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Database: UniProt
Entry: A0A2K5YPE3_MANLE
LinkDB: A0A2K5YPE3_MANLE
Original site: A0A2K5YPE3_MANLE 
ID   A0A2K5YPE3_MANLE        Unreviewed;      1289 AA.
AC   A0A2K5YPE3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN   Name=INSR {ECO:0000313|Ensembl:ENSMLEP00000017404.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000017404.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000017404.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171,
CC         ECO:0000256|RuleBase:RU000312};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000312}.
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DR   Ensembl; ENSMLET00000040880.1; ENSMLEP00000017404.1; ENSMLEG00000032885.1.
DR   GeneTree; ENSGT00940000155404; -.
DR   OMA; WTEATHF; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043560; F:insulin receptor substrate binding; IEA:InterPro.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00064; FU; 1.
DR   CDD; cd05061; PTKc_InsR; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR040969; Insulin_TMD.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF535; INSULIN RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF17870; Insulin_TMD; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000620; Insulin_receptor; 2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00261; FU; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000620-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000620-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW   ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000312};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        865..886
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          590..692
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          930..1205
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          652..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1267..1289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1066
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT   BINDING         940
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         964
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1011..1017
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1070..1071
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1084
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ   SEQUENCE   1289 AA;  146508 MW;  BE0937FCF7782598 CRC64;
     CPGMDIRNNL TRLHELENCS VIEGHLQILL MFKTRPEDFR DLSFPKLIMI TDYLLLFRVY
     GLESLKDLFP NLTVIRGSRL FFNYALVIFE MVHLKELGLY NLMNITRGSV RIEKNNELCY
     LATIDWSRIL DSVEDNYIVL NKDDNEECGD ICPGTAKGKT NCPATVINGQ FVERCWTHSH
     CQKVCPTICK SHGCTAEGLC CHSECLGNCS EPDDPTKCVA CRNFYLDGRC VETCPPPYYH
     FQDWRCVNFS FCQDLHHKCK NSRRQGCHQY VIHNNKCIPE CPSGYTMNSS NLLCTPCLGP
     CPKVCHLLEG EKTIDSVTSA QELRGCTVIN GSLIINIRGG NNLAAELEAN LGLIEEISGY
     LKIRRSYALV SLSFFRKLRL IRGETLEIGN YSFYALDNQN LRQLWDWSKH NLTITQGKLF
     FHYNPKLCLS EIHKMEEVSG TKGRQERNDI ALKTNGDQAS CENELLKFSY IRTSFDKILL
     RWEPYWPPDF RDLLGFMLFY KEAPYQNVTE FDGQDACGSN SWTVVDIDPP LRSNDPKSQN
     HPGWLMRGLK PWTQYAIFVK TLVTFSDERR TYGAKSDIIY VQTDATNPSV PLDPISVSNS
     SSQIILKWKP PSDPNGNITH YLVFWERQAE DSELFELDYC LKGLKLPSRT WSPPFESEDS
     QKHNQSEHED SAGECCSCPK TDSQILKELE ESSFRKTFED YLHNVVFVPR PSRKRRSLGD
     VGNVTVAVPT VAAFPNTSST STPTSPEEHR PFEKVVNKES LVISGLRHFT GYRIELQACN
     QDTPEERCSV AAYVSARTMP EELHLCVSRK HFALERGCRL RGLSPGNYSV RVRATSLAGN
     GSWTEPTYFY VTDYLDVPSN IAKIIIGPLI FVFLFSIVIG SIYLFLRKRQ PDGPLGPLYA
     SSNPEYLSAS DVFPCSVYVP DEWEVPREKI TLLRELGQGS FGMVYEGNAR DIIKGEAETR
     VAVKTVNESA SLRERIEFLN EASVMKGFTC HHVVRLLGVV SKGQPTLVVM ELMAHGDLKS
     YLRSLRPEAE NNPGRPPPTL QEMIQMAAEI ADGMAYLNAK KFVHRDLAAR NCMVAHDFTV
     KIGDFGMTRD IYETDYYRKG GKGLLPVRWM APESLKDGVF TTSSDMWSFG VVLWEITSLA
     EQPYQGLSNE QVLKFVMDGG YLDQPDNCPE RVTDLMRMCW QFNPKMRPTF LEIVNLLKDD
     LHPSFPEVSF FHSEENKAPE NEELEMEFED MENVPLDRSS HCQREEAGGR DGGSSLGFKR
     SYEEHIPYTH MNGGKKNGRI LTLPRSNPS
//
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