wanglab/gogpt-training-data huggingface dataset:
Protein: Trimethylamine-N-oxide reductase 2 (TMAO reductase 2) (Trimethylamine oxidase 2) (EC 1.7.2.3) (P46923)
Organism: Escherichia coli (strain K12)
Function: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. Can also reduce other N- and S-oxide compounds such as 4-methylmorpholine-N-oxide and biotin sulfoxide (BSO), but with a lower catalytic efficiency.
Subcellular location: Periplasm {ECO:0000269|PubMed:11004177}.
Interaction partners:
- Cytochrome c-type protein TorY
- Cytochrome c-type protein TorC
- Chaperone protein TorD
- Trimethylamine-N-oxide reductase 1
Sequence:
MTLTRREFIKHSGIAAGALVVTSAAPLPAWAEEKGGKILTAGRWGAMNVEVKDGKIVSSTGALAKTIPNSLQSTAADQVHTTARIQHPMVRKSYLDNPLQPAKGRGEDTYVQVSWEQALKLIHEQHDRIRKANGPSAIFAGSYGWRSSGVLHKAQTLLQRYMNLAGGYSGHSGDYSTGAAQVIMPHVVGSVEVYEQQTSWPLILENSQVVVLWGMNPLNTLKIAWSSTDEQGLEYFHQLKKSGKPVIAIDPIRSETIEFFDDNATWIAPNMGTDVALMLGIAHTLMTQGKHDKVFLEKYTTGYPQFEEYLTGKSDNTPKSAVWAAEITGVPEAQIVKLAELMAANRTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGGFGFSYHYSNGGNPTRVGGVLPEMSAAIAGHASEAADDGGMTAIPVARIVDALENPGGKYQHNGKEQTYPNIKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTGDYSNQHIVPMKQAVAPQFEARNDFDVFADLAELLKPGGKEIYTEGKDEMAWLKFFYDAAQKGARAQRVTMPMFNAFWQQNKLIEMRHSEKNEQYVRYGDFRADPVKNALGTPSGKIEIYSKTLEKFGYKDCPAHPTWLAPDEWKGTADEKQLQLLTAHPAHRLHSQLNYAELRKKYAIADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEGAWPDLENGLCKNGSANVLTADIPSSQLANACAGNSALVYIEKYTGNAPKLTAFDQPAVQA
Protein: Neuropeptide CCHamide-2 receptor (Q4V622)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for the neuropeptide CCHamide-2.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuropeptide CCHamide-1 receptor
- Neuropeptide CCHamide-2
Sequence:
MYASLMDVGQTLAARLADSDGNGANDSGLLATGQGLEQEQEGLALDMGHNASADGGIVPYVPVLDRPETYIVTVLYTLIFIVGVLGNGTLVIIFFRHRSMRNIPNTYILSLALADLLVILVCVPVATIVYTQESWPFERNMCRISEFFKDISIGVSVFTLTALSGERYCAIVNPLRKLQTKPLTVFTAVMIWILAILLGMPSVLFSDIKSYPVFTATGNMTIEVCSPFRDPEYAKFMVAGKALVYYLLPLSIIGALYIMMAKRLHMSARNMPGEQQSMQSRTQARARLHVARMVVAFVVVFFICFFPYHVFELWYHFYPTAEEDFDEFWNVLRIVGFCTSFLNSCVNPVALYCVSGVFRQHFNRYLCCICVKRQPHLRQHSTATGMMDNTSVMSMRRSTYVGGTAGNLRASLHRNSNHGVGGAGGGVGGGVGSGRVGSFHRQDSMPLQHGNAHGGGAGGGSSGLGAGGRTAAVSEKSFINRYESGVMRY
Protein: Alpha-copaene synthase (EC 4.2.3.133) ((+)-delta-cadinene synthase) (EC 4.2.3.13) (Terpene synthase 1) (RcSeTPS1) (B9S9Z3)
Organism: Ricinus communis (Castor bean)
Function: Catalyzes the cyclization of farnesyl diphosphate to alpha-copaene and (+)-delta cadinene.
Interaction partners:
- Alpha-farnesene synthase
- Probable terpene synthase 4
- Probable terpene synthase 3
- Uncharacterized protein
- Farnesyl-pyrophosphate synthetase, putative
- Farnesyl-pyrophosphate synthetase, putative
- Geranyl geranyl pyrophosphate synthase, putative
- Geranyl geranyl pyrophosphate synthase, putative
- Geranyl geranyl pyrophosphate synthase, putative
- Geranyl geranyl pyrophosphate synthase, putative
Sequence:
MSLQVSAVPIKTSTQNATSAVKRHSSTYHPTIWGDHFLANLSHSKIIDGSIEQQFEGLKQKVRKMIIDLNNEPCKKLGLIDAVQRLGVGYHFKSEIEDVLQKVYHDYSDDEDDLNTVALRFRLLRQHGIKVSCAIFEKFKDSEGNFKTSLINDALGMLSLYEATHLSIRGEDVLDEALAFTTTNLQSVLPQLNTHLAAQISRALNRPIRKYLPRLEARNYIDIYATEESYNTTLLNFAKLDFNMLQELHQKELNVVTKWWKSLDVATKLPYARDRVVECYFWMVGVYFEPQYSFARIMMTKIIAITSLLDDTYDNYATGEELEILTEAIERWDIKAKDALPEYMKIIYTTLLDIYNEYEENIAKEEKSLLYSVYYAKEVMKRVVRAYLAEVRWRDNCYTPTMEEYMQSALLTTCSPMLAIASFLGLKEIATKEAYEWASEDPKIIRASSIVCRLMDDIVSHEFEQTRKHVASGVECYIKQYGASEEEVIKLFRKEVTNAWKDLNEECLNPTPVPMPMLERVVNLTRAIDVIYKDDDGYTNSHIMKDYVASVLKDPVPV
Protein: Cyclin D binding myb like transcription factor 1 (J3QKU5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
PEHLLNTSDNVTVQCHTPRVIIQTVATEDITSSISQAELTVDSDIQSSDFPEPPDALEADTFPDEIHHPKMTVEPSFNDAHVSKFSDQNSTELMNSVMVRTEEEISDTDLKQEESPSDLASAYVTEGLESPTIEEQVDQTIDDETILIVPSPHGFIQASDVIDTESVLPLTTLTGTVI
Protein: DNA methyltransferase 1-associated protein 1 (DNMAP1) (DNMT1-associated protein 1) (MAT1-mediated transcriptional repressor) (Q9JI44)
Organism: Mus musculus (Mouse)
Function: Involved in transcription repression and activation. Its interaction with HDAC2 may provide a mechanism for histone deacetylation in heterochromatin following replication of DNA at late firing origins. Can also repress transcription independently of histone deacetylase activity. May specifically potentiate DAXX-mediated repression of glucocorticoid receptor-dependent transcription. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Participates in the nuclear localization of URI1 and increases its transcriptional corepressor activity (By similarity).
Subcellular location: Nucleus. Cytoplasm {ECO:0000250}. Note=Targeted to replication foci throughout S phase by DNMT1.
Interaction partners:
- Transformation/transcription domain-associated protein
- YEATS domain-containing protein 4
- RuvB-like 1
- RuvB-like 2
- DNA
- Actin-like protein 6A
- E1A-binding protein p400
- MRG/MORF4L-binding protein
- Bromodomain-containing protein 8
- Enhancer of polycomb homolog 2
Sequence:
MATGADVRDILELGGPEGDAASGTISKKDIINPDKKKSKKSSETLTFKRPEGMHREVYALLYSDKKDAPPLLPSDTGQGYRTVKAKLGSKKVRPWKWMPFTNPARKDGAMFFHWRRAAEEGKDYPFARFNKTVQVPVYSEQEYQLYLHDDAWTKAETDHLFDLSRRFDLRFVVIHDRYDHQQFKKRSVEDLKERYYHICAKLANVRAVPGTDLKIPVFDAGHERRRKEQLERLYNRTPEQVAEEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAEKPAVPETAGIKFPDFKSAGVTLRSQRMKLPSSVGQKKIKALEQMLLELGVELSPTPTEELVHMFNELRSDLVLLYELKQACANCEYELQMLRHRHEALARAGVLGAPAAAAVGPTPASAEPTVSESGLGLDPTKDTIIDVVGAPLTPNSRKRRESASSSSSVKKAKKP
Protein: Armadillo repeat-containing protein 10 (Q9D0L7)
Organism: Mus musculus (Mouse)
Function: May play a role in cell survival and cell growth. May suppress the transcriptional activity of p53/TP53 (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N2F6}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8N2F6}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGGARDVGWVAAGLVLGAGACYCIYRLTRGPRRGGRRLRPSRSAEDLTDGSYDDILNAEQLKKLLYLLESTDDPVITEKALVTLGNNAAFSTNQAIIRELGGIPIVGNKINSLNQSIKEKALNALNNLSVNVENQTKIKIYVPQVCEDVFADPLNSAVQLAGLRLLTNMTVTNDYQHLLSGSVAGLFHLLLLGNGSTKVQVLKLLLNLSENPAMTEGLLSVQVDSSFLSLYDGQVANEILLRALTLFQNINNCLKVEGRLANQIPFAKGSLFFLLYGEECAQKMRALACHHDVDVKEKALAIKPKF
Protein: Fatty acid desaturase 3 (FADS3) (EC 1.14.19.-) (Delta(13) fatty acid desaturase) (Delta(13) desaturase) (Q9Y5Q0)
Organism: Homo sapiens (Human)
Function: Mammals have different sphingoid bases that differ in their length and/or pattern of desaturation and hydroxyl groups. The predominant sphingoid base in mammalian ceramides is sphing-4-enine (sphingosine or SPH) which has a trans desaturation at carbon 4. FADS3 is a ceramide desaturase that introduces a cis double bond between carbon 14 and carbon 15 of the SPH-containing ceramides, producing sphinga-4,14-dienine-containing ceramides (SPD ceramides). SPD ceramides occur widely in mammalian tissues and cells. Due to their unusual structure containing a cis double bond, SPD ceramides may have an opposite, negative role in lipid microdomain formation relative to conventional ceramides. FADS3 also acts as a methyl-end fatty acyl coenzyme A (CoA) desaturase that introduces a cis double bond between the preexisting double bond and the terminal methyl group of the fatty acyl chain. Desaturates (11E)-octadecenoate (trans-vaccenoate, the predominant trans fatty acid in human milk) at carbon 13 to generate (11E,13Z)-octadecadienoate (also known as conjugated linoleic acid 11E,13Z-CLA).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31916624}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Stearoyl-CoA desaturase
- Cytochrome b5 type B
Sequence:
MGGVGEPGPREGPAQPGAPLPTFCWEQIRAHDQPGDKWLVIERRVYDISRWAQRHPGGSRLIGHHGAEDATDAFRAFHQDLNFVRKFLQPLLIGELAPEEPSQDGPLNAQLVEDFRALHQAAEDMKLFDASPTFFAFLLGHILAMEVLAWLLIYLLGPGWVPSALAAFILAISQAQSWCLQHDLGHASIFKKSWWNHVAQKFVMGQLKGFSAHWWNFRHFQHHAKPNIFHKDPDVTVAPVFLLGESSVEYGKKKRRYLPYNQQHLYFFLIGPPLLTLVNFEVENLAYMLVCMQWADLLWAASFYARFFLSYLPFYGVPGVLLFFVAVRVLESHWFVWITQMNHIPKEIGHEKHRDWVSSQLAATCNVEPSLFTNWFSGHLNFQIEHHLFPRMPRHNYSRVAPLVKSLCAKHGLSYEVKPFLTALVDIVRSLKKSGDIWLDAYLHQ
Protein: NAD-specific glutamate dehydrogenase (NAD-GDH) (EC 1.4.1.2) (P28997)
Organism: Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus)
Interaction partners:
Sequence:
MTDTLNPLVAAQEKVRIACEKLGCDPAVYELLKEPQRVIEISIPVKMDDGTVKVFKGWRSAHSSAVGPSKGGVRFHPNVNMDEVKALSLWMTFKGGALGLPYGGGKGGICVDPAELSERELEQLSRGWVRGLYKYLGDRIDIPAPDVNTNGQIMSWFVDEYVKLNGERMDIGTFTGKPVAFGGSEGRNEATGFGVAVVVRESAKRFGIKMEDAKIAVQGFGNVGTFTVKNIERQGGKVCAIAEWDRNEGNYALYNENGIDFKELLAYKEANKTLIGFPGAERITDEEFWTKEYDIIVPAALENVITGERAKTINAKLVCEAANGPTTPEGDKVLTERGINLTPDILTNSGGVLVSYYEWVQNQYGYYWTEAEVEEKQEADMMKAIKGVFAVADEYNVTLREAVYMYAIKSIDVAMKLRGWY
Protein: Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial (EC 1.4.7.1) (Fd-GOGAT 1) (Q9ZNZ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in glutamate biosynthesis in leaf. Required for the reassimilation of ammonium ions generated during photorespiration.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19223513}. Mitochondrion matrix {ECO:0000269|PubMed:19223513}. Note=Dual targeting is supposed to depend on alternative initiation: Met-1 or Met-3 for chloroplast or mitochondrion location, respectively. {ECO:0000269|PubMed:19223513}.
Interaction partners:
- Glutamine synthetase, chloroplastic/mitochondrial
- Glutamate dehydrogenase 2
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- glutamate dehydrogenase
- Glutamate dehydrogenase 1
- Glutamine synthetase cytosolic isozyme 1-1
- Glutamine synthetase cytosolic isozyme 1-4
- Glutamine synthetase cytosolic isozyme 1-3
- Glutamine synthetase cytosolic isozyme 1-2
- Glutamine synthetase cytosolic isozyme 1-5
Sequence:
MAMQSLSPVPKLLSTTPSSVLSSDKNFFFVDFVGLYCKSKRTRRRLRGDSSSSSRSSSSLSRLSSVRAVIDLERVHGVSEKDLSSPSALRPQVANLEDILSERGACGVGFIANLDNIPSHGVVKDALIALGCMEHRGGCGADNDSGDGSGLMSSIPWDFFNVWAKEQSLAPFDKLHTGVGMIFLPQDDTFMQEAKQVIENIFEKEGLQVLGWREVPVNVPIVGKNARETMPNIQQVFVKIAKEDSTDDIERELYICRKLIERAVATESWGTELYFCSLSNQTIVYKGMLRSEALGLFYLDLQNELYESPFAIYHRRYSTNTSPRWPLAQPMRFLGHNGEINTIQGNLNWMQSREASLKAAVWNGRENEIRPFGNPRGSDSANLDSAAEIMIRSGRTPEEALMILVPEAYKNHPTLSVKYPEVVDFYDYYKGQMEAWDGPALLLFSDGKTVGACLDRNGLRPARYWRTSDNFVYVASEVGVVPVDEAKVTMKGRLGPGMMIAVDLVNGQVYENTEVKKRISSFNPYGKWIKENSRFLKPVNFKSSTVMENEEILRSQQAFGYSSEDVQMVIESMASQGKEPTFCMGDDIPLAGLSQRPHMLYDYFKQRFAQVTNPAIDPLREGLVMSLEVNIGKRGNILELGPENASQVILSNPVLNEGALEELMKDQYLKPKVLSTYFDIRKGVEGSLQKALYYLCEAADDAVRSGSQLLVLSDRSDRLEPTRPSIPIMLAVGAVHQHLIQNGLRMSASIVADTAQCFSTHHFACLVGYGASAVCPYLALETCRQWRLSNKTVAFMRNGKIPTVTIEQAQKNYTKAVNAGLLKILSKMGISLLSSYCGAQIFEIYGLGQDVVDLAFTGSVSKISGLTFDELARETLSFWVKAFSEDTTKRLENFGFIQFRPGGEYHSNNPEMSKLLHKAVREKSETAYAVYQQHLSNRPVNVLRDLLEFKSDRAPIPVGKVEPAVAIVQRFCTGGMSLGAISRETHEAIAIAMNRIGGKSNSGEGGEDPIRWKPLTDVVDGYSPTLPHLKGLQNGDIATSAIKQVASGRFGVTPTFLVNADQLEIKVAQGAKPGEGGQLPGKKVSAYIARLRSSKPGVPLISPPPHHDIYSIEDLAQLIFDLHQINPNAKVSVKLVAEAGIGTVASGVAKGNADIIQISGHDGGTGASPISSIKHAGGPWELGLTETHQTLIANGLRERVILRVDGGLKSGVDVLMAAAMGADEYGFGSLAMIATGCVMARICHTNNCPVGVASQREELRARFPGVPGDLVNYFLYVAEEVRGILAQLGYNSLDDIIGRTELLRPRDISLVKTQHLDLSYLLSSVGTPSLSSTEIRKQEVHTNGPVLDDDILADPLVIDAIENEKVVEKTVKICNVDRAACGRVAGVIAKKYGDTGFAGQVNLTFLGSAGQSFGCFLIPGMNIRLIGESNDYVGKGMAGGEIVVTPVEKIGFVPEEATIVGNTCLYGATGGQIFARGKAGERFAVRNSLAEAVVEGTGDHCCEYMTGGCVVVLGKVGRNVAAGMTGGLAYLLDEDDTLLPKINREIVKIQRVTAPAGELQLKSLIEAHVEKTGSSKGATILNEWEKYLPLFWQLVPPSEEDTPEASAAYVRTSTGEVTFQSA
Protein: Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP) (Zipcode-binding protein 2) (Q8UVD9)
Organism: Gallus gallus (Chicken)
Function: Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs. Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Binds to a 54-nucleotide localization signal (the 'zipcode') found in the 3'-UTR of beta-actin mRNA and may play a role in its localization.
Subcellular location: Nucleus {ECO:0000269|PubMed:11781334}. Cytoplasm {ECO:0000269|PubMed:11781334}. Note=Predominantly nuclear.
Interaction partners:
Sequence:
MEISTPDFGFGTEDSSAQQSANRAIPQPVPAPAFPLKETASDTGGTAPTFGTLQDNINELCLRYQTVCSEGRDGTGGGGPPGGGIRKDAFADAVQRARQIAAKIGGDAATTVNNSTPDFGFGGQKRQLEDGDQPESKKLAAQGDCEYGPRGGAPAAPPERSGPVGDPPGPPRAERGRRPPPALTGGALPSAALPPQLGPMHPPPRSTTVTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGSPEAVQKAKLMLDDIVSRGRGGPPGQFHDYANGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMIFIQDGSQNTNVDKPLRIIGDPYKVQQACEMVMDILRERDQGGFGDRNEYGSRIGGGIDVPVPRHSVGVVIGRSGEMIKKIQNDAGVRIQFKQDDGTGPEKIAHIMGPPERCEHAARIINDLLQSLRSGPPGPPGHGMPPGGRGRGRGQGIWGPPGGEMTFSIPTHKCGLVIGRGGENVKAINQQRGAFVEISRQLPPNGDPNFKLFIIRGSPQQIEHAKQPIEEKIEGPLCPVGPGPGPGGPPGPAGPMGPFNPGPFNQGPPGGPPPHQYPPQGWGNTYPQWQPPAPHDPSKAAAAADPNAAWAGYYSHYYQQPPGPVPGQPPAPTAPPVQGEPPQPPPTGQSDYTKAWEEYYKKIGQQPQQPGAPPQQDYTKAWEEYYKKQAAQVATGGGPGAPPGPQPDYSAAWAEYYRQQAAYYGQTPGAAGPAPPPTQQGQQAQ
Protein: Glucose-regulated protein 78, putative (Q384Q5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Lipophosphoglycan biosynthetic protein, putative
- Pretranslocation protein, alpha subunit, putative
- Ribosomal protein L7Ae/L30e/S12e/Gadd45 domain-containing protein
- Protein disulfide isomerase
- Chaperone protein DNAJ, putative
- Chaperone protein DNAJ, putative
- Nucleotide exchange factor Fes1 domain-containing protein
- Calreticulin
- Calreticulin
Sequence:
MSRMWLTTAAVFLTVTVAAVSAAPESGGKVEAPCVGIDLGTTYSVVGVWQKGDVHIIPNEMGNRITPSVVAFTDTERLIGDGAKNQLPQNPHNTIYTIKRLIGRKYTDAAVQADKKLLSYEVIADRDGKPKVQVMVGGKKKQFTPEEISAMVLQKMKEIAETYLGEKVKNAVVTVPAYFNDAQRQSTKDAGTIAGLNVVRIINEPTAAAIAYGLNKAGEKNILVFDLGGGTFDVSLLTIDEGFFEVVATNGDTHLGGEDFDNNMMRHFVDMLKKKKNVDISKDQKALARLRKACEAAKRQLSSHPEARVEVDSLTEGFDFSEKITRAKFEELNMDLFKGTLVPVQRVLEDAKLKKSDIHEIVLVGGSTRVPKVQQLISDFFGGKELNRGINPDEAVAYGAAVQAAVLTGESEVGGRVVLVDVIPLSLGIETVGGVMTKLIERNTQIPTKKSQVFSTHADNQPGVLIQVYEGERQLTKDNRLLGKFELSGIPPAARGVPQIEVTFDVDENSILQVSAMDKSSGKKEEITITNDKGRLSEEEIERMVREAAEFEDEDRKVRERVDARNSLESVAYSLRNQVNDKDKLGGKLDPNDKAAVETAVAEAIRFLDENPNAEKEEYKTALETLQSVTNPIIQKTYQSAGGGDKPQPMDDL
Protein: Reticulon-4 receptor-like 2 (Nogo receptor-like 3) (Nogo-66 receptor homolog 1) (Nogo-66 receptor-related protein 2) (NgR2) (Q7M6Z0)
Organism: Mus musculus (Mouse)
Function: Cell surface receptor that plays a functionally redundant role in the inhibition of neurite outgrowth mediated by MAG (By similarity). Plays a functionally redundant role in postnatal brain development. Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum. Does not seem to play a significant role in regulating axon regeneration in the adult central nervous system. Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG. Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development. Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q86UN3}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q86UN3}. Membrane raft {ECO:0000250|UniProtKB:Q80WD1}. Cell projection, dendrite {ECO:0000269|PubMed:22325200}. Cell projection, axon {ECO:0000269|PubMed:22325200}. Perikaryon {ECO:0000250|UniProtKB:Q80WD1}. Note=Localized to the surface of neurons, including axons. Detected close to synapses, but is excluded from synapses. {ECO:0000269|PubMed:22325200}.
Interaction partners:
- Reticulon-4
- Myelin-associated glycoprotein
- Paired immunoglobulin-like receptor B
- Tumor necrosis factor receptor superfamily member 19
Sequence:
MLPGLRRLLQGPASACLLLTLLALPSVTPSCPMLCTCYSSPPTVSCQANNFSSVPLSLPPSTQRLFLQNNLIRSLRPGTFGPNLLTLWLFSNNLSTIHPGTFRHLQALEELDLGDNRHLRSLEPDTFQGLERLQSLHLYRCQLSSLPGNIFRGLVSLQYLYLQENSLLHLQDDLFADLANLSHLFLHGNRLRLLTEHVFRGLGSLDRLLLHGNRLQGVHRAAFHGLSRLTILYLFNNSLASLPGEALADLPALEFLRLNANPWACDCRARPLWAWFQRARVSSSDVTCATPPERQGRDLRALRDSDFQACPPPTPTRPGSRARGNSSSNHLYGVAEAGAPPADPSTLYRDLPAEDSRGRQGGDAPTEDDYWGGYGGEDQRGEQTCPGAACQAPADSRGPALSAGLRTPLLCLLPLALHHL
Protein: Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2 (EC 2.7.8.11) (Phosphatidylinositol synthase 2) (AtPIS2) (PI synthase 2) (PtdIns synthase 2) (Q8GUK6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta 1
- Phosphatidate cytidylyltransferase 4, chloroplastic
- Phosphatidate cytidylyltransferase 5, chloroplastic
- Phosphatidate cytidylyltransferase 2
- Phosphatidate cytidylyltransferase 3
- Phosphatidylinositol 4-kinase beta 2
- Phosphatase IMPL1, chloroplastic
- Phosphatidate cytidylyltransferase 1
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 2
- Phosphatidylinositol 4-kinase alpha 1
Sequence:
MAKQRPATLSVYLYIPNIVGYMRVLLNCIAFSVCFSNKTLFSLLYFFSFCCDAVDGWCARKFNQVSTFGAVLDMVTDRVSTACLLVILSQIYRPSLVFLSLLALDIASHWLQMYSTFLSGKTSHKDVKDSTSWLFRLYYGNRMFMGYCCVSCEVLYIILLLIATNQTENLMNVVVKSLMQISPLSLLLALSIFGWSIKQIINVIQMKTAADVCVLYDIEKQHKKP
Protein: Progonadoliberin-1 (Progonadoliberin I) [Cleaved into: Gonadoliberin-1 (Gonadoliberin I) (Gonadotropin-releasing hormone I) (GnRH-I) (Luliberin I) (Luteinizing hormone-releasing hormone I) (LH-RH I); Prolactin release-inhibiting factor 1 (Prolactin release-inhibiting factor I)] (P13562)
Organism: Mus musculus (Mouse)
Function: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones.
Subcellular location: Secreted {ECO:0000269|PubMed:37189369}.
Interaction partners:
- Gonadotropin-releasing hormone receptor
- Metastasis-suppressor KiSS-1
- RAC-alpha serine/threonine-protein kinase
- Mitogen-activated protein kinase 3
- KiSS-1 receptor
- Mitogen-activated protein kinase 1
- RAC-gamma serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- Tachykinin-3
- Oxytocin-neurophysin 1
Sequence:
MILKLMAGILLLTVCLEGCSSQHWSYGLRPGGKRNTEHLVESFQEMGKEVDQMAEPQHFECTVHWPRSPLRDLRGALESLIEEEARQKKM
Protein: MAGUK p55 subfamily member 3 (Discs large homolog 3) (Protein MPP3) (O88954)
Organism: Rattus norvegicus (Rat)
Function: Participates in cell spreading through the phosphoinositide-3-kinase (PI3K) pathway by connecting CADM1 to DLG1 and the regulatory subunit of phosphoinositide-3-kinase (PI3K) (By similarity). Stabilizes HTR2C at the plasma membrane and prevents its desensitization. May participates in the maintenance of adherens junctions (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:O88910}. Cell membrane {ECO:0000250|UniProtKB:Q13368}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q13368}. Note=Localized in apical villi of Mueller glia cells. Localized at the apical membrane in the developing cortex and colocalized with apical proteins and adherens junction proteins (By similarity). Localized at the outer limiting membrane (OLM), and outer plexiform (OPL) of retina (By similarity). {ECO:0000250|UniProtKB:O88910, ECO:0000250|UniProtKB:Q13368}.
Interaction partners:
Sequence:
MPVLSEDSGLHETLALLTSQLRPDSNHREEMGFLRDVFSEKSLGYLMKIHEKLRYYERQSPTPVLHSAMALAEDVMEELQAASVHSDERELLQLLSTPHLRAVLMVHDTVAQKNFDPVLPPLPDNIDEDFEEESVKIVRLVKNKEPLGATIRRDEHSGAVVVARIMRGGAADRSGLVHVGDELREVNGITVLHKRPDEISQILAQSQGSITLKIIPATQEEDRFKESKVFMRALFHYDPREDRAIPCQEAGLPFQQRQVLEVVSQDDPTWWQAKRVGDTNLRAGLIPSKQFQERRLSYRRTTGTIPSPQNLRKPLYDQPCDKETCDCDGYFKGHYVAGLRRSFRLGCRERLTGSQEVKVPVGAESQVLLTYEEVARYQHQPGERSRLVVLIGSLGAHLHELKQRVVAEDPQHFGVAVPHTTRPRKSHEREGVEYHFVSKQAFEADIQHNKFLEHGEHKENLYGTSLEAIQTVMAKNKVCLVDVEPEALRHLRTPEFKPYVIFVKPAIQEKRKTPPVSPDSEDPATPLDEQQQEMAASAAFIDQHYGHLIDTVLVRQDLQSVCSQLRAVIESLSKDTYWVPISWVR
Protein: Large ribosomal subunit protein eL34B (60S ribosomal protein L34-2) (60S ribosomal protein L34-B) (Q9URT8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL39
Sequence:
MAQRVTYRRRLAYNTRSNKTRIIKTPGNNIRYLHIKKLGTIPRCGDTGVPLQGIPALRPREFARLSHNQKKVQRAYGGCLSANAVKDRIVRAFLIEEQKIVKQKLKQMSQK
Protein: UDP-glycosyltransferase 73B1 (EC 2.4.1.-) (Q8VZE9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses low quercetin 3-O-glucosyltransferase and 7-O-glucosyltransferase activities in vitro.
Interaction partners:
- Cytochrome P450 71A21
Sequence:
MGTPVEVSKLHFLLFPFMAHGHMIPTLDMAKLFATKGAKSTILTTPLNAKLFFEKPIKSFNQDNPGLEDITIQILNFPCTELGLPDGCENTDFIFSTPDLNVGDLSQKFLLAMKYFEEPLEELLVTMRPDCLVGNMFFPWSTKVAEKFGVPRLVFHGTGYFSLCASHCIRLPKNVATSSEPFVIPDLPGDILITEEQVMETEEESVMGRFMKAIRDSERDSFGVLVNSFYELEQAYSDYFKSFVAKRAWHIGPLSLGNRKFEEKAERGKKASIDEHECLKWLDSKKCDSVIYMAFGTMSSFKNEQLIEIAAGLDMSGHDFVWVVNRKGSQVEKEDWLPEGFEEKTKGKGLIIRGWAPQVLILEHKAIGGFLTHCGWNSLLEGVAAGLPMVTWPVGAEQFYNEKLVTQVLKTGVSVGVKKMMQVVGDFISREKVEGAVREVMVGEERRKRAKELAEMAKNAVKEGGSSDLEVDRLMEELTLVKLQKEKV
Protein: Pentatricopeptide repeat-containing protein At1g06140, mitochondrial (Q9LND4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Phosphoglycerate mutase family protein
- Protein phosphatase EYA
- Transmembrane 9 superfamily member 7
- Mitochondrial uncoupling protein 3
- Transmembrane 9 superfamily member 12
Sequence:
MLPVNRARALLTILSQAKTLNHTQQVHAKVIIHGFEDEVVLGSSLTNAYIQSNRLDFATSSFNRIPCWKRNRHSWNTILSGYSKSKTCCYSDVLLLYNRMRRHCDGVDSFNLVFAIKACVGLGLLENGILIHGLAMKNGLDKDDYVAPSLVEMYAQLGTMESAQKVFDEIPVRNSVLWGVLMKGYLKYSKDPEVFRLFCLMRDTGLALDALTLICLVKACGNVFAGKVGKCVHGVSIRRSFIDQSDYLQASIIDMYVKCRLLDNARKLFETSVDRNVVMWTTLISGFAKCERAVEAFDLFRQMLRESILPNQCTLAAILVSCSSLGSLRHGKSVHGYMIRNGIEMDAVNFTSFIDMYARCGNIQMARTVFDMMPERNVISWSSMINAFGINGLFEEALDCFHKMKSQNVVPNSVTFVSLLSACSHSGNVKEGWKQFESMTRDYGVVPEEEHYACMVDLLGRAGEIGEAKSFIDNMPVKPMASAWGALLSACRIHKEVDLAGEIAEKLLSMEPEKSSVYVLLSNIYADAGMWEMVNCVRRKMGIKGYRKHVGQSATEVG
Protein: X globin (Xgb protein) (A3KNI8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGCAISGSGLTARAPEIRAGEEETPAGLTANHIRLIKESWRLIQEDIAKVGIIMFVRLFETHPECKDVFFLFRDVEDLERLRTSRELRAHGLRVMSFIEKSVARLDQLERLETLALELGKSHYRYNAPPKYYGYVGAEFICAVRPILKDRWTPELEEAWKTLFQYVTSIMREGFLEEERNKRSNTQTSSRERPDKRSTAI