ID   ILPR_BRALA              Reviewed;        1363 AA.
AC   O02466;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=Insulin-like peptide receptor;
DE            Short=ILP receptor;
DE            EC=2.7.10.1;
DE   Contains:
DE     RecName: Full=Insulin-like peptide receptor alpha chain;
DE   Contains:
DE     RecName: Full=Insulin-like peptide receptor beta chain;
DE   Flags: Precursor;
OS   Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8813726; DOI=10.1210/mend.10.7.8813726;
RA   Pashmforoush M., Chan S.J., Steiner D.F.;
RT   "Structure and expression of the insulin-like peptide receptor from
RT   amphioxus.";
RL   Mol. Endocrinol. 10:857-866(1996).
CC   -!- FUNCTION: This receptor binds to the insulin related peptide and has a
CC       tyrosine-protein kinase activity.
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:0000255|PROSITE-ProRule:PRU10028};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Probable tetramer of 2 alpha and 2 beta chains linked by
CC       disulfide bonds. The alpha chains contribute to the formation of the
CC       ligand-binding domain, while the beta chains carry the kinase domain
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; S83394; AAB50848.1; -; mRNA.
DR   PIR; T43220; T43220.
DR   AlphaFoldDB; O02466; -.
DR   SMR; O02466; -.
DR   BRENDA; 2.7.10.1; 932.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043560; F:insulin receptor substrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.
DR   CDD; cd00064; FU; 1.
DR   CDD; cd05032; PTKc_InsR_like; 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; 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:SF525; INSULIN-LIKE RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000620; Insulin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00261; FU; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
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; 3.
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   2: Evidence at transcript level;
KW   ATP-binding; Cleavage on pair of basic residues; Disulfide bond;
KW   Glycoprotein; Kinase; Manganese; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..716
FT                   /note="Insulin-like peptide receptor alpha chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016711"
FT   CHAIN           721..1363
FT                   /note="Insulin-like peptide receptor beta chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016713"
FT   TOPO_DOM        721..928
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        929..949
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        950..1363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          473..586
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          590..680
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          712..804
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          813..912
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          994..1283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          739..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1091..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1316..1363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         1000..1008
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1028
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1174
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        599
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        617
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        665
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        666
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        711
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        732
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        736
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        743
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        816
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        885
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        898
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1363 AA;  154105 MW;  238120B4EAB1ED65 CRC64;
     MRVVDKMAGL MWAALTLVIG LGLLVPSNGE EYICDSMDIR NRVSNLRQLE NCTVIEGYLQ
     ILLIDFAEEQ DYSGLAFPNL VEITDYFLLY RVRGLTNLSE LFPNLAVIRG TNLFFNYALV
     VFEMLDMQKI GLYSLQNITR GSVRIEKNPN LCYLDTIDWS FIAESGYSNN FIVDNREEEE
     CVNFCPGRCR IKHPVLQDLC WAEEHCQKVC PESCLGNCRD GISGCCHENC IGGCDGPTER
     DCVACKYFVH NGECLIQCPP DTYQYKDRRC ITEEECPNTT NSVWKLHHRK CIPECPSGYT
     TDINNPRLCT ECEGQCPKSC KGGLVDSLAA AQRFRGCTII EGELKISIRG GDNIIDELEE
     NLGLIEEVGH YVAIVRSYAL VTLDFLRSLK RIRGIQKENG YAFYVLDNRN LEKLFDWDRT
     DITIDEGKLF FHFNPKLCRH VILTMVDKVG LPEHAITDTD ISTLTNGDQA QCSFSRLEIE
     EINTSKDMII LRWSEFRPPD PRDLLSYTVS YRETEDQGID EYDGQDACGN TEWKEFDVSP
     TQTAHIITGL KPWTQYALLV KTYTKAGARE GSGAKSDIVY ARTDADKPTH PQDVVVYSNS
     SNTLIITWKP PNRPNGNVTH YIVKYKRQQE DVAEMEQREY CKGGLKPHRP TQGLEDIVNN
     EEEPNNSTIG DGTCCECPKS EDEIRIEEEE AAFQQEFENF LHNNVYHKRE NETRAGRRRR
     ELPVTARPFY SNQTVNVTLP STNRTVPPTP TPNPNPQLET TVWNEHMVVL TGLRHFSEYI
     IEVIACNADA AVGCSGSAVE LARTQADDSA DNIPGNITVV EIKEDMAKLY WPKPDSPNSM
     VVHYNIEYKK LGSDFNYEQQ EPKCVENFKF LQSQGYTISN LVAGNYSVRF RATSFAGNGS
     WSNYVTFYVE EEDTSPDPQD PQQQVPVSLM IGMGVGFSLL LILAVIFGIW YCTKKRFGDK
     QMPNGVLYAS VNPEYMSSDD VYVPDEWEVP REKITLIREL GQGSFGMVYE GEAKDVVKDE
     PMVSVAVKTV NESASIRERI EFLNEASVMK TFNCHHVVKL MGVVSKGQPT LVVMELMALG
     DLKNYLRRHR PEEDVGLSDS PASNEAKNSP FAENDNDLPP TFKDIIQMAG VIADGMSYLA
     AKKFVHRDLA CRNCMVAQDR TVKIGDFGMT RDIYETDYYR KGGKGLLPVR WMSPESLKVG
     VFTSQSDVWS YGVVLWEMAT LASQPYQGKS NEEVLKFVID GGMLEKPEGC PNKLYDLMKL
     CWQYRQSMRP TFLEIVEILS PELQAHFNEV SFYHSLDNHG REPLEMDDVA LDSGADTETE
     MYPSGSEFSS TPSPPSETPY SHMNGSHPQN GSMNLRIPKS TLC
//