSRPDAVSALLRKFVRTELQLKGFSEEGIQLYLRKHHREPGVADRLIQLIQATSALHGLCHLPVFSWMVSRCHRELLLQNRGFPTTSTDMYLLILQHFLLHASPPDSSPLGLGPGLLQSRLSTLLHLGHLALRGLAMSCYVFSAQQLQAAQVDSDDISLGFLVRAQSSVPGSKAPLEFLHITFQCFFAAFYLAVSADTSVASLKHLFSCGRLGSSLLGRLLPNLCIQGSRVKKGSEAALLQKAEPHNLQITAAFLAGLLSQQHRDLLAACQVSERVLLQRQARARSCLAHSLREHFHSIPPAVPGETKSMHAMPGFIWLIRSLYEMQEEQLAQEAVRRLDIGHLKLTFCRVGPAECAALAFVLQHLQRPVALQLDYNSVGDVGVEQLRPCLGVCTALYLRDNNISDRGARTLVECALRCEQLQKLALFNNKLTDACACSMAKLLAHKQNFLSLRVGNNHITAAGAEVLAQGLKSNTSLKFLGFWGNSVGDKGTQALAEVVADHQNLKWLSLVGNNIGSMGAEALALMLEKNKSLEELCLEENHICDEGVYSLAEGLKRNSTLKFLKLSNNGITYRGAEALLQALSRNSAILEVWLRGNTFSLEEIQTLSSRDARLLL | Function: Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and plays an important role in gastrointestinal immunity . Specifically activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan found in every bacterial peptidoglycan type . NOD2 specifically recognizes and binds 6-O-phospho-MDP, the phosphorylated form of MDP, which is generated by NAGK . 6-O-phospho-MDP-binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 . Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling . This in turn leads to the transcriptional activation of hundreds of genes involved in immune response . Its ability to detect bacterial MDP plays a central role in maintaining the equilibrium between intestinal microbiota and host immune responses to control inflammation . An imbalance in this relationship results in dysbiosis, whereby pathogenic bacteria prevail on commensals, causing damage in the intestinal epithelial barrier as well as allowing bacterial invasion and inflammation . Acts as a regulator of appetite by sensing MDP in a subset of brain neurons: microbiota-derived MDP reach the brain, where they bind and activate NOD2 in inhibitory hypothalamic neurons, decreasing neuronal activity, thereby regulating satiety and body temperature . NOD2-dependent MDP-sensing of bacterial cell walls in the intestinal epithelial compartment contributes to sustained postnatal growth upon undernutrition . Also plays a role in antiviral response by acting as a sensor of single-stranded RNA (ssRNA) from viruses: upon ssRNA-binding, interacts with MAVS, leading to activation of interferon regulatory factor-3/IRF3 and expression of type I interferon (By similarity). Also acts as a regulator of autophagy in dendritic cells via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry . NOD2 activation in the small intestine crypt also contributes to intestinal stem cells survival and function: acts by promoting mitophagy via its association with ATG16L1 . In addition to its main role in innate immunity, also regulates the adaptive immune system by acting as regulator of helper T-cell and regulatory T-cells (Tregs) . Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling . May also be involved in NLRP1 activation following activation by MDP, leading to CASP1 activation and IL1B release in macrophages .
PTM: Palmitoylated by ZDHHC5; palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection (By similarity). Palmitoylation promotes localization to the cell membrane (By similarity). Palmitoylation protects from SQSTM1/p62-dependent autophagic degradation (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 113562
Sequence Length: 1020
Domain: The ATG16L1-binding motif mediates interaction with ATG16L1.
Subcellular Location: Cell membrane
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Q91609 | MAFLNLFFCLVFISPLMAMPPVLQGRKSISPDSILKDTSTDIGAREFQGRKFPNFMMQLYQNIIRGRDNDLSNLEHPTLQESDTVQSFIAKSYTTVGNRWTLFFDMSSISRSNELKLAELRICLPSFRKSHSVTVDIYHTNDGKEKLFMGSFKTKLSSALDSDCKVFNLTILLQNFLTRGKRLIKDEYIQAKGLHLKDLEKSATEKDTENVDTMKQHQYHVSDFAAERIMLVVFAKEQSHAKPDPPSLGQKLFPSKYGIDDNANKVNGFRRLRRNKKEKTQIHVSTVPPKPIEEIKPECKKVDMFVDFQKIGWGSWIIYPKAYNAYRCESTCAVPQNETENATNHSYIKSLLPLSDMERKECPSCVPMKMMSMSMLYYENEDFILRHHEEMIVEECGFKDM | Function: Exhibits mesoderm-dorsalizing activity and neural-inducing activity, but lacks mesoderm-inducing activity. Regulates the expression of specific mesodermal and neural genes. Induces convergent extension movements at the embryonic midline by activating the fgf signaling pathway to induce t/bra expression in the organizer region. Acts with wnt11 to induce Spemann organizer cells and induce axis formation. The unprocessed protein antagonizes bmp-signaling.
Sequence Mass (Da): 46301
Sequence Length: 401
Domain: The propeptide region is both necessary and sufficient for bmp-inhibitory activity (By similarity). The propeptide region and the N- and C-terminal thirds of the mature protein are necessary for neural induction activity. Although cleavage doesn't appear essential for activity, residues surrounding the cleavage site are necessary for activity.
Subcellular Location: Secreted
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Q9Y2X3 | MLVLFETSVGYAIFKVLNEKKLQEVDSLWKEFETPEKANKIVKLKHFEKFQDTAEALAAFTALMEGKINKQLKKVLKKIVKEAHEPLAVADAKLGGVIKEKLNLSCIHSPVVNELMRGIRSQMDGLIPGVEPREMAAMCLGLAHSLSRYRLKFSADKVDTMIVQAISLLDDLDKELNNYIMRCREWYGWHFPELGKIISDNLTYCKCLQKVGDRKNYASAKLSELLPEEVEAEVKAAAEISMGTEVSEEDICNILHLCTQVIEISEYRTQLYEYLQNRMMAIAPNVTVMVGELVGARLIAHAGSLLNLAKHAASTVQILGAEKALFRALKSRRDTPKYGLIYHASLVGQTSPKHKGKISRMLAAKTVLAIRYDAFGEDSSSAMGVENRAKLEARLRTLEDRGIRKISGTGKALAKTEKYEHKSEVKTYDPSGDSTLPTCSKKRKIEQVDKEDEITEKKAKKAKIKVKVEEEEEEKVAEEEETSVKKKKKRGKKKHIKEEPLSEEEPCTSTAIASPEKKKKKKKKRENED | Function: Required for 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome .
PTM: Sumoylation is essential for high-affinity binding to snoRNAs.
Sequence Mass (Da): 59578
Sequence Length: 529
Subcellular Location: Nucleus
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Q6DFW4 | MLVLFETSVGYAIFKVLNEKKLQEVDSLWKEFETPEKANKIVKLKHFEKFQDTAEALAAFTALMEGKINKQLKKVLKKIVKEAHEPLAVADAKLGGVIKEKLNLSCIHSPVVNELMRGIRSQMDGLIPGVEPREMAAMCLGLAHSLSRYRLKFSADKVDTMIVQAISLLDDLDKELNNYIMRCREWYGWHFPELGKIISDNLTYCKCLQKVGDRKNYASASLSEFLSEEVEAEVKAAAEISMGTEVSEEDICNILHLCTQVIEISEYRTQLYEYLQNRMMAIAPNVTVMVGELVGARLIAHAGSLLNLAKHAASTVQILGAEKALFRALKSRRDTPKYGLIYHASLVGQSSPKHKGKISRMLAAKTVLAIRYDAFGEDSSSAMGIENRAKLEARLRILEDRGIRKISGTGKALAKAEKYEHKSEVKTYDPSGDSTLPTCSKKRKIEEVDKEDEITEKKAKKAKIKIKAEVEEEMEEEEAEEEQVVEEEPTVKKKKKKDKKKHIKEEPLSEEEPCTSTAVPSPEKKKKKKKKKDAED | Function: Required for 60S ribosomal subunit biogenesis (By similarity). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs (By similarity). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (By similarity).
PTM: Sumoylation is essential for high-affinity binding to snoRNAs.
Sequence Mass (Da): 60343
Sequence Length: 536
Subcellular Location: Nucleus
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Q59105 | MSKEKASIGNGPGGIGRRQFLGTAALAGLAGVVACTDKGAAPAAAAVGAPASGAHGAAHGAGASVHLKPGELDTYYGLWSGGHTGDMRVLGLPSGREILRIPCFVPDALVGWGITNESKKVMGARPDGTLRYTVADTHHTHASYKDGNYDGRYAWVNDKINSRIARIRLDYFICDKITELPNVQGFHGIFPDKRDPVDTKINYTTRVFCGGEFGIPLPSAPTEDAGKYRSLFTCVDAETMAVRWQVLIDGNCDLVATSYDGKLAATNQYNTENGAHFEDMMSAERDACVFFNIARIEAAVQAGKFKTYGDSKVPVVDGTQAANKDPKTALTAYVSVPKNPHGVNASPDQKYFICAGKLSPTATVIELSRVLGWFDGKQEKLDDAIVAEVELGLGPLHTAFDGRGNAYTTLFLDSQLVKWNLDAAIKFHKGDKNAKYVVDRLDLQYQPGHVNASQSETVAADGKYLAVGCKFSKDRFLPVGPLHPENEQLIDISGQKMVLMADHPVRGEPHDFIIFKRELVRPKQVYALDDFPLAIKDPKESGVFRNGRKVTVKITSQAPAFSLREFKLKKGDEVTLILTNLDKIEDLTHGFAIPKYNVNFIVNPQETASVTFVADKPGVFWCYCTHFCHALHLEMRTRMIVEA | Cofactor: Binds 2 calcium ions per subunit.
Function: Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c] + 2 H(+) + nitrous oxide
Sequence Mass (Da): 70085
Sequence Length: 643
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4.
Subcellular Location: Periplasm
EC: 1.7.2.4
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Q51705 | MESKQEKGLSRRALLGATAGGAAVAGAFGGRLALGPAALGLGTAGVATVAGSGAALAASGDGSVAPGQLDDYYGFWSSGQSGEMRILGIPSMRELMRVPVFNRCSATGWGQTNESVRIHERTMSERTKKFLAANGKRIHDNGDLHHVHMSFTEGKYDGRFLFMNDKANTRVARVRCDVMKCDAILEIPNAKGIHGLRPQKWPRSNYVFCNGEDETPLVNDGTNMEDVANYVNVFTAVDADKWEVAWQVLVSGNLDNCDADYEGKWAFSTSYNSEKGMTLPEMTAAEMDHIVVFNIAEIEKAIAAGDYQELNGVKVVDGRKEASSLFTRYIPIANNPHGCNMAPDKKHLCVAGKLSPTATVLDVTRFDAVFYENADPRSAVVAEPELGLGPLHTAFDGRGNAYTSLFLDSQVVKWNIEDAIRAYAGEKVDPIKDKLDVHYQPGHLKTVMGETLDATNDWLVCLSKFSKDRFLNVGPLKPENDQLIDISGDKMVLVHDGPTFAEPHDAIAVHPSILSDIKSVWDRNDPMWAETRAQAEADGVDIDNWTEEVIRDGNKVRVYMSSVAPSFSIESFTVKEGDEVTVIVTNLDEIDDLTHGFTMGNYGVAMEIGPQMTSSVTFVAANPGVYWYYCQWFCHALHMEMRGRMLVEPKEA | Cofactor: Binds 2 calcium ions per subunit.
Function: Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c] + 2 H(+) + nitrous oxide
Sequence Mass (Da): 71414
Sequence Length: 652
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4.
Subcellular Location: Periplasm
EC: 1.7.2.4
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Q8XQB8 | MMSKHPHSPSTPQDETPSVPGRRRFMNSAALAGLATVVACTDKGAPAGSAAATGVAATAEEHTVAGLHPKPGQLDTYYGLWSGGHTGDMRVMGMPSGREIHRIPMFVPDALVGWGITNESKKVMGTRPDGRLKYTVGDTHHVHASYKDGNYDGRYAWINDKINSRLGRVRLDYFICDKITELPNVQGFHGIFPDKRDPVDPQINYTTRVFCGGEFAIPLPNTAGIDDPAKYRSLFTCVDAESMEVRWQVLIDGNCDLVATSYDGKLAATNQYNTEMGAHYEDMMSAERDACLFFNVARIEAAVKAGRFKTIGDSKVPVVDGTHAANQDPKTALTAYVSVPKNPHGVNASPDQKYFICAGKLSPTATVIELARVLDWFDGKLAKIDDAIVAEVELGLGPLHTAFDGRGNAYTTLFLDSQIVKWNIDAAIRFHKGDKNAKYVVDRLDVHYQPGHLNASQSETVAADGKFLAVGCKFSKDRFLPVGPLHPENEQFIDISGDKMVLLQDHPIRSEPHDFIIFKRELLHPKQIYSLDDFPLATKDPKQSGVVRNGKKVTVRLTSQAPSYSLREFKLKKGDEVTLILTNLDKVEDLTHGFAIPKYDINFIVNPQETASVTFIADKPGVFWCYCTHFCHALHLEMRSRMIVEA | Cofactor: Binds 2 calcium ions per subunit.
Function: Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c] + 2 H(+) + nitrous oxide
Sequence Mass (Da): 71307
Sequence Length: 646
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4.
Subcellular Location: Periplasm
EC: 1.7.2.4
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P19573 | MSDKDSKNTPQVPEKLGLSRRGFLGASAVTGAAVAATALGGAVMTRESWAQAVKESKQKIHVGPGELDDYYGFWSGGHQGEVRVLGVPSMRELMRIPVFNVDSATGWGLTNESRHIMGDSAKFLNGDCHHPHISMTDGKYDGKYLFINDKANSRVARIRLDIMKCDKMITVPNVQAIHGLRLQKVPHTKYVFANAEFIIPHPNDGKVFDLQDENSYTMYNAIDAETMEMAFQVIVDGNLDNTDADYTGRFAAATCYNSEKAFDLGGMMRNERDWVVVFDIHAVEAAVKAGDFITLGDSKTPVLDGRKKDGKDSKFTRYVPVPKNPHGCNTSSDGKYFIAAGKLSPTCSMIAIDKLPDLFAGKLADPRDVIVGEPELGLGPLHTTFDGRGNAYTTLFIDSQVVKWNMEEAVRAYKGEKVNYIKQKLDVHYQPGHLHASLCETNEADGKWLVALSKFSKDRFLPVGPLHPENDQLIDISGDEMKLVHDGPTFAEPHDCIMARRDQIKTKKIWDRNDPFFAPTVEMAKKDGINLDTDNKVIRDGNKVRVYMTSMAPAFGVQEFTVKQGDEVTVTITNIDQIEDVSHGFVVVNHGVSMEISPQQTSSITFVADKPGLHWYYCSWFCHALHMEMVGRMMVEPA | Cofactor: Binds 2 calcium ions per subunit.
Function: Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c] + 2 H(+) + nitrous oxide
Sequence Mass (Da): 70822
Sequence Length: 638
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4.
Subcellular Location: Periplasm
EC: 1.7.2.4
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Q6YPG5 | MAAPPLLSLSQRLLFLSLSLPKPQLAPNPSSFSPTRAASTAPPPPEGAGPAAPSRGDRFLGTQLAAEAAARVLAPEDAERRRRRREKRKALARKPSAAACYGCGAPLQTADEAAPGYVHPATYDLKKRHHQLRTVLCGRCKLLSHGHMITAVGGHGGYPGGKQFVSADQLRDKLSYLRHEKALIIKLVDIVDFNGSFLARVRDFAGANPIILVITKVDLLPRDTDLNCIGDWVVEAVVKKKLNVLSVHLTSSKSLVGVTGVISEIQQEKKGRDVYILGSANVGKSAFISAMLRTMAYKDPVAAAAQKYKPIQSAVPGTTLGPIQIEAFLGGGKLYDTPGVHLHHRQAAVIHADDLPSLAPQSRLRARCFPANDTDVGLSGNSLFWGGLVRIDVVKALPRTRLTFYGPKKLKINMVPTTEADEFYEREVGVTLTPPAGKEKAEGWVGLQGVRELQIKYEESDRPACDIAISGLGWVAVEPLGVPSSNPDESAEEEDNESGELHLRVHVPKPVEIFVRPPLPVGKAASQWYRYQELTEEEEELRPKWHY | Function: Produces nitric oxide (NO) which is a messenger molecule involved in hormonal signaling and defense responses in plant.
Catalytic Activity: H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide
Sequence Mass (Da): 59510
Sequence Length: 547
EC: 1.14.13.39
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Q9I9M2 | LNYQLSPSFEYQSDPWFTHVWKGVNGTPTKKRAIGFKKLAKAVKFSTKLMGQAMAKRVKATILYATETGKSQVYAKTLCEIFKHAFDAKVMSMDEYDIVHLEHEALVLVVTSTFGNGDPPENGEKFGSALMEIRHPSSNSAERKSYKVRFNSVSSYSDSRKSSSDEPEHKDNFESTGPLANVRFSAFGLGSRAYPHFCAFARAVDTLLEELG | Cofactor: Binds 1 FAD.
Function: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body.
Catalytic Activity: H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide
Sequence Mass (Da): 23651
Sequence Length: 212
EC: 1.14.13.39
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C5H5C4 | MKRSLWVMQVLHWAVMLALVQCGALGARRFRGGRNPQPRRALPSAHYRDRGETTESFSLDFTAVEENMDNFMTQVKNLAQSLYPCSAQKLDYDMKLHFLENTSVTCNDGTPAGYYLKESKGSKRWLIFLEGGWYCFNKENCDSRYETMRRLMSSSKWPQTKTGTGMLSSLPEENPHWWNANMVFIPYCSSDVWSGASPKTDQNDYAFMGSLIIKEVVKDLLSKGLDNAKILLLAGSSAGGTGVLLNVDSVSELLEELGHTNIQVRGLSDSGWFLDNKQYRCTDCVDTINCAPTEVIKRGIKYWGGVVPERCRQAYEGKEWNCFFGYKVYPTIKRPVFIVQWLFDEAQLTVDNIHLTGQPVQEGQWRYIQNLGTELRNTLKDVPAMFAPACLSHEFITRNYWTDVQVKGTSLPRALHCWDRSLQDTSRNNKSPPKGCPVHLIDSCPWPHCNPTCPTIRDQSTGQEMNVIQFLMHMGFDVQKMAHQQGMDPSKLLGMLSSGS | Function: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway . Acts by specifically mediating depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors (By similarity).
Catalytic Activity: [Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + H2O = (9Z)-hexadecenoate + [Wnt protein]-L-serine + H(+)
Sequence Mass (Da): 56715
Sequence Length: 500
Subcellular Location: Secreted
EC: 3.1.1.98
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Q8IUM7 | MYRSTKGASKARRDQINAEIRNLKELLPLAEADKVRLSYLHIMSLACIYTRKGVFFAGGTPLAGPTGLLSAQELEDIVAALPGFLLVFTAEGKLLYLSESVSEHLGHSMVDLVAQGDSIYDIIDPADHLTVRQQLTLPSALDTDRLFRCRFNTSKSLRRQSAGNKLVLIRGRFHAHPPGAYWAGNPVFTAFCAPLEPRPRPGPGPGPGPASLFLAMFQSRHAKDLALLDISESVLIYLGFERSELLCKSWYGLLHPEDLAHASAQHYRLLAESGDIQAEMVVRLQAKTGGWAWIYCLLYSEGPEGPITANNYPISDMEAWSLRQQLNSEDTQAAYVLGTPTMLPSFPENILSQEECSSTNPLFTAALGAPRSTSFPSAPELSVVSASEELPRPSKELDFSYLTFPSGPEPSLQAELSKDLVCTPPYTPHQPGGCAFLFSLHEPFQTHLPTPSSTLQEQLTPSTATFSDQLTPSSATFPDPLTSPLQGQLTETSVRSYEDQLTPCTSTFPDQLLPSTATFPEPLGSPAHEQLTPPSTAFQAHLDSPSQTFPEQLSPNPTKTYFAQEGCSFLYEKLPPSPSSPGNGDCTLLALAQLRGPLSVDVPLVPEGLLTPEASPVKQSFFHYSEKEQNEIDRLIQQISQLAQGMDRPFSAEAGTGGLEPLGGLEPLDSNLSLSGAGPPVLSLDLKPWKCQELDFLADPDNMFLEETPVEDIFMDLSTPDPSEEWGSGDPEAEGPGGAPSPCNNLSPEDHSFLEDLATYETAFETGVSAFPYDGFTDELHQLQSQVQDSFHEDGSGGEPTF | Function: Transcription factor expressed in neurons of the brain that regulates the excitatory-inhibitory balance within neural circuits and is required for contextual memory in the hippocampus (By similarity). Plays a key role in the structural and functional plasticity of neurons (By similarity). Acts as an early-response transcription factor in both excitatory and inhibitory neurons, where it induces distinct but overlapping sets of late-response genes in these two types of neurons, allowing the synapses that form on inhibitory and excitatory neurons to be modified by neuronal activity in a manner specific to their function within a circuit, thereby facilitating appropriate circuit responses to sensory experience (By similarity). In excitatory neurons, activates transcription of BDNF, which in turn controls the number of GABA-releasing synapses that form on excitatory neurons, thereby promoting an increased number of inhibitory synapses on excitatory neurons (By similarity). In inhibitory neurons, regulates a distinct set of target genes that serve to increase excitatory input onto somatostatin neurons, probably resulting in enhanced feedback inhibition within cortical circuits (By similarity). The excitatory and inhibitory balance in neurons affects a number of processes, such as short-term and long-term memory, acquisition of experience, fear memory, response to stress and social behavior (By similarity). Acts as a regulator of dendritic spine development in olfactory bulb granule cells in a sensory-experience-dependent manner by regulating expression of MDM2 (By similarity). Efficient DNA binding requires dimerization with another bHLH protein, such as ARNT, ARNT2 or BMAL1 . Can activate the CME (CNS midline enhancer) element .
PTM: Ubiquitinated, leading to degradation by the proteosome.
Sequence Mass (Da): 87117
Sequence Length: 802
Subcellular Location: Nucleus
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Q8BGD7 | MYRSTKGASKARRDQINAEIRNLKELLPLAEADKVRLSYLHIMSLACIYTRKGVFFAGGTPLAGPTGLLSAQELEDIVAALPGFLLVFTAEGKLLYLSESVSEHLGHSMVDLVAQGDSIYDIIDPADHLTVRQQLTMPSALDADRLFRCRFNTSKSLRRQSSGNKLVLIRGRFHAHPPGAYWAGNPVFTAFCAPLEPRPRPGPGPGPGPGPASLFLAMFQSRHAKDLALLDVSESVLIYLGFERSELLCKSWYGLLHPEDLAQASSQHYRLLAESGDIQAEMVVRLQAKHGGWTWIYCMLYSEGPEGPFTANNYPISDTEAWSLRQQLNSEDTQAAYVLGTPAVLPSFSENVFSQEQCSNPLFTPSLGTPRSASFPRAPELGVISTPEELPQPSKELDFSYLPFPARPEPSLQADLSKDLVCTPPYTPHQPGGCAFLFSLHEPFQTHLPPPSSSLQEQLTPSTVTFSEQLTPSSATFPDPLTSSLQGQLTESSARSFEDQLTPCTSSFPDQLLPSTATFPEPLGSPAHEQLTPPSTAFQAHLNSPSQTFPEQLSPNPTKTYFAQEGCSFLYEKLPPSPSSPGNGDCTLLALAQLRGPLSVDVPLVPEGLLTPEASPVKQSFFHYTEKEQNEIDRLIQQISQLAQGVDRPFSAEAGTGGLEPLGGLEPLNPNLSLSGAGPPVLSLDLKPWKCQELDFLVDPDNLFLEETPVEDIFMDLSTPDPNGEWGSGDPEAEVPGGTLSPCNNLSPEDHSFLEDLATYETAFETGVSTFPYEGFADELHQLQSQVQDSFHEDGSGGEPTF | Function: Transcription factor expressed in neurons of the brain that regulates the excitatory-inhibitory balance within neural circuits and is required for contextual memory in the hippocampus . Plays a key role in the structural and functional plasticity of neurons . Acts as an early-response transcription factor in both excitatory and inhibitory neurons, where it induces distinct but overlapping sets of late-response genes in these two types of neurons, allowing the synapses that form on inhibitory and excitatory neurons to be modified by neuronal activity in a manner specific to their function within a circuit, thereby facilitating appropriate circuit responses to sensory experience . In excitatory neurons, activates transcription of BDNF, which in turn controls the number of GABA-releasing synapses that form on excitatory neurons, thereby promoting an increased number of inhibitory synapses on excitatory neurons . In inhibitory neurons, regulates a distinct set of target genes that serve to increase excitatory input onto somatostatin neurons, probably resulting in enhanced feedback inhibition within cortical circuits . The excitatory and inhibitory balance in neurons affects a number of processes, such as short-term and long-term memory, acquisition of experience, fear memory, response to stress and social behavior . Acts as a regulator of dendritic spine development in olfactory bulb granule cells in a sensory-experience-dependent manner by regulating expression of MDM2 . Efficient DNA binding requires dimerization with another bHLH protein, such as ARNT, ARNT2 or BMAL1 . Can activate the CME (CNS midline enhancer) element .
PTM: Ubiquitinated, leading to degradation by the proteosome.
Sequence Mass (Da): 87286
Sequence Length: 802
Subcellular Location: Nucleus
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Q8MJV3 | MHNASYWGPERANTSCPAPAPTLGCPNASGPAPPLPPPLAVAVPVVYAVICAVGLAGNSAVLFVLLRAPRRKTVTNLFILNLAVADELFTLVPPVNIADFLLRRWPFGELLCKLVVAVDQYNTFSSLYFLTVMSADRYLVVLATAESRRVAGRTYGAARAVSLAVWGVATLVVLPFAVFARLDEEQGRRQCVLVFPQPEALWWRASRLYTLVLGFAIPVSTICVLYTSLLCRLRAIRLDSHAKALDRAKKRVTVLVVAILAVCLLVWTPYHLSTVVALTTDLPQTPLVIAVSYFITSLSYANSCLNPFLYAFLDDSFRRSLRQLLACRTTS | Function: Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36268
Sequence Length: 331
Subcellular Location: Cell membrane
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P48145 | MDNASFSEPWPANASGPDPALSCSNASTLAPLPAPLAVAVPVVYAVICAVGLAGNSAVLYVLLRAPRMKTVTNLFILNLAIADELFTLVLPINIADFLLRQWPFGELMCKLIVAIDQYNTFSSLYFLTVMSADRYLVVLATAESRRVAGRTYSAARAVSLAVWGIVTLVVLPFAVFARLDDEQGRRQCVLVFPQPEAFWWRASRLYTLVLGFAIPVSTICVLYTTLLCRLHAMRLDSHAKALERAKKRVTFLVVAILAVCLLCWTPYHLSTVVALTTDLPQTPLVIAISYFITSLSYANSCLNPFLYAFLDASFRRNLRQLITCRAAA | Function: Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals. Has a higher affinity for neuropeptide B.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36103
Sequence Length: 328
Subcellular Location: Cell membrane
|
Q8MJV2 | MMEATGLEGLESTSSPCPGSTGTGLSWDNGTRHNATFPEPLPALYVLLPVVYSVICAVGLVGNAAVICVILRAPKMKTVTHVFILNLAIADGLFTLVLPTNIAEHLLQRWPFGEVLCKLVLAIDHCNIFSSVYFLAAMSIDRYLVVLATARSRRMPRRTVHRAKVASLCVWLGVTVAVLPFLTFAGVYNNELQVTSCGLSFPRPERAWFQASRIYTLVLGFVVPMCTLCVLYADLLRRLRALRLHSGAKALGKAKRKVSLLVLAVLAVGLLCWTPFHLASIVALTTDLPQTPLVIIVSYVVTSLSYTSSCLNPFLYAFLDHSFRKSLRTACRCQGA | Function: Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36727
Sequence Length: 336
Subcellular Location: Cell membrane
|
P48146 | MQAAGHPEPLDSRGSFSLPTMGANVSQDNGTGHNATFSEPLPFLYVLLPAVYSGICAVGLTGNTAVILVILRAPKMKTVTNVFILNLAVADGLFTLVLPVNIAEHLLQYWPFGELLCKLVLAVDHYNIFSSIYFLAVMSVDRYLVVLATVRSRHMPWRTYRGAKVASLCVWLGVTVLVLPFFSFAGVYSNELQVPSCGLSFPWPEQVWFKASRVYTLVLGFVLPVCTICVLYTDLLRRLRAVRLRSGAKALGKARRKVTVLVLVVLAVCLLCWTPFHLASVVALTTDLPQTPLVISMSYVITSLSYANSCLNPFLYAFLDDNFRKNFRSILRC | Function: Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36861
Sequence Length: 333
Subcellular Location: Cell membrane
|
Q9GZQ6 | MEGEPSQPPNSSWPLSQNGTNTEATPATNLTFSSYYQHTSPVAAMFIVAYALIFLLCMVGNTLVCFIVLKNRHMHTVTNMFILNLAVSDLLVGIFCMPTTLVDNLITGWPFDNATCKMSGLVQGMSVSASVFTLVAIAVERFRCIVHPFREKLTLRKALVTIAVIWALALLIMCPSAVTLTVTREEHHFMVDARNRSYPLYSCWEAWPEKGMRRVYTTVLFSHIYLAPLALIVVMYARIARKLCQAPGPAPGGEEAADPRASRRRARVVHMLVMVALFFTLSWLPLWALLLLIDYGQLSAPQLHLVTVYAFPFAHWLAFFNSSANPIIYGYFNENFRRGFQAAFRARLCPRPSGSHKEAYSERPGGLLHRRVFVVVRPSDSGLPSESGPSSGAPRPGRLPLRNGRVAHHGLPREGPGCSHLPLTIPAWDI | Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47819
Sequence Length: 430
Subcellular Location: Cell membrane
|
Q9EP86 | MEAEPSQPPNGSWPLGQNGSDVETSMATSLTFSSYYQHSSPVAAMFIAAYVLIFLLCMVGNTLVCFIVLKNRHMRTVTNMFILNLAVSDLLVGIFCMPTTLVDNLITGWPFDNATCKMSGLVQGMSVSASVFTLVAIAVERFRCIVHPFREKLTLRKALFTIAVIWALALLIMCPSAVTLTVTREEHHFMLDARNRSYPLYSCWEAWPEKGMRKVYTAVLFAHIYLVPLALIVVMYVRIARKLCQAPGPARDTEEAVAEGGRTSRRRARVVHMLVMVALFFTLSWLPLWVLLLLIDYGELSELQLHLLSVYAFPLAHWLAFFHSSANPIIYGYFNENFRRGFQAAFRAQLCWPPWAAHKQAYSERPNRLLRRRVVVDVQPSDSGLPSESGPSSGVPGPGRLPLRNGRVAHQDGPGEGPGCNHMPLTIPAWNI | Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48324
Sequence Length: 432
Subcellular Location: Cell membrane
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Q9Y5X5 | MNSFFGTPAASWCLLESDVSSAPDKEAGRERRALSVQQRGGPAWSGSLEWSRQSAGDRRRLGLSRQTAKSSWSRSRDRTCCCRRAWWILVPAADRARRERFIMNEKWDTNSSENWHPIWNVNDTKHHLYSDINITYVNYYLHQPQVAAIFIISYFLIFFLCMMGNTVVCFIVMRNKHMHTVTNLFILNLAISDLLVGIFCMPITLLDNIIAGWPFGNTMCKISGLVQGISVAASVFTLVAIAVDRFQCVVYPFKPKLTIKTAFVIIMIIWVLAITIMSPSAVMLHVQEEKYYRVRLNSQNKTSPVYWCREDWPNQEMRKIYTTVLFANIYLAPLSLIVIMYGRIGISLFRAAVPHTGRKNQEQWHVVSRKKQKIIKMLLIVALLFILSWLPLWTLMMLSDYADLSPNELQIINIYIYPFAHWLAFGNSSVNPIIYGFFNENFRRGFQEAFQLQLCQKRAKPMEAYALKAKSHVLINTSNQLVQESTFQNPHGETLLYRKSAEKPQQELVMEELKETTNSSEI | Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60270
Sequence Length: 522
Subcellular Location: Cell membrane
|
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