ILPR_BRALA
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 03-AUG-2022, entry version 132.
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 Branchiostomidae; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0046777; P:protein autophosphorylation; IEA:InterPro.
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 Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.80.20.20; -; 2.
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 Pfam; PF00041; fn3; 2.
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; SSF49265; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 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
