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
//