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INSR_AEDAE
ID   INSR_AEDAE              Reviewed;        1393 AA.
AC   Q93105; Q17IL5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Insulin-like receptor;
DE            Short=MIR;
DE            EC=2.7.10.1;
DE   Contains:
DE     RecName: Full=Insulin-like receptor alpha chain;
DE   Contains:
DE     RecName: Full=Insulin-like receptor beta chain;
DE   Flags: Precursor;
GN   Name=InR; ORFNames=AAEL002317;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=UGAL; TISSUE=Ovary;
RX   PubMed=9099579; DOI=10.1111/j.1365-2583.1997.tb00083.x;
RA   Graf R., Neuenschwander S., Brown M.R., Ackermann U.;
RT   "Insulin-mediated secretion of ecdysteroids from mosquito ovaries and
RT   molecular cloning of the insulin receptor homologue from ovaries of
RT   bloodfed Aedes aegypti.";
RL   Insect Mol. Biol. 6:151-163(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
CC   -!- FUNCTION: This receptor probably binds an insulin related protein and
CC       has a tyrosine-protein kinase activity. {ECO:0000250}.
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: Tetramer of 2 alpha and 2 beta chains linked by disulfide
CC       bonds. The alpha chains contribute to the formation of the ligand-
CC       binding domain, while the beta chains carry the kinase domain (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain and ovary.
CC       {ECO:0000269|PubMed:9099579}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT46545.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U72939; AAB17094.1; -; mRNA.
DR   EMBL; CH477238; EAT46545.1; ALT_SEQ; Genomic_DNA.
DR   PIR; T30346; T30346.
DR   RefSeq; XP_001661260.1; XM_001661210.1.
DR   AlphaFoldDB; Q93105; -.
DR   SMR; Q93105; -.
DR   DIP; DIP-29908N; -.
DR   IntAct; Q93105; 1.
DR   STRING; 7159.AAEL002317-PA; -.
DR   PRIDE; Q93105; -.
DR   VEuPathDB; VectorBase:AAEL002317; -.
DR   eggNOG; KOG4258; Eukaryota.
DR   HOGENOM; CLU_000288_166_1_1; -.
DR   InParanoid; Q93105; -.
DR   OrthoDB; 223327at2759; -.
DR   BRENDA; 2.7.10.1; 149.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProt.
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:0043559; F:insulin binding; ISS:UniProtKB.
DR   GO; GO:0005009; F:insulin receptor activity; ISS:UniProtKB.
DR   GO; GO:0043560; F:insulin receptor substrate binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00064; FU; 1.
DR   Gene3D; 2.60.40.10; -; 3.
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; 1.
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; 3.
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; Reference proteome; Repeat;
KW   Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..753
FT                   /note="Insulin-like receptor alpha chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016719"
FT   CHAIN           758..1393
FT                   /note="Insulin-like receptor beta chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016721"
FT   TOPO_DOM        758..966
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        967..987
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        988..1393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          240..287
FT                   /note="FU"
FT   DOMAIN          507..623
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          624..729
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          860..961
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1025..1302
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          754..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1328..1365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1374..1393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1349..1363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         1031..1039
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1059
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1189
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1193
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1194
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        765
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        772
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        793
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        796
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        871
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        919
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        933
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        38
FT                   /note="S -> T (in Ref. 1; AAB17094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110..111
FT                   /note="IR -> YP (in Ref. 1; AAB17094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        331
FT                   /note="L -> V (in Ref. 1; AAB17094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        419
FT                   /note="L -> P (in Ref. 1; AAB17094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        474
FT                   /note="C -> W (in Ref. 1; AAB17094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1126..1132
FT                   /note="NGEDPSP -> MRRSIR (in Ref. 1; AAB17094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1151..1153
FT                   /note="MAY -> IGV (in Ref. 1; AAB17094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1380..1393
FT                   /note="GPMATIRSPHSPLR -> ARWPRSVRHTRH (in Ref. 1;
FT                   AAB17094)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1393 AA;  156728 MW;  BD75381D755CEC60 CRC64;
     MVSLLLFSIL VVPVAVVQGD EMKAGQVGPV PKGGVCGSVD VRNSPAHLDR LKDCVVVEGF
     VHILLIDKYI DSSFENYSFP LLTEITEYLL LFRVNGLKSL RRLFPNLAVI RGDALVGDYA
     MVIYELMHIE EIGLISLMDI TRGGVRIEKN PKLCFANTID WKAMTVPGTN NYIKDNQKDN
     VCPICPAEST AVMLPNGSKQ KCPAAPVRGG NKDHKRTLCW NANHCQTICP PECPKACSKT
     GVCCDAESCL GGCNLPNTSS CSVCRHLSID PAGKRQCVAK CPPNTFKYHT RCVTRDECYA
     MKKPISLDSN PDLPDQPFIP HNGSCLMECP LDHELITELN KTRWCRKCSG TCPKRCEGSN
     IDNIQSAQLL KGCEIIDGSL EIQLRSRGGE NIVKELENFL SSITEIKGYL KVVRSYPLLS
     LGFLKKLKII HGKGNKVSNS SLYVVENQNL QELFDHNVTI GEGKLFFFNN PMLCTDRIKA
     VKKYNPGIEI ENESQLESNN GDRAACSITE LETSLKSIGS ETAIIQWAPF TELSDARMLL
     GYVIYYIEAP YANVTFFDGR DACNTEGWRL DDISDFNMDK ETTKILTQLK PYTQYAYYVK
     TYTLGSEGLG GQSKIKYFTT APGTPSVVRD VEVSVNKNML TVKWLPPLKM NGRLKEYEVF
     IELNADDNEQ LMLRDYCEDD KLRDIVPETP TSAPPPKTSI CTADQCRNYC KAPTSGGSTG
     TIDVTDKENQ ITFEDQLHNY VYIKNPLLRD KTTRRKRSTN LLFPNNTENK KNDTTDRRTE
     KVKDEPYYQY IFNATNETSI TFPLSYFNHY SLYVFKIRAC RHPGDPPAPS VRLVDVELAC
     GNEVFENFRT PKKEGADDIP PESILIEEQS NNTQRQIRVQ WKEPSKPNGP IVKFVVKYQR
     VDLESVSSTD ICIRYSSFNQ TRGALLTKLE PGNYSIRVMA TTIAGDGAPS AARYVLIAKD
     DSMGTTLIWL GTLIVIFLCS VGFVAFYWYK YRYMSKQIRM YPEVNPDYAG VQYKVDDWEV
     ERNHIIQLEE LGQGSFGMVY KGILTQLRGE KCNQPCAIKT VNESATAREK DSFLLEASVM
     KQFNTHHVVR LLGVVSQGDP TLVIMELMAN GDLKSYLRRH RPDYENGEDP SPQPPTLRQI
     IQMAIEIADG MAYLSAKKFV HRDLAARNCM VADDMTVKIG DFGMTRDIYE TDYYRKGTKG
     FLPVRWMAPE SLKDGIFSSS SDVFSYGVVL WEMATLASQP YQGLTNDQVL RYVIDGGVME
     RPENCPDNLY NLMRRCWQHR PTARPTFMEI ISELLPDASP HFQDVAFYNS QDALDMLRGQ
     HQTVIIDEAT TPLRPGDDHD EEPGEDDDLV GHGEGHIGDV GTDDEFSMEM TNSHLVRNNG
     PMATIRSPHS PLR
 
 
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