wanglab/gogpt-training-data huggingface dataset:
Protein: Protection of telomeres protein 1 (cPot1) (POT1-like telomere end-binding protein) (P62597)
Organism: Gallus gallus (Chicken)
Function: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. Is a component of the double-stranded telomeric DNA-binding TRF1 complex that is involved in the regulation of telomere length by cis-inhibition of telomerase. Also acts as a single-stranded telomeric DNA-binding protein and thus may act as a downstream effector of the TRF1 complex and may transduce information about telomere maintenance and/or length to the telomere terminus. Binds to at least two telomeric single-stranded 5'-TTAGGG-3' repeats (G-strand). Its activity is TERT dependent but it does not increase TERT activity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:14966288}. Chromosome, telomere {ECO:0000269|PubMed:14966288}. Note=Colocalizes with telomeric DNA.
Interaction partners:
- Telomeric repeat-binding factor 2-interacting protein 1
- Telomerase reverse transcriptase
- Telomeric repeat-binding factor 2
- Uncharacterized protein.
- Doublecortin domain-containing protein.
- H/ACA ribonucleoprotein complex subunit
- Tripeptidyl peptidase 1.
- Uncharacterized protein.
Sequence:
MPVQVLKIIKGKPETQLPSHLQREDLKHLQTGLDHTNKYFQGIVILSYPLTKLGDGTDFFKIVLQDDTCSRINSINVLMYGKMAEDCAKLIRNGDTFIVAGFKVAESPTAREDGRHACHLQVSEESGSAIFICTQPSITPFSEATSPSVAPKYVYTPLNCLKDGTVVNLYGIVKFFKPPYISKGTDYCSVVTLVDQSNVKLTCTLFNGNLDSLPKIYKNGDIVRFHRVKIREYNGQMQGITSAGFASLTFDGTVGAPVVPRASSKVYTFVDEEQKTVEELRIWAASNLSVSGPEAKLSDVKPMMFFDLTCQLVGKAKVDGSSFLLKVWDGTKCPYPTWKVPVEAKELEGDRVLLHHLRNLTVDVLVYDNHVQLAKSLKTGSFLRIYSIHTKQASAKNEDMSSHIEFHLHGGTCYGRGIGILPENNPDVEELKSFLECVELTDSQNMESVSSLELGDTFDSYTDLESPLQRCQQLSATVLTDHQDMSNTVLKTVLNSSAPQQYRIRAKLRSFKPQKLYQSVKLHCSKCNTLQEVPNGDAIDFILQGCAATAPNPELQSMSWYESVVWTTEEDQGRKITIHFVKHYEMLQRPENTLLMIEGGTLKEIWKLTRRFKCVIPVKSKEDDLELLDLSAPFLLQGNIKYYGCKKCSTPKSIKNLSSLAEKREPSWEPTEIAQVLGIEPLQYVFVMKFTLVDGTGVLNAYLFDYEKFFQIPASEILTNSFLQQKMEMTMNTLSPPGRKLDDLPWLECFIKSYNVADGMKHQVYYQIFDTTVAEDVV
Protein: High-affinity hexose transporter ght4 (Hexose transporter 4) (O59932)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- SNF1-like protein kinase ssp2
Sequence:
MGRTLTSVLVVFISMAGWLGGADTGSISGILGMRDFQSRFADRYNPITNSYSYSAWRQALLTGTVNAGCLFGAMLSSPFTEAIGKKYSIAFFSGCYIIGQILLVTAVPSWVQIMVGKLFTGLTIGALSVLSPGYQSEVAPPQIRGAVVSTYQLFQTCGTLIAACINMGTHKLRKTASWRTSFGINILWGIFLMVGVLFLPESPRYLIYKGRDEEALRIMCQTAELDPESEIIQTNFNTIKSDIEMEMAGGKARWPEVFGKEVRYRTVLGFLTMLLRELIGNNYYFYYATQVFKGTGMTDIFLPAVILGAINFGTTFGALYTIDNLGRRNPLIFGAAFQSICFFIYAAVGDRKLIYKNGTSDHRAGAVMIVFSCLFLFSYCCSWGPMGWVIVGETFPIRYRSKCAAVATSGNWLGNFMVSFFTPFISNSIGFKLGYIYACINMTSAFQIFLMAKETKGLTLEEVNELYESDIKPWDSYKYVRQIESRRIHFSKEEEKREREKSKGYRGQEERFIENADGADNDDSSASSESFASAGAHSRSVFPRRSNVSEESHPTWV
Protein: Metal homeostasis factor ATX2 (Q12067)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in the homeostasis of manganese ions.
Subcellular location: Golgi apparatus membrane; Multi-pass membrane protein.
Interaction partners:
- Metal homeostatis protein BSD2
- Zinc transporter YKE4
- Zinc-regulated transporter 3
- Copper chaperone ATX1
- Transketolase 1
Sequence:
MKFLGVILLASFLLIATFLIGLIPLYYIDKQKSSIVTNQEGADSISDFTTNADTQTINDDVSSYRVKIAVLSQFGIGMLLGTSFMLVIPEGIKACVEHDGNVGVNLLIGFLGVYVLDRLVTLWVSRKQTVYTHDAVKFQSWKDIINHPRQIWMNLIQNNVVFALFIHGLSDGIALGTTTNNDSLLIVVLIAIVIHKIPAVLSLTSLMVSRQNLMKWEVICNVFLFASSTPIGYIVLSLLNLSHSPTMDWISGNLLLMSGGSLLYASFTAFVGGDSHDHDLSVEQEVVLPHDESVYVLIGVCIPLVISYCISEE
Protein: Protection of telomeres protein 1 (hPot1) (POT1-like telomere end-binding protein) (Q9NUX5)
Organism: Homo sapiens (Human)
Function: Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. Is a component of the double-stranded telomeric DNA-binding TRF1 complex which is involved in the regulation of telomere length by cis-inhibition of telomerase. Also acts as a single-stranded telomeric DNA-binding protein and thus may act as a downstream effector of the TRF1 complex and may transduce information about telomere maintenance and/or length to the telomere terminus. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Binds to two or more telomeric single-stranded 5'-TTAGGG-3' repeats (G-strand) and with high specificity to a minimal telomeric single-stranded 5'-TAGGGTTAG-3' sequence. Binds telomeric single-stranded sequences internally or at proximity of a 3'-end. Its activity is TERT dependent but it does not increase TERT activity by itself. In contrast, the ACD-POT1 heterodimer enhances telomere elongation by increasing telomerase processivity.
Subcellular location: Nucleus {ECO:0000269|PubMed:12391173, ECO:0000269|PubMed:27013236, ECO:0000269|PubMed:30586141, ECO:0000269|PubMed:35420632, ECO:0000269|PubMed:37140166}. Chromosome, telomere {ECO:0000269|PubMed:12391173, ECO:0000269|PubMed:27013236, ECO:0000269|PubMed:30586141, ECO:0000269|PubMed:35420632, ECO:0000269|PubMed:37140166}. Note=Colocalizes with telomeric DNA. {ECO:0000269|PubMed:12391173}.
Interaction partners:
- Adrenocortical dysplasia protein homolog
- TERF1-interacting nuclear factor 2
- Telomeric repeat-binding factor 2-interacting protein 1
- Telomeric repeat-binding factor 2
- Telomeric repeat-binding factor 1
- Tripeptidyl-peptidase 1
- Telomerase reverse transcriptase
- CST complex subunit CTC1
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- X-ray repair cross-complementing protein 6
Sequence:
MSLVPATNYIYTPLNQLKGGTIVNVYGVVKFFKPPYLSKGTDYCSVVTIVDQTNVKLTCLLFSGNYEALPIIYKNGDIVRFHRLKIQVYKKETQGITSSGFASLTFEGTLGAPIIPRTSSKYFNFTTEDHKMVEALRVWASTHMSPSWTLLKLCDVQPMQYFDLTCQLLGKAEVDGASFLLKVWDGTRTPFPSWRVLIQDLVLEGDLSHIHRLQNLTIDILVYDNHVHVARSLKVGSFLRIYSLHTKLQSMNSENQTMLSLEFHLHGGTSYGRGIRVLPESNSDVDQLKKDLESANLTANQHSDVICQSEPDDSFPSSGSVSLYEVERCQQLSATILTDHQYLERTPLCAILKQKAPQQYRIRAKLRSYKPRRLFQSVKLHCPKCHLLQEVPHEGDLDIIFQDGATKTPDVKLQNTSLYDSKIWTTKNQKGRKVAVHFVKNNGILPLSNECLLLIEGGTLSEICKLSNKFNSVIPVRSGHEDLELLDLSAPFLIQGTIHHYGCKQCSSLRSIQNLNSLVDKTSWIPSSVAEALGIVPLQYVFVMTFTLDDGTGVLEAYLMDSDKFFQIPASEVLMDDDLQKSVDMIMDMFCPPGIKIDAYPWLECFIKSYNVTNGTDNQICYQIFDTTVAEDVI
Protein: Ubiquitin-like protein ATG12A (Autophagy-related protein 12a) (APG12-like protein a) (AtAPG12a) (Q8S924)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt) and autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. ATG12/ATG5 conjugate has an essential role in plant nutrient recycling.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Autophagy-related protein 16
- Ubiquitin-like-conjugating enzyme ATG10
- Autophagy-related protein 3
- Ubiquitin-like modifier-activating enzyme atg7
- Autophagy protein 5
- Beclin-1-like protein
- Phosphatidylinositol 3-kinase VPS34
- Serine/threonine-protein kinase ATG1a
- Autophagy-related protein 18b
- Autophagy-related protein 8a
Sequence:
MATESSSPSSVRKVVVHLRATGGAPILKQSKFKIPGTDKFAKVIDFLRRQLHSDSLFVYVNSAFSPNPDESVIDLYNNFGFDGKLVVNYACSMAWG
Protein: Tripartite motif containing 28 (M0R0K9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
IYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPAPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSEPHVSGVKRSRSGEGEVSGLMRKVPRVSLERLDLDLTADSQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMALAEGPGAEGPRLASPSGSTSSGLEVVAPEGTSAPGGGPGTLDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSLDQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNEAFGDTKFSAVLVEPPPMSLPGAGLSSQELSGGPGDGP
Protein: Ferrochelatase-2, chloroplastic (AtFC2) (EC 4.98.1.1) (Ferrochelatase-II) (AtFC-II) (Heme synthase 2) (Protoheme ferro-lyase 2) (O04921)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the last step of heme biosynthesis by inserting ferrous iron into protoporphyrin IX to produce protoheme. Produces heme for photosynthetic cytochromes, and for proteins involved in abiotic and biotic stress responses. May play a role in the quality control of individual chloroplasts during photo-oxidative stress through regulation of heme biosynthesis.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:9210462}; Peripheral membrane protein {ECO:0000305|PubMed:9210462}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:9210462}; Peripheral membrane protein {ECO:0000305|PubMed:9210462}. Note=(PubMed:11602264) shows experimental evidences that FC2 is not present in Arabidopsis mitochondria in vivo. {ECO:0000305|PubMed:11602264}.
Interaction partners:
- Protoporphyrinogen oxidase 1, chloroplastic
- Protoporphyrinogen oxidase 2, chloroplastic/mitochondrial
- Frataxin, mitochondrial
- Heme oxygenase 1, chloroplastic
- Protoheme IX farnesyltransferase, mitochondrial
- Magnesium-chelatase subunit ChlH, chloroplastic
- Magnesium-chelatase subunit ChlD, chloroplastic
- Magnesium-chelatase subunit ChlI-1, chloroplastic
- Magnesium-chelatase subunit ChlI-2, chloroplastic
- Uroporphyrinogen decarboxylase 1, chloroplastic
Sequence:
MNCPAMTASPSSSSSSSYSTFRPPPPLLPQLSNDSQRSVVMHCTRLPFEAFAATSSNRLLGKHSLPLRAALVTSNPLNISSSSVISDAISSSSVITDDAKIGVLLLNLGGPETLDDVQPFLFNLFADPDIIRLPPVFQFLQKPLAQFISVARAPKSKEGYASIGGGSPLRHITDAQAEELRKCLWEKNVPAKVYVGMRYWHPFTEEAIEQIKRDGITKLVVLPLYPQFSISTSGSSLRLLERIFREDEYLVNMQHTVIPSWYQREGYIKAMANLIQSELGKFGSPNQVVIFFSAHGVPLAYVEEAGDPYKAEMEECVDLIMEELDKRKITNAYTLAYQSRVGPVEWLKPYTEEAITELGKKGVENLLAVPISFVSEHIETLEEIDVEYKELALKSGIKNWGRVPALGTEPMFISDLADAVVESLPYVGAMAVSNLEARQSLVPLGSVEELLATYDSQRRELPAPVTMWEWGWTKSAETWNGRAAMLAVLALLVLEVTTGKGFLHQWGILPSL
Protein: Aerobactin synthase (EC 6.3.2.39) (Q47318)
Organism: Escherichia coli
Function: Catalyzes the attachment of the second N-acetyl-N-hydroxylysine to the carboxylic group of N-citryl-N-acetyl-N-hydroxylysine to yield aerobactin. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Interaction partners:
Sequence:
MNHKDWDLVNRRLVAKMLSELEYEQVFHAESQGDDRYCINLPGAQWRFIAERGIWGWLWIDAQTLRCADEPVLAQTLLMQLKQVLSMSDATVAEHMQDLYATLLGDLQLLKARRGLSASDLINLNADRLQCLLSGHPKFVFNKGRRGWGKEALERYAPEYANTFRLHWLAVKREHMIWRCDNEMDIHQLLTAAMDPQEFARFSQVWQENGLDHNWLPLPVHPWQWQEKIATDFIADFGEGRMVSLGEFGDQWLAQQSLRTLTNASRRGGLDIKLPLTIYNTSCYRGIPGRYIAAGPLASRWLQQVFATDATLVQSGAVILGEPAAGYVSHEGYAALARAPYRYQEMLGVIWRENPCRWLKPDESPFLMATLMEWDENNQPLAGAYIDRSGLDAETWLTQLFRVVVVPLYHLLCRYGVALIAHGQNITLAMKEGVPQRVLLKDFQGDMRLVKEEFPEMDSLPQEVRDVTSRLSADYLIHDLQTGHFVTVLRFISPLMVRLGVPERRFYQLLAAVLSDYMKKHPQMSERFALFSLFRPQIIRVVLNPVKLTWPDLDGGSRMLPNYLEDLQNPLWLVTQEYES
Protein: Borealin (Cell division cycle-associated protein 8) (Dasra-B) (DasraB) (DrDasraB) (Q5XLR4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. {ECO:0000250}.
Interaction partners:
- Uncharacterized protein.
- Baculoviral IAP repeat-containing 5a.
- ATP synthase subunit alpha
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase subunit d
- ATP synthase peripheral stalk-membrane subunit b.
- ATP synthase F1 subunit delta.
- ATP synthase subunit gamma.
- ATP synthase F
- Aurora kinase B
Sequence:
MAPRKRTQNAKSKKNPKAPKLEAFLLDFDDEVHTIVERLKEKTNNLLKDADNLYKTALIKLPMAVRKMNWIEYCNLEKPKSPVDDSKVREEAAQVELAIAGNHTIPKVAAKEAKSSANSEDENMAPLKSTMKKKKASKKAPSTSKKPRTLSISKQGGTIQRTTRKPLITPARSFLDSSIIGATPLITPRFDPRLPKTPALRSALHREKVYSMSVNGSPLSAGGEDIVISVPIGNGECIQLLASEMDSVDLSQLDEKALRSIRNLQNRLTTLCGSSK
Protein: CcbJ (SAM-dependent methyltransferase) (E9JES0)
Organism: Streptomyces caelestis
Interaction partners:
Sequence:
MRNYDETTYGDQIADVYDEWPGDAGPPPDGREAALFVAALAAARPVLELGVGTGRVAFPLADLGVEVHGVESSEPMLDKLREKAAAHPNGNLVVPVLGNFAKLDLGEQRYSVVFAAFNTLFCLLGQDEQIDCMRQARELLEPGGTFVVQCLNPAGQRLATGNTFGTVELEDTAVHLEASKHDPLAQTLSAHHIVLSEGGGIRLFPYRLRYAYPAELDLMANVAGLELVERHADFERRRFDASSRYHVSVYRAAASA
Protein: UL54 (B4XS02)
Organism: anatid alphaherpesvirus 1
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
Interaction partners:
Sequence:
MEPGKSENPNVATDEDRGTTANEKKKPSDHDTGKYVKRARAKRHSPRNHGSPYGHHGNKRRSSDHDQRHQSKMQSDNEATVGDADRSPPNRDRRRMSDKSDFKQSRRSQRSSPAHEGRDQRAINRPTIQQRINSIFERCRATLSGGVQNGGFRTTAEHPWASVLSFDNANSGPEGRRVSWHTLCLIGKELRRMFEIRQLASSAAIGLRAAVLRNEDLIAALASCDEIMAWLKMHEFYGLPLIPNDPIVATVNSLLENLKLKLRPIFLCREMKTRRSFDEMLKRGDKGDIVDLPSFLFITLVKLSRALKRPSDYIPLGDVDPLGLLRSYIPGACITGILEMIDEHLHDCHDQQCKLYSSYVISPVFLHGKYFYCNEMF
Protein: Uncharacterized protein (Q582U6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKSRQPTKNCINMHDIVAQPLDAVVGAINATLRRPEELDDAEVRSIFEETSFILLRAEEALMASEEAAFRALFTLLNKGFAHSAESFGKGVEVFSSQVMLLEVLESIFHRAVKLQVFPLQGEAVAALLYTVGNLCDGDGTKDSCGRLFIGGLANILVHMYSQDVEEAHQHFVTQRAAVGAMIKLMKRSPRNRKLITSWDFLANCCALSVDPFFQLQCIELLYRVSRSNKSIFKQMKSRLSTEVIEKLASLTNSATLISDMMGVLAVINRDRESLLVFPLGACEVAGVDLNGSMTCYFAPHYFVLISSDAVTESTIPYSSIRSAKFVEPSGVAIRVHEFPASLVAGLSRKTPKGDTLTLRVSREQLQRFKSSSIHSWITAAMKTREGAHQTPVGAPGAGNNERWSSGVTPVASDHPQDGSGRKRYREESVQSAGSGKPGTTSDLKNVGSSEGPTSGIMKHSAEAVKLMSEVFPQKVTSIMSESINKIQEAVDGARVTTDGYRSHVKSAVEGAIQLVEDSLMASHSKAAAAVEKLNHELQERKATDTAFHQRIACIEIAAQQALEESRESEVRSLDSIKKEFEQHAAKYAAALDDELIRLSNPVSTLFNIFNSEGNQSIC
Protein: Transmembrane emp24 domain-containing protein bai (Protein baiser) (Q8SXY6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Eca and bai are essential, though not redundant, for dorsoventral patterning of the embryo. Specifically required during early embryogenesis for the activity of maternal tkv, while the zygotic tkv is not affected.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250, ECO:0000312|FlyBase:FBgn0045866}.
Interaction partners:
- CHOp24, isoform A
- IP11573p
- Transmembrane emp24 domain-containing protein eca
- LP01981p
- P24-related-1, isoform A
- GPI ethanolamine phosphate transferase 2
- GPI inositol-deacylase
- Coatomer subunit delta
- Opossum, isoform A
- LD30746p
Sequence:
MARAAFIVCLLMACAWSSHAVMFKLSPNTQKCLKEDIQANQLVMGEFEVSDVPGQIIDYIARDTKGHILSQKEHITKGKFSFMSEVYDTYEICFISKVPAHQRGVIQEVSLLTKKGVETKSYEGIGEASKLKPLEVDLKRLEDLSDSIVRDFVLMRKREEEMRDTNEKTNSRVLFFSIFSMCCLLGLATWQVLYLRRYFKAKKLIE
Protein: Bifunctional hemolysin/adenylate cyclase (AC-HLY) (ACT) (Cyclolysin) [Cleaved into: Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase); Hemolysin] (P0DKX7)
Organism: Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Function: Bifunctional adenylate cyclase toxin-hemolysin that plays a crucial role in host colonization. It causes whooping cough by acting on mammalian cells by elevating cAMP-concentration and thus disrupts normal cell function.
Subcellular location: Secreted {ECO:0000269|PubMed:2542030}.; SUBCELLULAR LOCATION: [Hemolysin]: Host cell membrane {ECO:0000305|PubMed:8077197}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cyclolysin secretion/processing ATP-binding protein CyaB
- Protein-lysine palmitoyltransferase CyaC
- Protein CyaD
- Pertactin autotransporter
- Protein CyaE
- Calcineurin-like phosphoesterase domain-containing protein
- cAMP phosphodiesterase
- Autotransporter subtilisin-like protease
- Tracheal colonization factor
- Nucleoside diphosphate kinase
Sequence:
MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATGESQMLTRGQLKEYIGQQRGEGYVFYENRAYGVAGKSLFDDGLGAAPGVPSGRSKFSPDVLETVPASPGLRRPSLGAVERQDSGYDSLDGVGSRSFSLGEVSDMAAVEAAELEMTRQVLHAGARQDDAEPGVSGASAHWGQRALQGAQAVAAAQRLVHAIALMTQFGRAGSTNTPQEAASLSAAVFGLGEASSAVAETVSGFFRGSSRWAGGFGVAGGAMALGGGIAAAVGAGMSLTDDAPAGQKAAAGAEIALQLTGGTVELASSIALALAAARGVTSGLQVAGASAGAAAGALAAALSPMEIYGLVQQSHYADQLDKLAQESSAYGYEGDALLAQLYRDKTAAEGAVAGVSAVLSTVGAAVSIAAAASVVGAPVAVVTSLLTGALNGILRGVQQPIIEKLANDYARKIDELGGPQAYFEKNLQARHEQLANSDGLRKMLADLQAGWNASSVIGVQTTEISKSALELAAITGNADNLKSVDVFVDRFVQGERVAGQPVVLDVAAGGIDIASRKGERPALTFITPLAAPGEEQRRRTKTGKSEFTTFVEIVGKQDRWRIRDGAADTTIDLAKVVSQLVDANGVLKHSIKLDVIGGDGDDVVLANASRIHYDGGAGTNTVSYAALGRQDSITVSADGERFNVRKQLNNANVYREGVATQTTAYGKRTENVQYRHVELARVGQLVEVDTLEHVQHIIGGAGNDSITGNAHDNFLAGGSGDDRLDGGAGNDTLVGGEGQNTVIGGAGDDVFLQDLGVWSNQLDGGAGVDTVKYNVHQPSEERLERMGDTGIHADLQKGTVEKWPALNLFSVDHVKNIENLHGSRLNDRIAGDDQDNELWGHDGNDTIRGRGGDDILRGGLGLDTLYGEDGNDIFLQDDETVSDDIDGGAGLDTVDYSAMIHPGRIVAPHEYGFGIEADLSREWVRKASALGVDYYDNVRNVENVIGTSMKDVLIGDAQANTLMGQGGDDTVRGGDGDDLLFGGDGNDMLYGDAGNDTLYGGLGDDTLEGGAGNDWFGQTQAREHDVLRGGDGVDTVDYSQTGAHAGIAAGRIGLGILADLGAGRVDKLGEAGSSAYDTVSGIENVVGTELADRITGDAQANVLRGAGGADVLAGGEGDDVLLGGDGDDQLSGDAGRDRLYGEAGDDWFFQDAANAGNLLDGGDGRDTVDFSGPGRGLDAGAKGVFLSLGKGFASLMDEPETSNVLRNIENAVGSARDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGSDLLSGDAGNDDLFGGQGDDTYLFGVGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQAGIEKLVEAMAQYPDPGAAAAAPPAARVPDTLMQSLAVNWR
Protein: Long-form leptin receptor (R9QT79)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MKTMILSAMLTFLVHILIISHSAVLVEPVEVSPHGDLLDLPWQTELCCSSTPAQLHHGGEEEDTGSAPSDTGHPHTLQCLFRNFTSTLGPHPESELSRATCWDILCRVDETWDNVICDLKHPATSSDTSIPGSVALSLQHLTTLPDIEVNSTHGTDCVGEDSITCSVALHVVSSIVVVTANVSNTTAGPLVMLSVPPRTSQRLWKPSPPLNLTHTQTTEGELILSWSDPQPHASPVQLSYEVRYNTSQSTSHPNWLHVNVSGAQWVSLTGLGPGLQYTLQIRSHHPALPHLWSDWSQQHRIRLENVTYLPERVVASFGDSVTVYCVCNDLRVNASTMVWILNSRDRLPKSQYAAVNDRVSKITVRPSEQRLSGTLHCCQPFGEMYSCNYHYSTIYIKDPVIDISCVTSGDLDSMTCRWNNLPIGGINFMSRVADLSCDVMEEAERVGVPVGVVRQAKCESSGYRGVKSCNLQPIRVTSCYKLWMEAKTDNSTRSHPVYITPMDHVKPHPPSGLEAVSMPSGVLKLAWVPPELPIYDMQYQVRYALSTGKAHPFWQVLALQTESWAEVLEPDVCGVYNVQVRCMHINGSGTWSDWSHLLYTTTHNSRAPDQGPDFWRVFQEDPASMQTNVTLLFEHSPIVEPTYCVEELVVQHQDSGGTVTEERIGLVSSYSFEWRGEVHSVTVKAQNSQGSSTRNTHMTLDRHPKRQCVRSFSASRVNSSCVVLLWSLQPNSSVPWSLVVEWSGQNHQDRPDQTPESRERWTRFPPTDKLLYLYGHFYDTEYEFILYPVFADGEGEPVYTKVFRGSDAGPAAYMLLMIIAFLSIVLFVTLVISQNHMKKFMWKDVPNPNNCSWAQGIDFGKADTMEQLFRHPEGLPAWPLLLVSETISQATIMEKTGPPTSGSDKDLIPASSPALCVDSEVPGLPEEEESLQLPDLPRSLESSAQPSVTYATVLLSDNPHHLYKQEGSLSSSSDEGNFSGNNSDISGSFPGGLWELEISHSGAGESDLDPRRSCSYNSIEEFSETSEQEDEALGGERDGGIEIIEEKDLYYLGMDCQEESEEEEDTRAMLLKEVMVLGRGGSSVESIPLLGSQDSMFSEYSDEGSVVGMRSVPLYLPQFRTAPSSPLKAQDS
Protein: Leukotriene A-4 hydrolase (LTA-4 hydrolase) (EC 3.3.2.6) (Leukotriene A(4) hydrolase) (Tripeptide aminopeptidase LTA4H) (EC 3.4.11.4) (P24527)
Organism: Mus musculus (Mouse)
Function: Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities (By similarity). Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4). Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides (By similarity). In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P09960}.
Interaction partners:
- Leukotriene C4 synthase
- Polyunsaturated fatty acid 5-lipoxygenase
- Cytochrome P450 4F3
- Leukotriene-B4 omega-hydroxylase 3
- Cytochrome P450 CYP4F13
- tRNA dimethylallyltransferase
- Leukotriene B4 receptor 1
- Arachidonate 5-lipoxygenase-activating protein
- Leukotriene B4 receptor 2
Sequence:
MPEVADTCSLASPASVCRTQHLHLRCSVDFARRTLTGTAALTVQSQEENLRSLTLDTKDLTIEKVVINGQEVKYTLGESQGYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKQHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGEAPDPEDPSRKIYRFNQRVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSANEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFHALGGWGELQNTIKTFGESHPFTKLVVDLKDVDPDVAYSSIPYEKGFALLFYLEQLLGGPEVFLGFLKAYVKKFSYQSVTTDDWKSFLYSHFKDKVDLLNQVDWNTWLYAPGLPPVKPNYDVTLTNACIALSQRWVTAKEEDLSSFSIADLKDLSSHQLNEFLAQVLQKAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEEAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVHTYQEHKASMHPVTAMLVGRDLKVD