wanglab/gogpt-training-data huggingface dataset:
Protein: Bud site selection protein 5 (P25300)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GDP-GTP exchange factor (GEF) for the small GTPase BUD1/RSR1. Regulates the activity of BUD1 together with BUD2 which is a GTPase-activating protein (GAP) of BUD1. Required to produce both the axial and bipolar patterns of bud site selection. Determines the orientation of division axis. Overexpression can suppress mutations in PRP20 which is the GEF for GSP1. May be a cytoplasmic GEF for GSP1. Might also act on the Ras-like protein CDC42. Appears to bind to Ras proteins but not to activate them.
Subcellular location: Bud neck. Cytoplasm, cell cortex. Note=In haploid cells, forms double rings that encircle the mother-bud neck and split upon cytokinesis, each progeny cell inheriting BUD5 at the axial division remnant. In diploid cells, localizes to the poles of the cell.
Interaction partners:
- Inhibitory regulator protein BUD2/CLA2
- Ras-related protein RSR1
- Axial budding pattern protein 2
- Bud emergence protein 1
- Bud site selection protein 9
- Bud site selection protein 4
- Bud site selection protein 3
- Putative protease AXL1
- Cell division control protein 42
- Bud site selection protein 8
Sequence:
MSPKNKYVYICVEYIYIYFAKIHKQSTLSSDTTKMFVLIDNVLAYLLEQDDLFVTARFAIQGQIVSRRVNKIHISNITDVLLQQFISHTLPYNDNIVPKKILDSMRTAVRQLLEATACVSRECPLVKRSQDIKRARKRLLSDWYRLGADANMDAVLLVVNSAWRFLAVWRPFVNSIQHATQELYQNIAHYLLHGNVNIQRVTALIQLVMGQDDLLFSMDDVLQEVFRIQLYLNKMLPHNSHKWQKPSPFDSANLLLNFRDWTTDNALLQELLLSYPTINKNKHKNHSVPRLIQIWVESYWQDSETTLKDILNFWYSHLAEYYEYQELFADIVQLFINKKRTRQLKIHYIGLTDKEIEENKPPLDYENLFLQYEIDKTNANDELCGATDLSDLLFQWKQGELLEVEAFALNVSPWSLAKTLTLLESSLYLDIETIEFTRHFKHNDTTIDSVFTLSNQLSSYVLETTLQQTHTISYWLQVALSCLYLRNLNSLASIITSLQNHSIERLSLPIDVKSDHLFQRLKVVVHPNNNYNVYRRTIKHIFHSQLPCVPFTSLLIRDITFIRDGNDTFTKDGNNVNMQKFNQITKIVAFAQYLQQKQYEDIHCSNTTARSLLGAMIKVHTLYNDNKDRAYQVSIAKVPRLT
Protein: Large ribosomal subunit protein eL15 (60S ribosomal protein L15) (Q86K01)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS10
- Small ribosomal subunit protein eS4
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS13
Sequence:
MGAYKYLQELYKKKQSDAVRFLLRVRCWEYRNLPVCHRASHPTRVDKARRLGYKATQGFVVYRIRVRRGGRKRQVPGGRTGGKPKTHGVNELKPSRNLRSVAEERVGRRCPNLRVLNSYWVNQDSTYKYYEVILVDNSHNAIRNDPRYNWICKPVHKHRELRGLTSAGIKARGLRRKGTHRASKTRPSRQANYKRRNTVVFHRYR
Protein: Thyroid receptor-interacting protein 6 (TR-interacting protein 6) (TRIP-6) (Zyxin-related protein 1) (ZRP-1) (Q9Z1Y4)
Organism: Mus musculus (Mouse)
Function: Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15654}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q15654}. Nucleus {ECO:0000250|UniProtKB:Q15654}. Cytoplasm {ECO:0000250|UniProtKB:Q15654}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with actin. {ECO:0000250|UniProtKB:Q15654}.
Interaction partners:
- Receptor-interacting serine/threonine-protein kinase 2
- Na
- Vinculin
- Breast cancer anti-estrogen resistance protein 1
- Lysophosphatidic acid receptor 2
Sequence:
MSGPTWLPPKQPEPSRLPQGRSLPRGALGPPTAHGATLQPHPRVNFCPLPPEHCYQPPGVPEDRGPTWVGSHGTPQRLQGLPPDRGIIRPGSLDAEIDSLTSMLADLDGGRSHAPRRPDRQAFEAPPPHAYRGGSLKPSGGAVPTPMLPASHYGGPTPASYATASTPAGPAFPVQVKVAQPVRGCGLPRRGASQASGPLPGPHFPLTGRGEVWGAGYRSHREPGPGVPEGPSGVHIPAGGGRGGGHEPQGPLGQPPEEELERLTKKLVHDMSHPPSGEYFGRCGGCGEDVVGDGAGVVALDRVFHIGCFVCSTCRAQLRGQHFYAVERRAYCESCYVATLEKCSTCSEPILDRILRAMGKAYHPGCFTCVVCHRGLDGIPFTVDATSQIHCIEDFHRKFAPRCSVCGGAIMPEPGQEETVRIVALDRSFHIGCYKCEECGLLLSSEGECQGCYPLDGHILCKACSAWRIQELSATVTTDC
Protein: Probable tubulin polyglutamylase ttll-15 (EC 6.-.-.-) (Tubulin--tyrosine ligase-like protein 15) (Q21279)
Organism: Caenorhabditis elegans
Function: Probable polyglutamylase that forms polyglutamate side chains on tubulin. Probably acts when complexed with other proteins. Appears to be dispensable for polar spindle formation in dividing embryonic cells, for cilia-dependent osmotic avoidance and for male mating behavior. Regulates microtubule dynamics in uterine muscle cells.
Interaction partners:
- Tubulin--tyrosine ligase-like protein 12
- Cytosolic carboxypeptidase 1
- Cytosolic carboxypeptidase 6
- Kinesin-like protein
Sequence:
MGLLDSKLCMMILAVSVLIIDINFEARIGTFFDLRLRTSYFKKSSSPLLSHTDSEEDLNYLSKHEDKRPVAIVTGSYESAHTGHMMHIREMFEHTGYKIVTKNELSLDTKWDVMWHHEYSFTQEPFKTLIKNASPNQIVNHVPGSGFYTSKVQLATSDLSNGVPKAFQLPAEKSKLLEYAEKNPDVLWVQKDNTHRNIKIKSTNDMDLSKNNSFVQKFVDNPLLIDNKKFDIGIYTVVTSLLPLRVYIYDGDVLIRFCPEDYHPFDANNVDKYVVGDDYTPIWEINSLKKYFNTQKMSFKSTIDSYLGMQGMDTSKIWLQIRNIIGEVFRTQQTKMLMSLQNLKLNPQYFELSRFDFVVDDQLNVFLMEANMSPNLSSGHFKQNQILYEQVLMNIFSLTGISTPITKEADILFKSRTSEQNPLVNSRDINLPLKFCVENKCESCDEAPECQLCGHCMNTETRKILEQTFVENSNRKQMKRIQFDYENHHPLTKEDHLLTLWLSTKCQLDNTWC
Protein: Carbonyl reductase [NADPH] 1 (EC 1.1.1.184) (15-hydroxyprostaglandin dehydrogenase [NADP(+)]) (EC 1.1.1.196, EC 1.1.1.197) (20-beta-hydroxysteroid dehydrogenase) (Alcohol dehydrogenase [NAD(P)+] CBR1) (EC 1.1.1.71) (NADPH-dependent carbonyl reductase 1) (Prostaglandin 9-ketoreductase) (PG-9-KR) (Prostaglandin-E(2) 9-reductase) (EC 1.1.1.189) (Short chain dehydrogenase/reductase family 21C member 1) (P16152)
Organism: Homo sapiens (Human)
Function: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E to prostaglandin F2-alpha (By similarity). Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. In addition, participates in the glucocorticoid metabolism by catalyzing the NADPH-dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF) or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1 and NR3C2 in adipose tissue.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Aldo-keto reductase family 1 member B1
- Carbonyl reductase 3
- Dihydrofolate reductase 2, mitochondrial
- Dihydrofolate reductase
- Sepiapterin reductase
- Aldo-keto reductase family 1 member C3
- Aldo-keto reductase family 1 member B10
- Cytochrome P450 3A4)
- Prostaglandin E synthase 3
- Prostaglandin E synthase
Sequence:
MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW
Protein: Uncharacterized protein (Q5AYK9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Phosphoribosylamine-glycine ligase
- Phosphoribosylaminoimidazole carboxylase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Hypothetical bifunctional AICARFT/IMPCHase bienzyme
- Adenylosuccinate synthetase
- Uncharacterized protein
- Multifunctional tryptophan biosynthesis protein
- Amidophosphoribosyltransferase
- Phosphoribosylformylglycinamidine synthase
- Outer spore wall protein RRT8
Sequence:
MFRLTQAACLLQALGALIQGSLAFTPAATDSHEAEALHRRSYFYVGGEYVNTTDGWMMHNQMYVEKLSPARGTTQLYPIVFLHGGAQTGTNFLNKPDGGRGWASWFLSHGYEVYIADRTMTARSPVLPADGYGESVFSAEFISQRFTNVQDYPLWPQAKLHSQWPGTGERGDPVFDAYYASNVQSISDSEAQEVTMKAAGEALLDIIGPVILITHSQGGLYGWSWADSRPELIKGLIQIEPKGPPFKEVIFSNSFSRPYGLTSIPLTYQPAPTNESSPLSMKTVSSDKPGELLDCIIQAEPARQLTNLAKVPILIDTGEASYHATYDYCFIKFLKQAGVSNVQHLELGKWGIHGNAHLQFLEKNSDVIAGVLHEWIGNVTALN
Protein: L-lactate dehydrogenase (EC 1.1.1.27) (A0A5F9ZHM4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDLXLVSSRL
Protein: Mitochondrial uncoupling protein 5 (AtPUMP5) (Mitochondrial dicarboxylate carrier 1) (Q9SJY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PUMPS are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. This leads to a decrease in the efficiency of oxidative phosphorylation and an increase in heat production. May be involved in protecting plant cells against oxidative stress damage. Recombinant PUMP5, reconstituted into liposomes, transports a wide range of dicarboxylic acids including malate, oxaloacetate and succinate as well as phosphate, sulfate and thiosulfate. However, it is unknown if these transports are of any biological significance in vivo.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- MJK13.9 protein family protein)
- Cytochrome b561 and DOMON domain-containing protein At3g25290
- Mitochondrial substrate carrier family protein
- Uncharacterized protein At1g23150
- At1g72820/F3N23_2
- Dicarboxylate transporter 1, chloroplastic
Sequence:
MGLKGFAEGGIASIVAGCSTHPLDLIKVRMQLQGESAPIQTNLRPALAFQTSTTVNAPPLRVGVIGVGSRLIREEGMRALFSGVSATVLRQTLYSTTRMGLYDIIKGEWTDPETKTMPLMKKIGAGAIAGAIGAAVGNPADVAMVRMQADGRLPLTDRRNYKSVLDAITQMIRGEGVTSLWRGSSLTINRAMLVTSSQLASYDSVKETILEKGLLKDGLGTHVSASFAAGFVASVASNPVDVIKTRVMNMKVVAGVAPPYKGAVDCALKTVKAEGIMSLYKGFIPTVSRQAPFTVVLFVTLEQVKKLFKDYDF
Protein: Autophagy-related protein 9 (C9JD65)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000256|ARBA:ARBA00004542}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004542}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004107}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}. Preautophagosomal structure membrane {ECO:0000256|ARBA:ARBA00004511, ECO:0000256|RuleBase:RU364027}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004511, ECO:0000256|RuleBase:RU364027}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
Sequence:
MVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLP
Protein: CWF19-like protein 2 (Q2TBE0)
Organism: Homo sapiens (Human)
Interaction partners:
- Pre-mRNA-processing factor 17
- Pre-mRNA-processing factor 19
- 116 kDa U5 small nuclear ribonucleoprotein component
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor SYF2
- Peptidyl-prolyl cis-trans isomerase-like 1
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing-splicing factor 8
- Pleiotropic regulator 1
- Protein BUD31 homolog
Sequence:
MATSMAAASGRFESAKSIEERKEQTRNARAEVLRQAKANFEKEERRKELKRLRGEDTWMLPDVNERIEQFSQEHSVKKKKKKDKHSKKAKKEKKKKSKKQKYEKNNESSDSSSSSEDEWVEAVPSQTPDKEKAWKVKDEKSGKDDTQIIKRDEWMTVDFMSVKTVSSSSLKAEKETMRKIEQEKNQALEQSKLMERELNPYWKDGGTGLPPEDCSVSSITKVSVVEDGGLSWLRKSYLRMKEQAEKQSRNFEDIVAERYGSMEIFQSKLEDAEKAASTKEDYRRERWRKPTYSDKAQNCQESRESDLVKYGNSSRDRYATTDTAKNSNNEKFIGDEKDKRPGSLETCRRESNPRQNQEFSFGNLRAKFLRPSDDEELSFHSKGRKFEPLSSSSALVAQGSLCSGFRKPTKNSEERLTSWSRSDGRGDKKHSNQKPSETSTDEHQHVPEDPREKSQDEVLRDDPPKKEHLRDTKSTFAGSPERESIHILSVDEKNKLGAKIIKAEMMGNMELAEQLKVQLEKANKFKETITQIPKKSGVENEDQQEVILVRTDQSGRVWPVNTPGKSLESQGGRRKRQMVSTHEERERVRYFHDDDNLSLNDLVKNEKMGTAENQNKLFMRMASKFMGKTDGDYYTLDDMFVSKAAERERLGEEEENQRKKAIAEHRSLAAQMEKCLYCFDSSQFPKHLIVAIGVKVYLCLPNVRSLTEGHCLIVPLQHHRAATLLDEDIWEEIQMFRKSLVKMFEDKGLDCIFLETNMSMKKQYHMVYECIPLPKEVGDMAPIYFKKAIMESDEEWSMNKKLIDLSSKDIRKSVPRGLPYFSVDFGLHGGFAHVIEDQHKFPHYFGKEIIGGMLDIEPRLWRKGIRESFEDQRKKALQFAQWWKPYDFTKSKNY
Protein: Galactolipid galactosyltransferase SFR2, chloroplastic (EC 2.4.1.184) (Galactolipid:galactolipid galactosyltransferase) (GGGT) (Protein SENSITIVE TO FREEZING 2) (AtSFR2) (Q93Y07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycosyl hydrolase family protein acting primarily as a highly specific galactosyltransferase. Synthesizes digalactosyldiacylglycerol from monogalactosyldiacylglycerol in the absence of UDP-galactose in vitro. Hydrolyzes o- and p-nitrophenyl beta-D-glucoside in vitro. Plays a role in freezing tolerance. May play a role in chloroplast protection.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:14600212}. Plastid, chloroplast outer membrane {ECO:0000269|PubMed:18466306, ECO:0000269|PubMed:25100720}; Single-pass type II membrane protein {ECO:0000269|PubMed:25100720}.
Interaction partners:
- Monogalactosyldiacylglycerol synthase 1, chloroplastic
- Digalactosyldiacylglycerol synthase 1, chloroplastic
- Monogalactosyldiacylglycerol synthase 2, chloroplastic
- Monogalactosyldiacylglycerol synthase 3, chloroplastic
- Digalactosyldiacylglycerol synthase 2, chloroplastic
- Alpha-galactosidase 1
- Alpha-galactosidase 3
- Alpha-galactosidase 2
- Outer envelope pore protein 37, chloroplastic
- Mediator of RNA polymerase II transcription subunit 16
Sequence:
MELFALLIKVAGLLATVTVGANVVSYSRFRRQNLAKFRSPIDESKEVLADFNSIEHEEGKFFFGLATAPAHAEDDLDDAWLQFAKETPCSAEEAEAADKKARRKKVKLAVGAITKGLAKNTHGKEDKNAADKPPSKNVAAWHNAPHAEDRLKFWSDPDKEVKLAKDTGVTVFRMGVDWSRIMPVEPTKGIKEAVNYEAVEHYKWILKKVRSNGMKVMLTLFHHSLPPWAADYGGWKMEKTVDYFMDFTRIVVDSMYDLVDSWVTFNEPHIFTMLTYMCGSWPGNNPDFLEIATSTLPMGVFHRALHWMAVAHSKAYDYIHGKISLKKPLVGVAHHVSFMRPYGLFDIGAVTISNSLTIFPYIDSICEKLDFIGINYYGQEAVCGAGLKLVETDEYSESGRGVYPDGLYRVLLMFHERYKHLKVPFIVTENGVSDETDVIRRPYLIEHLLALYAAMLKGVPVLGYIFWTISDNWEWADGYGPKFGLVAVDRSHDLARTLRQSYHLFSKIVKSGKVTRKDRSLAWNELQKAAKAGKLRPFYRGVDNHNLMYADGLDKPQWRPFVDRDWRFGHYQMDGLQDPLSRVARTLLIWPLIMKKRIRKVKIKHTDDAGLVLHPALASPFD
Protein: LD42159p (Receptor expression enhancing protein A, isoform D) (Q8SX60)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRPIYQQEPPLFYQRPANLRRLRHPPGTVYGRSYSLEDQPEDVIPVYPKFIYAPQQQQQQQRAPYPLYQLGDSLSSLDSDFPENEYAGAYIVEDRVPLANAPTPKVVQNLNALGRMLELLQRCPLPCLSFNTACICSLIVIFLAPRTCAQSLLFPAFRLFCGTLYPAYASYKAVRTKDVKEYVKWMMYWIVFAFFTCIETFTDIFISWLPFYYEVKVALVFWLLSPATKGSSTLYRKFVHPMLTRHEQEIDEYVNQAKERGYSAVLQLGSKGVNYATNVLMQTAIKTYALTTAPSGHGRGLQNSHSADELYRGQDTMDSTENWLPRASSLSSIESYTETIYEPRTETKRLVIREVSEEAEFDDDPLGDAGAARLRDMPVRKAQPRRAASTAKAAGKRGQKHNDIEGARSSSSSSNVIRSRRKLREPTPDVDVENY
Protein: Frizzled-3 (Fz-3) (Xfz3) (O42579)
Organism: Xenopus laevis (African clawed frog)
Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activated by Wnt8. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Plays a role in controlling early axon growth and guidance processes necessary for the formation of a subset of central and peripheral major fiber tracts. Involved in the migration of cranial neural crest cells. May also be implicated in the transmission of sensory information from the trunk and limbs to the brain. Controls commissural sensory axons guidance after midline crossing along the anterior-posterior axis in the developing spinal cord in a Wnt-dependent signaling pathway. Together with FZD6, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle in a beta-catenin-dependent manner (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein. Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell surface {ECO:0000250|UniProtKB:Q61086}. Apical cell membrane {ECO:0000250|UniProtKB:Q61086}; Multi-pass membrane protein.
Interaction partners:
Sequence:
MAAYLISFIWVSVILAQKSMGHSLFACEPITLRMCQDLPYNSTFMPNLLNHYDQQTAALAMEPFHPMVNLECSRDLRPFLCALYTPVCMEYGRMTLPCRKLCQRAYNECFKLMEMFGVPWPEEMECSRFPDCDEPYPRIVDISLSGEPSEETPLAVQRDYGFWCPRELKIDPDLRSSFLGVRDCSPPCPHMYFRREELSFARYFIGVISIVCLSATLFTFLTFLIDVTRFRYPERPIIFYAVCYMMVSLIFFIGFLLEDKVACNGANPSQYKASTVTQGSHNKACTMLFMVLYFFTMAGSVWWVILTITWFLAAVPKWGSEAIEKKALLFHASAWGIPGTLTIILLAMNKIEGDNISGVCFVGLYDVHALRYFVLAPLCLDVVVGVSLLLAGIISLNRVRIEIPLEKENQDKLVKFMIRIGVFSILYLVPLLVVIGCYFYEQAYRGVWETTWVQERCREYHIPCPYKVTQTSRPDLILFLMKYLMLLVVGIPSVFWVGSKKTCFEWASFFHGRKKKAGVNESRQVLQEPDFAQSLLRDPNTPIVRKSRGTSTQGTSTHASSTQLAMLDDQRSKAGSVQSKVSSYHGSLHRSRDGRYTPCSYRGIEERLPHGSMSHLTDHSRHSSTHRLNEQSHQGSIRDLSNPLAHISHGTSMNRVIEADATSA
Protein: VIP peptides [Cleaved into: Intestinal peptide PHV-42; Intestinal peptide PHI-27 (Peptide histidine isoleucinamide 27); Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)] (P01283)
Organism: Rattus norvegicus (Rat)
Function: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.
Subcellular location: Secreted.
Interaction partners:
- Protachykinin-1
- Vasoactive intestinal polypeptide receptor 2
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Pro-neuropeptide Y
- Glucagon-like peptide 1 receptor
- Gastric inhibitory polypeptide receptor
- Adrenocorticotropic hormone receptor
- D
- 5-hydroxytryptamine receptor 4
- Atrial natriuretic peptide receptor 1
Sequence:
MESRSKPQFLAILTLFSVLFSQSLAWPLYGPPSSVRLDDRLQFEGAGDPDQVSLKADSDILQNALAENDTPYYDVSRNARHADGVFTSDYSRLLGQISAKKYLESLIGKRISSSISEDPVPVKRHSDAVFTDNYTRLRKQMAVKKYLNSILNGKRSSEGDSPDFLEELEK
Protein: Transmembrane protein 135 (Peroxisomal membrane protein 52) (PMP52) (Q5U4F4)
Organism: Rattus norvegicus (Rat)
Function: Involved in mitochondrial metabolism by regulating the balance between mitochondrial fusion and fission (By similarity). May act as a regulator of mitochondrial fission that promotes DNM1L-dependent fission through activation of DNM1L (By similarity). May be involved in peroxisome organization.
Subcellular location: Mitochondrion membrane {ECO:0000250|UniProtKB:Q9CYV5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9CYV5}. Peroxisome membrane {ECO:0000305|PubMed:17522052}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisomal membrane protein 4
Sequence:
MAALSKSIPHNCYEIGHTWNPSCRVSFLQITWGALEESLRIYAPLYLIAAVLRKRKLEYYLYKLLPEILQSASFLTANGALYITFFCVLRKILGKFYSWTPGFGAALPASYVAILIERKSRRGLLTIYMANLATETLFRMGVARGTITTLRNGEVLLFCITAAMYMFFFRCKDGLKGFTFSALRFIVGKEEIPTHSYSPETAYAKVEQKREKHRGTTRAMSLIALVRSLVDSICKHGPRHRCCKHYEDNCISYCIKGFIRMFSVGYLIQCCLRIPSAFRHLFTEPSRLLSLFYNKENFQLGAFLGSFVSIYKGTSCFLRWIRNLDDELHAIVAGFLAGVSMMFYKSTTISMYLASKLVETMYFKGIEAGKVPYFPQADTIIYSISTAICFHAAVMEVQNLRPSYWKFLLRLTKGRFALMNRKALDVFGTGASREFHNFIPRLDPRYTVVTPELPIDFS
Protein: Pulmonary surfactant-associated protein A (PSAP) (PSP-A) (SP-A) (P35242)
Organism: Mus musculus (Mouse)
Function: In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration. Enhances the expression of MYO18A/SP-R210 on alveolar macrophages.
Subcellular location: Secreted {ECO:0000269|PubMed:31601679}. Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted, extracellular space, surface film {ECO:0000305}.
Interaction partners:
- Surfactant protein C
- Pulmonary surfactant-associated protein B
- Pulmonary surfactant-associated protein D
- Uteroglobin
- Secretoglobin family 3A member 2
- Advanced glycosylation end product-specific receptor
- Claudin-18
- Sodium-dependent phosphate transport protein 2B
- C-X-C motif chemokine 15
- Deleted in malignant brain tumors 1 protein
Sequence:
MSLGSLAFTLFLTVVAGIKCNGTEVCAGSPGIPGTPGNHGLPGRDGRDGIKGDPGPPGPMGPPGGMPGLPGRDGLPGAPGAPGEHGDKGEPGERGLPGFPAYLDEELQTASYEIKHQILQTMGVLSLQGSMLSVGDKVFSTNGQSVNFDTIREMCTRAGGHIAAPRNPEENEAIASITKKYNTYPYLGVIEGQTPGDFHYLDGASVNYTNWYPGEPRGRGKEKCVEMYTDGKWNDKGCLQYRLAICEF
Protein: Protein BEX2 (Brain-expressed X-linked protein 2 homolog) (Q3MKQ1)
Organism: Rattus norvegicus (Rat)
Function: Regulator of mitochondrial apoptosis and G1 cell cycle. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15958283}. Cytoplasm {ECO:0000269|PubMed:15958283}.
Interaction partners:
Sequence:
MESKVEQGVKNLNMENDHQEKEEKEEKPQDANKREPVVALPFEAGEYYVPRGSRRRFRVRQPIAHYRWDLMHRVGEPQGRMREENVQRFGEDMRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP
Protein: Flotillin (Q53HQ0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004543}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004543}. Membrane {ECO:0000256|RuleBase:RU366054}. Endosome {ECO:0000256|RuleBase:RU366054}.
Interaction partners:
Sequence:
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRVIMAHMTVGEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKRERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILTRLPESVERLTGVSISQVNHKPLRTA