wanglab/gogpt-training-data huggingface dataset:
Protein: L-threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) (L-threo-3-hydroxyaspartate dehydratase) (L-THA DH) (A4F2N8)
Organism: Pseudomonas sp
Function: Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threonine, L-threonine, D,L-allothreonine, D,L-threo-3-phenylserine, D-serine, and L-serine, are not substrates for this enzyme. Exhibits no detectable serine and aspartate racemase activity. Might play a role in the detoxification of naturally occurring 3-hydroxyaspartate in Pseudomonas sp. T62 cells.
Interaction partners:
Sequence:
MQLSSYHDVIKAAERLEGFANRTPVFTSRTLDAETGAQVFIKCENLQRTGSFKFRGAFNALSRFDEAQRKAGVVAFSSGNHAQGIALAARLLQMPATIVMPTDAPAAKVAATREYGATVVFYDRITEDREQIGRTLAEQHGMTLIPSYDHPDVLAGQGTAAKELLEFTGPLDALFVGLGGGGMLSGTALATRALSPDCLLYGVEPEAGNDGQRSFQTGSIVHIDTPATIADGAQTQHLGNHTFPIIRENVNDILTVSDAELVESMRFFMQRMKMVVEPTGCLGLAALRNLKQQFRGQRVGIIVTGGNVDIEKYASLLKG
Protein: glycerol kinase (EC 2.7.1.30) (Q9W0U0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glycerol-3-phosphate dehydrogenase
- glycerol kinase
- Glycerol-3-phosphate acyltransferase 4, isoform D
- Phospholipid/glycerol acyltransferase domain-containing protein
- BcDNA.GH07066
- LD24679p
- glycerol kinase
- AT10158p
- Glycerol-3-phosphate dehydrogenase
- AT18092p
Sequence:
MDSPTTETTPPPPTLSGPFVGAIDEGTTSARFIIFRAGTDEIVCFHQIEVESIFQKEGWCEQDPMAIVNTVNECITGACKKLVAVGGKVEEIITIGITNQRESTVVWDRNSGQPLVNAIIWLDNRTTSTVEELLETIPNNARNINYLRPLCGLPLSPYFSGVKLRWLRDNVPVVSQAMEKGTAMFGTIDTWLMYNLTGGKDCGVHKTDVTNASRTMLMNIETLQWDANLLKFFGLPKTILPEICSSSEFYGSIAQGVLQGIGITSVLGDQQAALVGQQCLAKGQAKATYGTGCFLLYNTGPSIVHSTHGLLTTVGYQLGRKAVPFYALEGSVSIAGAAFNWLRDNMNLIQNSGQIETMASTVDNSLDVYFVPAFNGLYAPYWNQDARGVICGLSEETTSEHIVRATLEAVCFQVRDILDSMHKDCKIPLAKLMVDGGMTVNNLFLQLQSDLVGIQVLRAKIAETTALGAAMAAYKAVENRYQMEAPLSKSGPREAIKPSISATDRNLRYQKWKMAIDRSLNWETSTLPQGEREAFDGA
Protein: Lysosomal phospholipase A and acyltransferase (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (1-O-acylceramide synthase) (ACS) (LCAT-like lysophospholipase) (LLPL) (EC 3.1.1.5) (Lysophospholipase 3) (Lysosomal phospholipase A2) (LPLA2) (Phospholipase A2 group XV) (Q8WMP9)
Organism: Bos taurus (Bovine)
Function: Has dual calcium-independent phospholipase and O-acyltransferase activities with a potential role in glycerophospholipid homeostasis and remodeling of acyl groups of lipophilic alcohols present in acidic cellular compartments. Catalyzes hydrolysis of the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group at the first carbon of lipophilic alcohols (O-acyltransferase activity). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines (By similarity). Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines and phosphatidylethanolamines (By similarity). Among preferred fatty acyl acceptors are natural lipophilic alcohols including short-chain ceramide N-acetyl-sphingosine (C2 ceramide), alkylacylglycerols, monoacylglycerols, and acylethanolamides such as anandamide and oleoylethanolamide (By similarity). Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized phospholipids and may play a role in detoxification of reactive oxidized phospholipids during oxidative stress. Required for normal phospholipid degradation in alveolar macrophages with potential implications in pulmonary surfactant clearance (By similarity). At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q6XPZ3}. Secreted {ECO:0000250|UniProtKB:Q8NCC3}. Membrane {ECO:0000250|UniProtKB:Q8NCC3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NCC3}.
Interaction partners:
- Acyl-protein thioesterase 1
- lysophospholipase
- lysophospholipase
- Acyl-protein thioesterase 1
- Phosphatidylcholine-sterol acyltransferase
- Glycerophosphocholine phosphodiesterase GPCPD1
- 85/88 kDa calcium-independent phospholipase A2
- Phospholipase A2
- Group 3 secretory phospholipase A2
- Cytosolic phospholipase A2
Sequence:
MGCLCLYRSTLLTGGLLFLLMLADPAFPAGSRPPVVLVPGDMGNQLEAKLDKPSVVHYVCSKRTDHYFTLWLNLELLLPVIIDCWIDNVRLIYNQTSHTTQFPEGVDVRVPGFGDTFSMEFLDPSKSSVGSYLHTMVESLVSWGYERGKDVRGAPYDWRRAPNENGPYFLALRKMIEEMYQLYGGPVVLVAHSMGNMYMLYFLQHQPQDWKDKYIRAFVALGPPWGGVPKTLRVLASGDNNRIPVIRSLKIRAQQRSAVSTTWLLPYSYTWSPQKVFVRTPKANYTLQDYRQFFQDIGFKDGWSMRQDTEGLVEATVPPGVRLHCLYGTGVPTPESFDYESFPDRDPKIHYGTGDGTVNLQSALHCHTWRGLQKQEVSLQALPGNEHIAMLANTTTLAYLKRVLLGP
Protein: Lupus La protein (La autoantigen) (La ribonucleoprotein) (Sjoegren syndrome type B antigen) (SS-B) (P05455)
Organism: Homo sapiens (Human)
Function: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. In case of Coxsackievirus B3 infection, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- E3 ubiquitin-protein ligase TRIM21
- RNA-binding protein RO60
- U1 small nuclear ribonucleoprotein 70 kDa
- Heterogeneous nuclear ribonucleoprotein A1
- ELAV-like protein 1
- Nucleolin
- Small nuclear ribonucleoprotein Sm D2
- Interleukin enhancer-binding factor 3
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Small nuclear ribonucleoprotein Sm D3
Sequence:
MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ
Protein: V-type proton ATPase subunit F (V-ATPase subunit F) (V-ATPase 14 kDa subunit) (Vacuolar proton pump subunit F) (Q9D1K2)
Organism: Mus musculus (Mouse)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P50408}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P50408}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit E 1
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit B, kidney isoform
Sequence:
MAGRGKLIAVIGDEDTVTGFLLGGIGELNKNRHPNFLVVEKDTTINEIEDTFRQFLNRDDIGIILINQYIAEMVRHALDAHQRSIPAVLEIPSKEHPYDAAKDSILRRAKGMFTAEDLR
Protein: RQC trigger complex subunit CUE3 (CUE domain-containing protein 3) (Coupling of ubiquitin conjugation to ER degradation protein 3) (P53137)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation. As part of the ribosome quality control trigger (RQT) complex, recognizes HEL2-dependent ubiquitination of RPS20 on stalled ribosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- RQC trigger complex helicase SLH1
- RQC trigger complex subunit RQT4
- Ribosome quality control complex subunit 2
- E3 ubiquitin-protein ligase HEL2
- ADP-ribosylation factor-binding protein GGA1
- Small ribosomal subunit protein uS10
- ATP-dependent DNA helicase MER3
- Small ribosomal subunit protein eS10A
- Small ribosomal subunit protein eS10B
- Endonuclease CUE2
Sequence:
MLSRYNRVIEINGGNADISLPIVKFPPFKLRAQLIEKDPVVWLHLIETYVTYFEYLMQGANVELLDESTLDHLRLFLRTYLHEIADEEGKLLSLGINHDVSEQLYLLKGWIFSLIKKCGLLHLQIFGDSLWNLIKVYVRRNPDSIRGLIDGSLKPRINTQRVQLDKSYQVQQHLKQLIESGKFKRIDLRCVEDLLSAKSMQPNKFAENFFTANWIEILEALWAKGQGRGHKEARELIIISLFSVSADRLLKITKELGISNFETLALYPLLGTMLINEGVHKRLPDLKSKLLFLNLGGLSMDEGDHMSYPTSSGTEVNEEQLSALMELFPQFSKYQLSQTLLAYDNNIELVTNKIFEDPTIIEAFSREPAEEEVEPVSDGDNASFTEELSILDRGDSSKNKELDKKIISEGVPDELRNKTLTRALKLLYEADEDERDDTYDEADVNRSDPSKRIGLQEDEESYDTKDDSNEVRQDHNYHIVEAYLWNLLKEDPKLFERSKRGTKVRKTMKEMTSWSDEKIEGWCRMLERSPTRARLLEKKFMFKGNSKTGKTSYVHNRDSQNDGNVVKEQAKQKKSENIKKHEPQSTEQKKRQHAKNEKRKGARANHNRKKGHDKKLARAGNNAI
Protein: Ras-related protein Ral-a (EC 3.6.5.2) (P48555)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P11233}; Lipid-anchor {ECO:0000250|UniProtKB:P11233}; Cytoplasmic side. Cleavage furrow {ECO:0000250|UniProtKB:P11233}. Midbody, Midbody ring {ECO:0000250|UniProtKB:P11233}.
Interaction partners:
- Exocyst complex component 2
- Ral guanine nucleotide dissociation stimulator-like, isoform E
- RalA-binding protein 1
- Exocyst complex component 8
- Exocyst complex component 7
- Raf homolog serine/threonine-protein kinase Raf
- Exocyst complex component 4
- non-specific serine/threonine protein kinase
- Neurofibromin 1, isoform B
Sequence:
MSKKPTAGPALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITDDESFQATQEFREQILRVKNDESIPFLLVGNKCDLNDKRKVPLSECQLRAQQWAVPYVETSAKTRENVDKVFFDLMREIRSRKTEDSKATSGRAKDRCKKRRLKCTLL
Protein: Uncharacterized protein, isoform G (A0A0B4KFZ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004283}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004283}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004283}.
Interaction partners:
Sequence:
MTVDFNDYFWGEKNNGYDVLYHNMKFGLIASKELSEFLREKSNIEEQNSKMMSKLAHKAGTLNSTFAPVWTILRTSAEKLSTLHLQMVQKLTELVKDVAKYADELHKKHKSVKEEESQTLECVQAIQTSTVAVQKLRDLYASKVQELEKLRKDNGSHKDAEKLESKLKKLQEEYKALLDKHNPIKNEFERRMTQTCKRFQEIEEVHLRQMKEFLSTYLEMLQNNHDMVGQVHSDFKRQFVDMSVDKLLEQFVLNKYTGLEKPEMPELEYVALSSGSRLQQPQVSASASNSNSATSIQAALRAGNAATTASGSAVSMDQRGDALAAISLGSGSAASGSIPFAEDPILGAMGSPRPTSPDMLAGANASGIQSQPTGGATSTVKSLRSWFLPTAKQQPSAGAGNFDQTQQQPAEALTPTASATAIAAASAPGKKQLNATTSEQQLSKSLNEQEHLQQTAAATAATTAAATTATTTTSRRATSLLNIFTSNSQVSGILRSRRDKTKTKKAKKKKDNEAAENIQEERLTSLDRGNNTLLDYDDHGRSMKTQNSSGSSAGGGLAALSVTSAQGSVDSAGASSMGGSGGAAVASGSLPNAGALTNSASITAPGAASGTGTGYEVDEEGFSIQPAKEIAWEEGQDKSGSFYSDSDTDSDNDKQERRIHVSIKPLKNGQAPMSASVDELRATVENISLSPTGVFSHHSQQLQAARGAPASRQQSPEISNASTPTASVHPYAPLQSPTLSNNNNANNTTNSRYADLGDIFSELGDMSMSAPSSATLGKPPGRQIPTPTSASTGGSIAIPRPPSRRSDMIAIGPAATGTAPGRGRMSPAPVTAMNRAESIGSLEFRTAIGGVGSSRGPSPLTIGISDTIPLAVAFHEIIHAYFRGSDESRCQVKVSGDMMLSFPAGIAGLLANNPNPAKLGFRIKHVQNLENLVPNGKLVQIDRQQSSSVSTMLEFNMGALTALLRRQAENNPTASYFNVDILKYQVRTKPGASSCPFQLVSYWKCESSYTALKVDYKYNNHAMASASPLLNVTLSVPVNGSVRNVQSKPHSAWLGESNRLVWNFTDISQNSQDGGVGTLRARLELNDGPSTPALLATQFNCEGTTLSGIEFELQGSGYRLSLVKRRFVSGKYVCEGDGIRSGATPTPPSVGSTSPYSAKSN
Protein: Bone marrow stromal antigen 2 (A0A024R7H5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ
Protein: dynamin GTPase (EC 3.6.5.5) (T1SXK0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGNRGMEELIPLINKLQDAFSSIGQSCNLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLVNNKAEYAEFLHCKGRKFVDFDEVRQEIEAETDRITGSNKGISPIPINLRVYSPNVLNLTLIDLPGMTKVAVGDQPPDIEHQIRDMIMQFITRESCLILAVTPANMDLANSDALKVAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIDGRKDIRAALAAERKFFLSHPSYRHMAERMGTPHLQKALNQQLTNHIRDTLPGLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKCIEGSGDQVDTAELSGGARINRIFHERFPFELVKIVFDEKELRREISHAIKNVHGVRTGLFTPDLAFEAIVKKQIIKLKEPCLKCIDLVIQELINTFRQCTNKLSSYPRLREETERIVTTYVREREGKTKDQVLLLIDTELSYINTNHEDFIGFANAQQRNIVNKKRAIPNQVIRKGWLTLNISIMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKLRDVEKGFMSTKHIFAIFNTEQRNVYKDLRQIELACDSQEDMDSWKASFLRAGVYPEKDQVESEEAAPADSFSMDPQLERQVETIRNLVDSYIGIVNKTIRDLMPKTIMHLMINSAKDFIHSELLAYLYSSGDQNSLMEESADQAQRRDEMLRMYHAIKEALSIIGDISTSTISTPVPPPVNDSWIPETSPTPQRRPPTSAPPPNRPPAVRGPTPGPPPLNPTPSFAAPPIPSRPGQPMNAFGNSSQDPFSAPPQIPSRPARIPPGVPSRRPPGAPNRPTIIRPAEPSLLD
Protein: Probable glycosyltransferase STELLO1 (EC 2.4.-.-) (O22943)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable glycosyltransferase regulating the assembly and trafficking of cellulose synthase complexes.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:27277162}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- NEDD8-like protein RUB3
- F12F1.16 protein
- Aconitate hydratase 2, mitochondrial
- Aconitate hydratase 3, mitochondrial
- Aconitase family protein
- Aconitate hydratase 1
- Serine/threonine-protein kinase STN8, chloroplastic
- NEDD8-activating enzyme E1 catalytic subunit
- Probable plastidic glucose transporter 3
- Serine/threonine-protein kinase STN7, chloroplastic
Sequence:
MLVQDRAAPSPAKPPKSQIRELPTHQQIRRRFSEPKNLDFSTWFSENLSRIAVFSLLIVTIVAFFFLYNTTDTASLLCFQSQSTQFLQSLSRPQIKWNSIPVVPDKTSPYANFQTEKWIVVSVTKYPTEELKSLVKIRGWQVLAIGNSATPKDWSLKGSIFLSLDAQAELGYRVLDHLPYDSFVRKSVGYLFAIQHGAKKIYDADDRGEVIDGDLGKHFDVELVGLDSKQEPILQYSHENPNRTVVNPYIHFGQRSVWPRGLPLENVGEINHEEYYTEVFGGKQFIQQGISNGLPDVDSVFYFTRKTTLEAFDIRFDEHSPKVALPQGVMVPVNSFNTLYHSSAFWGLMLPVSVSSMASDVLRGYWGQRLLWELGGYVAVYPPTAHRFDRIEAYPFVEEKDLHVNVGRLIKFLLAWRSEKHSFFETVLDLSFAMAEEGFWTEQDLKFTAAWLQDLIAVGYQQPRLMSLELDRPRASIGHGDRKEFVPRKLPSVHLGVEETGTVSTEIGNLIRWRKNFGNVVLVMFCNGPVERTALEWRLLYGRIFKTVVILSSQKNSDLYVEEAKLDHIYKHLPKIFDRYSSAEGFLFVEDDTVLNYWNLLQADKSKIWTTDKVSKSWTSVKPTGNSDWFSVQAELVKKTVSTMPAHFQVNYKDATKNNHETLTVCSSEVFYVPKRLVTDFIDLVDLVGDMDLHYKVAVPMFFLSMDSPQNFDPVLGSMVYKRKSASFNTSSSLYSAKAPAVHPWSISSEQDFIKLVQQMAEGDPLLMELV
Protein: Transient receptor potential cation channel subfamily M member 3 (Long transient receptor potential channel 3) (LTrpC-3) (LTrpC3) (Melastatin-2) (MLSN2) (Q9HCF6)
Organism: Homo sapiens (Human)
Function: Calcium channel mediating constitutive calcium ion entry. Its activity is increased by reduction in extracellular osmolarity, by store depletion and muscarinic receptor activation. In addition, forms heteromultimeric ion channels with TRPM1 which are permeable for calcium and zinc ions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12672827, ECO:0000305|PubMed:21278253}; Multi-pass membrane protein {ECO:0000250|UniProtKB:J9SQF3}.
Interaction partners:
- Guanine nucleotide-binding protein G
- ADP-ribose pyrophosphatase, mitochondrial
- Transient receptor potential cation channel subfamily V member 2
- Transient receptor potential cation channel subfamily A member 1
- Guanine nucleotide-binding protein G
- Transient receptor potential cation channel subfamily V member 1
- Transient receptor potential cation channel subfamily V member 4
- Transient receptor potential cation channel subfamily V member 3
- Polycystin-2
- Short transient receptor potential channel 1
Sequence:
MPEPWGTVYFLGIAQVFSFLFSWWNLEGVMNQADAPRPLNWTIRKLCHAAFLPSVRLLKAQKSWIERAFYKRECVHIIPSTKDPHRCCCGRLIGQHVGLTPSISVLQNEKNESRLSRNDIQSEKWSISKHTQLSPTDAFGTIEFQGGGHSNKAMYVRVSFDTKPDLLLHLMTKEWQLELPKLLISVHGGLQNFELQPKLKQVFGKGLIKAAMTTGAWIFTGGVNTGVIRHVGDALKDHASKSRGKICTIGIAPWGIVENQEDLIGRDVVRPYQTMSNPMSKLTVLNSMHSHFILADNGTTGKYGAEVKLRRQLEKHISLQKINTRCLPFFSLDSRLFYSFWGSCQLDSVGIGQGVPVVALIVEGGPNVISIVLEYLRDTPPVPVVVCDGSGRASDILAFGHKYSEEGGLINESLRDQLLVTIQKTFTYTRTQAQHLFIILMECMKKKELITVFRMGSEGHQDIDLAILTALLKGANASAPDQLSLALAWNRVDIARSQIFIYGQQWPVGSLEQAMLDALVLDRVDFVKLLIENGVSMHRFLTISRLEELYNTRHGPSNTLYHLVRDVKKGNLPPDYRISLIDIGLVIEYLMGGAYRCNYTRKRFRTLYHNLFGPKRPKALKLLGMEDDIPLRRGRKTTKKREEEVDIDLDDPEINHFPFPFHELMVWAVLMKRQKMALFFWQHGEEAMAKALVACKLCKAMAHEASENDMVDDISQELNHNSRDFGQLAVELLDQSYKQDEQLAMKLLTYELKNWSNATCLQLAVAAKHRDFIAHTCSQMLLTDMWMGRLRMRKNSGLKVILGILLPPSILSLEFKNKDDMPYMSQAQEIHLQEKEAEEPEKPTKEKEEEDMELTAMLGRNNGESSRKKDEEEVQSKHRLIPLGRKIYEFYNAPIVKFWFYTLAYIGYLMLFNYIVLVKMERWPSTQEWIVISYIFTLGIEKMREILMSEPGKLLQKVKVWLQEYWNVTDLIAILLFSVGMILRLQDQPFRSDGRVIYCVNIIYWYIRLLDIFGVNKYLGPYVMMIGKMMIDMMYFVIIMLVVLMSFGVARQAILFPNEEPSWKLAKNIFYMPYWMIYGEVFADQIDPPCGQNETREDGKIIQLPPCKTGAWIVPAIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIMTFHERPVLPPPLIIFSHMTMIFQHLCCRWRKHESDPDERDYGLKLFITDDELKKVHDFEEQCIEEYFREKDDRFNSSNDERIRVTSERVENMSMRLEEVNEREHSMKASLQTVDIRLAQLEDLIGRMATALERLTGLERAESNKIRSRTSSDCTDAAYIVRQSSFNSQEGNTFKLQESIDPAGEETMSPTSPTLMPRMRSHSFYSVNMKDKGGIEKLESIFKERSLSLHRATSSHSVAKEPKAPAAPANTLAIVPDSRRPSSCIDIYVSAMDELHCDIDPLDNSVNILGLGEPSFSTPVPSTAPSSSAYATLAPTDRPPSRSIDFEDITSMDTRSFSSDYTHLPECQNPWDSEPPMYHTIERSKSSRYLATTPFLLEEAPIVKSHSFMFSPSRSYYANFGVPVKTAEYTSITDCIDTRCVNAPQAIADRAAFPGGLGDKVEDLTCCHPEREAELSHPSSDSEENEAKGRRATIAISSQEGDNSERTLSNNITVPKIERANSYSAEEPSAPYAHTRKSFSISDKLDRQRNTASLRNPFQRSKSSKPEGRGDSLSMRRLSRTSAFQSFESKHN
Protein: Cysteinyl leukotriene receptor 1 (CysLTR1) (Cysteinyl leukotriene D4 receptor) (LTD4 receptor) (Q99JA4)
Organism: Mus musculus (Mouse)
Function: Receptor for cysteinyl leukotrienes mediating constriction of the microvascular smooth muscle during an inflammatory response. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTD4 >> LTE4 = LTC4 >> LTB4.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Cysteinyl leukotriene receptor 2
- Leukotriene C4 synthase
- Guanine nucleotide-binding protein G
- Uracil nucleotide/cysteinyl leukotriene receptor
- Polyunsaturated fatty acid 5-lipoxygenase
- Leukotriene B4 receptor 2
- Guanine nucleotide-binding protein subunit alpha-11
Sequence:
MYLQGTKQTFLENMNGTENLTTSLINNTCHDTIDEFRNQVYSTMYSVISVVGFFGNSFVLYVLIKTYHEKSAFQVYMINLAIADLLCVCTLPLRVVYYVHKGKWLFGDFLCRLTTYALYVNLYCSIFFMTAMSFFRCVAIVFPVQNINLVTQKKARFVCIGIWIFVILTSSPFLMYKSYQDEKNNTKCFEPPQNNQAKKYVLILHYVSLFFGFIIPFVTIIVCYTMIILTLLKNTMKKNMPSRRKAIGMIIVVTAAFLVSFMPYHIQRTIHLHLLHSETRPCDSVLRMQKSVVITLSLAASNCCFDPLLYFFSGGNFRRRLSTFRKHSLSSMTYVPKKKASLPEKGEEICNE
Protein: Probable eukaryotic translation initiation factor 5 (eIF-5) (Q09689)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]) (By similarity).
Interaction partners:
- Probable eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 2 subunit gamma
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 2 subunit alpha
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 5B
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit B
- Probable eukaryotic translation initiation factor 3 subunit J
Sequence:
MATINIRRDVKDSFYRYRMPKLQSKIEGKGNGIKTVIPNMSDIAKALGRPPLYVTKFFGFELGAQTTIIADMDRYIVNGAHDAGKLQDLLDVFIRRFVLCASCQNPETELSINKKDQTISYDCKACGYRGVIDGRHKLTGVIVKNPPAKKKSHKHKRDSPVAEEEDGAEDELTRRIRQEAAELPTAEVVNDEDWAVDTSEEAVRARVQELEGNMKDSLTLSDLRGDEEEAESSRYDQFGEWLEDNYPGVSDVEIYKKMKEENIHHKSKAIVVLVQCIITSPYVGEFEKHGALFKKLCTTDKHERALLGGFERLMENTELVHIDVVPKVLLEIYQNDLVSDDMFEKWGAKASKKYVSRETSKKIHEAAEPFLTWLAEASDESESEDEEEEEEDDDE
Protein: fructose-bisphosphate aldolase (EC 4.1.2.13) (H3BPS8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARRKPEGSSFNMTHLSMAMAFSFPPVASGQLHPQLGNTQHQTELGKELATTSTMPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYL
Protein: N-arachidonyl glycine receptor (NAGly receptor) (G-protein coupled receptor 18) (Q14330)
Organism: Homo sapiens (Human)
Function: Receptor for endocannabinoid N-arachidonyl glycine (NAGly). However, conflicting results about the role of NAGly as an agonist are reported. Can also be activated by plant-derived and synthetic cannabinoid agonists. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. May contribute to regulation of the immune system. Is required for normal homeostasis of CD8+ subsets of intraepithelial lymphocytes (IELs) (CD8alphaalpha and CD8alphabeta IELs)in small intstine by supporting preferential migration of CD8alphaalpha T-cells to intraepithelial compartment over lamina propria compartment, and by mediating their reconstitution into small intestine after bone marrow transplant (By similarity). Plays a role in hypotensive responses, mediating reduction in intraocular and blood pressure (By similarity). Mediates NAGly-induced process of reorganization of actin filaments and induction of acrosomal exocytosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24762058, ECO:0000269|PubMed:27018161}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:24762058}.
Interaction partners:
- Glucose-dependent insulinotropic receptor
- Cannabinoid receptor 2
- Cannabinoid receptor 1
- Transient receptor potential cation channel subfamily V member 1
- G-protein coupled receptor 55
- Fatty-acid amide hydrolase 1
- G-protein coupled receptor 3
- G-protein coupled receptor 183
Sequence:
MITLNNQDQPVPFNSSHPDEYKIAALVFYSCIFIIGLFVNITALWVFSCTTKKRTTVTIYMMNVALVDLIFIMTLPFRMFYYAKDEWPFGEYFCQILGALTVFYPSIALWLLAFISADRYMAIVQPKYAKELKNTCKAVLACVGVWIMTLTTTTPLLLLYKDPDKDSTPATCLKISDIIYLKAVNVLNLTRLTFFFLIPLFIMIGCYLVIIHNLLHGRTSKLKPKVKEKSIRIIITLLVQVLVCFMPFHICFAFLMLGTGENSYNPWGAFTTFLMNLSTCLDVILYYIVSKQFQARVISVMLYRNYLRSMRRKSFRSGSLRSLSNINSEML
Protein: Apolipoprotein C-IV (Apo-CIV) (ApoC-IV) (Apolipoprotein C4) (P55056)
Organism: Homo sapiens (Human)
Function: May participate in lipoprotein metabolism.
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein C-I
- Apolipoprotein C-II
- Apolipoprotein E
- Apolipoprotein A-II
- Apolipoprotein A-V
- Apolipoprotein C-III
- Serum paraoxonase/arylesterase 1
- Apolipoprotein A-I
- Apolipoprotein M
- Apolipoprotein A-IV
Sequence:
MSLLRNRLQALPALCLCVLVLACIGACQPEAQEGTLSPPPKLKMSRWSLVRGRMKELLETVVNRTRDGWQWFWSPSTFRGFMQTYYDDHLRDLGPLTKAWFLESKDSLLKKTHSLCPRLVCGDKDQG