wanglab/gogpt-training-data huggingface dataset:
Protein: 5'(3')-deoxyribonucleotidase, mitochondrial (5',3'-nucleotidase, mitochondrial) (EC 3.1.3.-) (Deoxy-5'-nucleotidase 2) (dNT-2) (Q8VCE6)
Organism: Mus musculus (Mouse)
Function: Dephosphorylates specifically the 5' and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- Cytosolic 5'-nucleotidase 1B
- Cytosolic 5'-nucleotidase 3A
- Cytosolic 5'-nucleotidase 1A
- Cytosolic purine 5'-nucleotidase
- Thymidylate kinase
- Deoxyguanosine kinase, mitochondrial
- Deoxycytidine kinase
- Thymidine phosphorylase
- UMP-CMP kinase 2, mitochondrial
Sequence:
MHRLRGCCARPRGAPLRAERSRASSRALRVLVDMDGVLADFEGGFLRKFRARFPDLPFVALEDRRGFWVSEQYGRLQPGLSEKAISIWESKDFFFELEPLPGAVEAVKQMANLQNTDVFICTSPIKMFKYCPYEKYAWVEKHFGPDFLEQIVLTRDKTVISADLLIDDRPDITGAEPHPSWEHILFTSCHNYHLQLQPPRRRLHSWADDWKAILDSKRLR
Protein: DNA polymerase (EC 2.7.7.7) (Q9HBN3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU366014}.
Interaction partners:
Sequence:
MEALCVCSLMPLHWSWILTASHLAAFFQGFRSLEDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRRGKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLPGPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNTHGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
Protein: Protein IMPACT (Imprinted and ancient gene protein) (O55091)
Organism: Mus musculus (Mouse)
Function: Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis. Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:23447528}.
Interaction partners:
- Stalled ribosome sensor GCN1
Sequence:
MAEEEVGNSQRQSEEIEAMAAIYGEEWCVIDENAKIFCIRVTDFMDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSLEEIYVHNMGESILYQWVEKIRDALIQKSQITEPDPDVKKKTEEVEVESEEDPILEHPPENPVKTLDLKISEETQPETEELPPVAHGVPITDRRSTFQAHVAPVVCPEQVKLVLAKLYENKKIASATHNIYAYRIFCEDKQTFLQDCEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNFTNTPDESTKNLGKKKVKKDKKKNDH
Protein: Peroxidase 2 (MsP2) (EC 1.11.1.-) (B0BK72)
Organism: Mycetinis scorodonius (Garlic mushroom) (Marasmius scorodonius)
Function: Peroxidase capable of degrading beta-carotene.
Interaction partners:
Sequence:
MRLTYLPLFAGIAIQSASALPDFFKSSVLKPRRTNSLLINPDAQPDLPTAQQASTAAASVGLNLTDIQGDILIGMKKNKEMFFFFSIADATAFKSHLDSAILPLITSTQQLLTVATQPTTAVNLAFSQTGLNALGLASQGLGDSLFASGQFSGAESLGDPGTSNWVQAFAGTGIHGVFLLASDTIDNVNAELSQIQSILGTSITEAYRLQGEARPDDQQGHEHFGFMDGISNPAIDGFSTALPGQAVLSPGLFLLAEDGDGSSSSRPSWAKDGSLLAFRQLQQRVPEFNKFLADNAALTQGNADLLGARMMGRWKSGAPVDLAPTADDVDLANDPQRNNNFNFTHPDFTETTDQTHCPFSAHIRKTNPRSDFNPLNTANHIIRAGIPYGPEVTDAEASSNTSSTDASLERGLAFVAYQSNIGNGFAFIQQNWVDNANFFFGKTTPPGIDPIIGSNAAQNNFAPNSPRPVSGLDPTDSTTIVTLNTDFVVSRGGEYFFSPSLSAIQNTLSV
Protein: Enoyl-[acyl-carrier-protein] reductase, mitochondrial (EC 1.3.1.104) (2-enoyl thioester reductase) (Nuclear receptor-binding factor 1) (BtNrbf-1) (NRBF-1) (Q7YS70)
Organism: Bos taurus (Bovine)
Function: Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Displays a preference for medium-chain over short- and long-chain substrates (By similarity). May provide the octanoyl chain used for lipoic acid biosynthesis, regulating protein lipoylation and mitochondrial respiratory activity particularly in Purkinje cells (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12654921}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Fatty acid synthase S-acetyltransferase; [Acyl-carrier-protein] S-malonyltransferase; 3-oxoacyl-[acyl-carrier-protein] synthase; 3-oxoacyl-[acyl-carrier-protein] reductase; 3-hydroxyacyl-[acyl-carrier-protein] dehydratase; Enoyl-[acyl-carrier-protein] reductase; Acyl-[acyl-carrier-protein] hydrolase]
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
- Acyl-coenzyme A oxidase
- Lipoyl amidotransferase LIPT1, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MWVCGALCRTRAPAQLGQRLLPESRRRRPASASFSASAEPSRVRALVYGHHGDPAKVVELKNLELAAVGGSHVHVKMLAAPINPSDINMIQGNYGLLPQLPAVGGNEGVGQVVAVGSGVTGVKPGDWVIPANPGLGTWRTEAVFGEEELITVPSDIPLQSAATLGVNPCTAYRMLVDFERLRPRDSIIQNASNSGVGQAVIQIAAARGLRTINVLRDTPDLQKLTDTLKNLGANHVVTEEELRKPEMKSFFKDVPQPRLALNCVGGKSSTELLRHLAPGGTMVTYGGMAKQPVIASVSQLIFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSEVPLQDYLCALEASTQPFVSSKQILTM
Protein: Renalase (EC 1.6.3.5) (Monoamine oxidase-C) (MAO-C) (Q5VYX0)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidation of the less abundant 1,2-dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis.
Subcellular location: Secreted {ECO:0000269|PubMed:15841207}.
Interaction partners:
- Plasma membrane calcium-transporting ATPase 4
- Amine oxidase [flavin-containing] B
Sequence:
MAQVLIVGAGMTGSLCAALLRRQTSGPLYLAVWDKAEDSGGRMTTACSPHNPQCTADLGAQYITCTPHYAKKHQRFYDELLAYGVLRPLSSPIEGMVMKEGDCNFVAPQGISSIIKHYLKESGAEVYFRHRVTQINLRDDKWEVSKQTGSPEQFDLIVLTMPVPEILQLQGDITTLISECQRQQLEAVSYSSRYALGLFYEAGTKIDVPWAGQYITSNPCIRFVSIDNKKRNIESSEIGPSLVIHTTVPFGVTYLEHSIEDVQELVFQQLENILPGLPQPIATKCQKWRHSQVTNAAANCPGQMTLHHKPFLACGGDGFTQSNFDGCITSALCVLEALKNYI
Protein: Dual specificity testis-specific protein kinase 1 (EC 2.7.12.1) (Testicular protein kinase 1) (Q15569)
Organism: Homo sapiens (Human)
Function: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues (By similarity). Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing microtubule breakdown via inhibition of TAOK1/MARKK kinase activity (By similarity). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Positively regulates integrin-mediated cell spreading, via phosphorylation of cofilin. Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1. Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15584898}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63572}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25849865}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q63572}. Note=Colocalizes with SPRY4 in vesicular spots in the cytoplasm (PubMed:15584898). Localized to F-actin-rich lamellipodia at the cell periphery following fibronectin-mediated cell adhesion of Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q63572, ECO:0000269|PubMed:15584898}.
Interaction partners:
- Alpha-parvin
- Protein sprouty homolog 4
Sequence:
MAGERPPLRGPGPGPGEVPGEGPPGPGGTGGGPGRGRPSSYRALRSAVSSLARVDDFHCAEKIGAGFFSEVYKVRHRQSGQVMVLKMNKLPSNRGNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIARGLRYLHSKGVFHRDLTSKNCLVRREDRGFTAVVGDFGLAEKIPVYREGARKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGIVLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGDDCPLPFLLLAIHCCNLEPSTRAPFTEITQHLEWILEQLPEPAPLTRTALTHNQGSVARGGPSATLPRPDPRLSRSRSDLFLPPSPESPPNWGDNLTRVNPFSLREDLRGGKIKLLDTPSKPVLPLVPPSPFPSTQLPLVTTPETLVQPGTPARRCRSLPSSPELPRRMETALPGPGPPAVGPSAEEKMECEGSSPEPEPPGPAPQLPLAVATDNFISTCSSASQPWSPRSGPVLNNNPPAVVVNSPQGWAGEPWNRAQHSLPRAAALERTEPSPPPSAPREPDEGLPCPGCCLGPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS
Protein: EMP1 trafficking protein-7 (O97336)
Organism: Plasmodium falciparum (isolate 3D7)
Function: During the asexual blood stage, plays an essential role in the recruitment and/or formation of EMP1-containing vesicles at the Maurer's clefts and their subsequent transfer to the host erythrocyte cell membrane.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:35930605}. Vesicle {ECO:0000269|PubMed:35930605}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Note=In the host erythrocyte cytoplasm, localizes to Maurer's clefts, chaperone-containing structures known as J-dots, and EMP1-containing electron dense vesicles (EDVs). {ECO:0000269|PubMed:35930605}.
Interaction partners:
Sequence:
MAKDSQKNLNVSNNNNVQCTMGRSSQNINKSDSKGKIKRCTYAYKILLCTIFIWICQCFYNKSYYVYKKDGRRNKGKKILGIRINKSLAEMDHTKYHPEYYDEVQENYDPYYGVNQYSDECESYKSEDDDSEEEYYNSTPRVTVLEPQTENSEDEENYEKTIVDELNELPNDKKALILSYIRNGNDNNMQLLPYANNNKQNTQENISRNKEFFRHFVDFIKGYKLFDSPVLNALLPFIFIAFVYCTITMLVGNVRYIIALYILAKILKMHYDYKHKENNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKKSKKN
Protein: Electron transfer flavoprotein regulatory factor 1 (Growth hormone-inducible soluble protein) (LYR motif-containing protein 5) (Q91V16)
Organism: Mus musculus (Mouse)
Function: Acts as a regulator of the electron transfer flavoprotein by promoting the removal of flavin from the ETF holoenzyme (composed of ETFA and ETFB).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q6IPR1}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- Electron transfer flavoprotein subunit alpha, mitochondrial
- LYR motif-containing protein 1
- LYR motif-containing protein 2
- LYR motif-containing protein 4
Sequence:
MANSLRGEVLTLYKNLLYLGRDYPKGADYFKRRLKNVFLKNKDVEDPEKIKELIARGEFVMKELEALYFLRKYRAMKQRYYSDTKV
Protein: RuvB-like helicase 2 (EC 3.6.4.12) (O94692)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes and is involved in DNA repair. Also involved in pre-rRNA processing (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- RuvB-like helicase 1
- Actin-like protein arp5
- Chromatin-remodeling complex subunit ies6
- TEL2-interacting protein 1
- Helicase swr1
- SWR1 complex subunit vps71
- Actin-like protein arp6
- Actin-related protein 4
- Probable actin-related protein 8
- SWR1-complex protein 4
Sequence:
MSISVTSHNDVSKLERIGAHSHIKGIGLNDNLEPKESSQGMVGQVKARRAAGVILKMIQEGRIAGRAILMAGPPSTGKTAIAMGMAQSLGSDTPFVTLSASEVYSLEMSKTEALLQALRKSIGVRIKEETEIIEGEVVEVQIDRSITGGNKQGKLTIRSTDMETVYDLGTKMIDSLTKEKVLAGDVISIDKSVGRVTKLGRSFSRARDYDAMGADTRFVQCPQGEIQKRKEVVHTVSLHDIDVINSRTQGFLALFSGDTGEIKPEVREQINTKVSEWREEGKAEIVPGVLFVDEVHMLDIECFSFFNRALEDDLAPIVIMASNRGITRIRGTNYRSPHGIPVDLLDRMLIISTLPYSHEEVKEILKIRCQEEDVDMEPSALDYLSTIGQETSLRYALLLISSSNQVALKRKSATIEESDIRRVYELFLDQKRSVEYLEEYGKNYITENEWSASGAQDNAVAMQED
Protein: Mitogen-activated protein kinase 9 (AtMPK9) (MAP kinase 9) (EC 2.7.11.24) (Q9LV37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- LRR receptor-like serine/threonine-protein kinase GHR1
- Guard cell S-type anion channel SLAC1
- Protein-tyrosine-phosphatase PTP1
- Uncharacterized protein
- Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein
- Dual specificity protein phosphatase 1B
Sequence:
MDPHKKVALETEFFTEYGEASRYQIQEVIGKGSYGVVASAIDTHSGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHVMLPPSRREFRDIYVVFELMESDLHQVIKANDDLTPEHYQFFLYQLLRGLKFIHTANVFHRDLKPKNILANSDCKLKICDFGLARVSFNDAPSAIFWTDYVATRWYRAPELCGSFFSKYTPAIDIWSIGCIFAEMLTGKPLFPGKNVVHQLDIMTDLLGTPPPEAIARIRNEKARRYLGNMRRKPPVPFTHKFPHVDPLALRLLHRLLAFDPKDRPSAEEALADPYFYGLANVDREPSTQPIPKLEFEFERRKITKEDVRELIYREILEYHPQMLQEYLRGGEQTSFMYPSGVDRFKRQFAHLEENYGKGEKGSPLQRQHASLPRERVPAPKKENGSHNHDIENRSIASLVTTLESPPTSQHEGSDYRNGTSQTGYSARSLLKSASISASKCIGMKPRNKSEYGESNNDTVDALSQKVAALHT
Protein: Cholesterol 25-hydroxylase (EC 1.14.99.38) (Cholesterol 25-monooxygenase) (h25OH) (O95992)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes. Plays a key role in cell positioning and movement in lymphoid tissues: 25-hydroxycholesterol is an intermediate in biosynthesis of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC), an oxysterol that acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (By similarity). May play an important role in regulating lipid metabolism by synthesizing a corepressor that blocks sterol regulatory element binding protein (SREBP) processing. As an interferon-stimulated gene, has broad antiviral activities against a wide range of enveloped viruses, such as vesicular stomatitis virus (VSV) and SARS coronavirus-2 (SARS-CoV-2). Its product, 25-hydroxycholesterol, activates the ER-localized enzyme ACAT to induce internalization of accessible cholesterol on the plasma membrane and restricts SARS-CoV-2 S protein-mediated fusion which inhibits virus replication. In testis, production of 25-hydroxycholesterol by macrophages plays a role in Leydig cell differentiation (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z0F5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z0F5}.
Interaction partners:
- Cytochrome P450 7B1
- Cytochrome P450 7A1
- Cholesterol 24-hydroxylase
- Lanosterol 14-alpha demethylase
- Squalene monooxygenase
- Lathosterol oxidase
- Sterol 26-hydroxylase, mitochondrial
- 7-dehydrocholesterol reductase
- Delta
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
Sequence:
MSCHNCSDPQVLCSSGQLFLQPLWDHLRSWEALLQSPFFPVIFSITTYVGFCLPFVVLDILCSWVPALRRYKIHPDFSPSAQQLLPCLGQTLYQHVMFVFPVTLLHWARSPALLPHEAPELLLLLHHILFCLLLFDMEFFVWHLLHHKVPWLYRTFHKVHHQNSSSFALATQYMSVWELFSLGFFDMMNVTLLGCHPLTTLTFHVVNIWLSVEDHSGYNFPWSTHRLVPFGWYGGVVHHDLHHSHFNCNFAPYFTHWDKILGTLRTASVPAR
Protein: Senescence/dehydration-associated protein At4g35985, chloroplastic (F4JNX2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Protein EARLY-RESPONSIVE TO DEHYDRATION 7
- Calmodulin-lysine N-methyltransferase
- Uncharacterized protein MHF15.4
- F14O23.23 protein
- Senescence/dehydration-associated protein At3g51250
- Spatacsin carboxy-terminus protein
- microtubule-severing ATPase
- At2g35290
- RING-H2 finger protein ATL72
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
Sequence:
MECSATPPKLYPTVDTSTTVAPLPKSSSSSSSTNNNNLYPSINVNDLVNNIFPDPTASDSASAPPLATEEVILTIHGAMVHLIDKSYSVELACGDLEILRLVQGDITVAVFARVGDEIQWPLTKDEPAVKVDESHYFFSLRPVKESESSDHSVNETENEMLNYGLTMASKGQEPMLEKLDKILADYSSFTAEEKQKEENVLDLTAAKETSPEELKGKRKKMVEKQCTAYWTTLAPNVEDYSGVAAKLIAAGSGQLIKGILWCGDLTMDRLMWGNDFMKKKLSKAEKERQVSPGTLKRLKRVKKMTKMTEKVANGVLSGVVKVSGFFSSSVINSKAGQKLFGLLPGEMVLATLDGFNKVCDAVEVAGRHVMKTTSDVTTEIVDHKYGAKTAQATNEGLSAAGHAFGTAWTVFKIRQALNPKSAMKPSSLAKTVVKTAAKERKKGKKSSK
Protein: Prostacyclin receptor (Prostaglandin I2 receptor) (E7FE45)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Major histocompatibility complex class I LIA
- Angiopoietin-like 1b.
- MANSC domain-containing 1.
- Guanine nucleotide-binding protein G
Sequence:
MLSNQSCENITSIEANGNPGTSTVMFIAGVVGNLIALAILGVHQKDRRTKSSVFCILVTGLALTDLLGTCLLSPPVFICYAYRTSLVGLTGDQRLCGLFAFAMTFFILASMLILCAMAVERCLAISHPYFYSKHVRRSFAKIVLLLIYLFTFVFCLMPFFGYGRHKQYCPGTWCFIKMEVEEGDDEERRSLAFSLSYAVLMALLIAIVFMCNGSVIVSLCRMHRSQLTRRGSVVSAGRKRRLSTWFGQGEEEMDHLLLLASMTLIFVICSLPLTICGFENAISPVGNDQRNLTAFRFSAFNPILDPWIFIIFRKAVFHHIRALFRCCFPREAVKTTAQSSQELKAEDIKHSSSIQSKIYHSLPQ
Protein: DUF3892 domain-containing protein (Q72P23)
Organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Interaction partners:
Sequence:
MSKNIKVTKESNTGLNKEFYDPSRGKSMTRGEFVEEIKNGKYPDYHVLDLEGKKIPRSNPDNSKRNNLG
Protein: LD05247p (Q7K2E1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glutamyl-tRNA
- Bifunctional glutamate/proline--tRNA ligase
- ZP domain-containing protein
- Uncharacterized protein, isoform D
- Curly Su
- Xaa-Pro dipeptidase
Sequence:
MAKSVPLTQAIGGYIFGILQACIRFVFRLIYGQKGESVPPITDAILLESATSLARKIRKQELSSVQVLESFIRRIKEVNPILNCVVDERYDQALKEAAEADALIKSGQYSTEELEKEKPFLGVPITTKDCISVKGMLHTAGLFERRDVRAARDADAMALMRKAGAIPIALTNVSEVCMWWESNNTVHGRTRNAYDTNRIVGGSSGGEGCIQSAAASAFGLGSDIGGSIRMPAFFNGIFGHKPSKLVVSNVGQFPAPFSAEQNSFLGLGPMSRFAEDLRPMLKIMAGEKAALLNLDEDVDLTKMKFFYQESDGGGRLVSAVDPDLREAMNRVAQHLREKFGNQKVERIQLPHFRQSAAIWFANMRDDSGHGFAYQLGNLNHDINTYLELFKWFFGASKHTFIGLSTAIMDSAQCKHGSPKYDHLVRKRNELREELQSLLGDNGVLIYPTHPTVAPYHNEPITRPINFAYTGIVNVLGFPATAVPLGKLGSEGLPLGVQIIANFNQDRLCLAVAEELERAFGGWAKPEVRL
Protein: FI04444p (Q9VMF0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Neural cell adhesion molecule 2
- MIP16756p
Sequence:
MVVIKNEQNISVPEYLNEHFFTETLEEGLRESKVTLKEINFAWGSNPGDNYCSAIYRVGVSFARWADGGESPVTEQLSLIVKTIPITEATQFLEDVCVFIKEKQTYTDVLPRLDILSRGDTFGAKYYHSVKTPVQTIVFSDLTVEGFKVASREKGLDWNHASLILQQLGKFHATSMVLAKKDPAIVKQYTRGMLSEDILMKSDTFEQMFGGFLKGLIKSSASWAGYEKISKHLQRLMDNFRNVCADAPRPRKGDRYVVLNHGDLWTNNFMYGYDNASQPDVPTRAIFVDFQLSFYGSPACDLNFFLNTSIKLQLLQERREELIKVYYASFKDALEYARFEDIPSYEDLQYELRSRETYGLFGMFAFLPMITMPKELAQDNSIENMQDEAFKQRKMDAIFSQKFLNDHQKWALKRADSLGVFGDY
Protein: Secretin receptor (SCT-R) (Q5FWI2)
Organism: Mus musculus (Mouse)
Function: Receptor for secretin (SCT), which is involved in different processes such as regulation of the pH of the duodenal content, food intake and water homeostasis. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Upon binding to secretin, regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas (By similarity). In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation. Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation. Also able to stimulate lipolysis in white adipocytes. Also plays an important role in cellular osmoregulation by regulating renal water reabsorption. Also plays a role in the central nervous system: required for synaptic plasticity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17283064}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47872}. Basolateral cell membrane {ECO:0000269|PubMed:17283064}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47872}. Note=In the renal medulla, localized on the basolateral membranes of cells in the collecting ducts. {ECO:0000269|PubMed:17283064}.
Interaction partners:
- Secretin
- Guanine nucleotide-binding protein G
- VIP peptides
- Pituitary adenylate cyclase-activating polypeptide
Sequence:
MLSTMSPRLSLLLLWLLLLINAAHPVGALPRLCDVRRVLLEERAECLRELSEEKKALGPKTASGCERFWDNMSCWPSSALAQTVEVPCPKFLRMFSGRNGSLFRNCTKDGWSETFPRPDLACGVNMNGSFNERRHAYLLKLKVMYTVGYSSSLAMLLVALSILCSFRRLHCTRNYIHMHLFVSFILRALSNFIKDAVLFPADDVTYCDAHRAGCKLVMIFFQYCIMANYAWLLVEGLYLHTLLAISFFSERKCLQAFVLFGWGSPAIFVALWAVTRHFLEDFGCWDINSNASIWWVIRGPVILSIVINFIFFINILRILMRKLRTQETRGNETHHYKRLAKSTLLLIPLFGIHYIVFAFSPEGAMEVQLFFELALGSFQGLVVAVLYCFLNGELEVQKKWRQWHLQEFPLRPVALSNSFSNATNGPTHSTKAGTSEQSRSIPGANVI
Protein: Metabotropic glutamate receptor 5 (mGluR5) (P31424)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. Plays an important role in the regulation of synaptic plasticity and the modulation of the neural network activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1320017}; Multi-pass membrane protein {ECO:0000269|PubMed:1320017}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Metabotropic glutamate receptor 1
- Muscarinic acetylcholine receptor M5
- Muscarinic acetylcholine receptor M1
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Muscarinic acetylcholine receptor M3
- Guanine nucleotide-binding protein subunit alpha-11
- Homer protein homolog 1
- Calcium/calmodulin-dependent protein kinase type II subunit delta
- Glutamate receptor ionotropic, NMDA 2B
Sequence:
MVLLLILSVLLLKEDVRGSAQSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLRSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNLRNPWFQEFWQHRFQCRLEGFAQENSKYNKTCNSSLTLRTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPIDGRKLLDSLMKTNFTGVSGDMILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDDEVWSKKNNIIRSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYVFDEYTCKACQLGSWPTDDLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLATLFVTVIFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCMFVPKVYIILAKPERNVRSAFTTSTVVRMHVGDGKSSSAASRSSSLVNLWKRRGSSGETLRYKDRRLAQHKSEIECFTPKGSMGNGGRATMSSSNGKSVTWAQNEKSTRGQHLWQRLSVHINKKENPNQTAVIKPFPKSTENRGPGAAAGGGSGPGVAGAGNAGCTATGGPEPPDAGPKALYDVAEAEESFPAAARPRSPSPISTLSHLAGSAGRTDDDAPSLHSETAARSSSSQGSLMEQISSVVTRFTANISELNSMMLSTAATPGPPGTPICSSYLIPKEIQLPTTMTTFAEIQPLPAIEVTGGAQGATGVSPAQETPTGAESAPGKPDLEELVALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL