位置:首页 > 蛋白库 > INSRR_RAT
INSRR_RAT
ID   INSRR_RAT               Reviewed;        1300 AA.
AC   Q64716; Q63146;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Insulin receptor-related protein;
DE            Short=IRR;
DE            EC=2.7.10.1;
DE   AltName: Full=IR-related receptor;
DE   Flags: Precursor;
GN   Name=Insrr;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-481, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley, and Wistar; TISSUE=Kidney, Liver, and Stomach;
RX   PubMed=1603082; DOI=10.1210/mend.6.5.1603082;
RA   Shier P., Watt V.M.;
RT   "Tissue-specific expression of the rat insulin receptor-related receptor
RT   gene.";
RL   Mol. Endocrinol. 6:723-729(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 896-996, AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=1530648; DOI=10.1016/0006-291x(92)91287-z;
RA   Kurachi H., Jobo K., Ohta M., Kawasaki T., Itoh N.;
RT   "A new member of the insulin receptor family, insulin receptor-related
RT   receptor, is expressed preferentially in the kidney.";
RL   Biochem. Biophys. Res. Commun. 187:934-939(1992).
RN   [4]
RP   FUNCTION, AND AUTOPHOSPHORYLATION.
RX   PubMed=21641549; DOI=10.1016/j.cmet.2011.03.022;
RA   Deyev I.E., Sohet F., Vassilenko K.P., Serova O.V., Popova N.V.,
RA   Zozulya S.A., Burova E.B., Houillier P., Rzhevsky D.I., Berchatova A.A.,
RA   Murashev A.N., Chugunov A.O., Efremov R.G., Nikol'sky N.N., Bertelli E.,
RA   Eladari D., Petrenko A.G.;
RT   "Insulin receptor-related receptor as an extracellular alkali sensor.";
RL   Cell Metab. 13:679-689(2011).
CC   -!- FUNCTION: Receptor with tyrosine-protein kinase activity. Functions as
CC       a pH sensing receptor which is activated by increased extracellular pH.
CC       Activates an intracellular signaling pathway that involves IRS1 and
CC       AKT1/PKB. {ECO:0000269|PubMed:21641549}.
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   -!- 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   -!- TISSUE SPECIFICITY: Expressed preferentially in the kidney. Also found
CC       in stomach and thymus but not in skeletal muscle, brain, intestine, and
CC       uterus. {ECO:0000269|PubMed:1530648, ECO:0000269|PubMed:1603082}.
CC   -!- DOMAIN: The extracellular domain is required for sensing alterations in
CC       external pH. {ECO:0000250}.
CC   -!- PTM: Autophosphorylated on tyrosine residues between pH 7.9 and pH
CC       10.5.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABR03012734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M90661; AAB59692.1; -; mRNA.
DR   EMBL; M90660; AAA41452.1; -; Genomic_DNA.
DR   EMBL; D12678; BAA20982.1; -; mRNA.
DR   PIR; PC1130; PC1130.
DR   RefSeq; NP_071548.2; NM_022212.2.
DR   AlphaFoldDB; Q64716; -.
DR   SMR; Q64716; -.
DR   STRING; 10116.ENSRNOP00000018638; -.
DR   GlyGen; Q64716; 10 sites.
DR   iPTMnet; Q64716; -.
DR   PhosphoSitePlus; Q64716; -.
DR   jPOST; Q64716; -.
DR   PaxDb; Q64716; -.
DR   PRIDE; Q64716; -.
DR   Ensembl; ENSRNOT00000080693; ENSRNOP00000073224; ENSRNOG00000057702.
DR   GeneID; 60663; -.
DR   KEGG; rno:60663; -.
DR   UCSC; RGD:67399; rat.
DR   CTD; 3645; -.
DR   RGD; 67399; Insrr.
DR   eggNOG; KOG1095; Eukaryota.
DR   eggNOG; KOG4258; Eukaryota.
DR   GeneTree; ENSGT00940000160437; -.
DR   HOGENOM; CLU_000288_166_0_1; -.
DR   InParanoid; Q64716; -.
DR   OMA; GTRGRWQ; -.
DR   OrthoDB; 223327at2759; -.
DR   TreeFam; TF351636; -.
DR   PRO; PR:Q64716; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000057702; Expressed in kidney and 6 other tissues.
DR   Genevisible; Q64716; RN.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005899; C:insulin receptor complex; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005009; F:insulin receptor activity; IBA:GO_Central.
DR   GO; GO:0043560; F:insulin receptor substrate binding; IBA:GO_Central.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0071469; P:cellular response to alkaline pH; ISO:RGD.
DR   GO; GO:0030238; P:male sex determination; ISO:RGD.
DR   GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd00063; FN3; 3.
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; IPR028792; INSRR.
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:SF338; PTHR24416:SF338; 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   1: Evidence at protein level;
KW   ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1300
FT                   /note="Insulin receptor-related protein"
FT                   /id="PRO_0000016707"
FT   TOPO_DOM        747..921
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        922..942
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        943..1300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          483..603
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          607..707
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          818..913
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          979..1254
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1270..1300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1115
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         985..993
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1013
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1145
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1146
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        411
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        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        616
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        634
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        756
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"
FT   DISULFID        214..222
FT                   /evidence="ECO:0000250"
FT   DISULFID        216..228
FT                   /evidence="ECO:0000250"
FT   DISULFID        229..237
FT                   /evidence="ECO:0000250"
FT   DISULFID        233..246
FT                   /evidence="ECO:0000250"
FT   DISULFID        249..258
FT                   /evidence="ECO:0000250"
FT   DISULFID        262..274
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..300
FT                   /evidence="ECO:0000250"
FT   DISULFID        304..317
FT                   /evidence="ECO:0000250"
FT   DISULFID        320..324
FT                   /evidence="ECO:0000250"
FT   DISULFID        657..864
FT                   /note="Interchain (between alpha and beta chains)"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        261
FT                   /note="T -> A (in Ref. 2; AAB59692)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="L -> M (in Ref. 2; AAB59692)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1300 AA;  144846 MW;  0CF24D5B96D68225 CRC64;
     MAVPALWPWG VYLLMSLLSL GSCLDTLEVC PSLDIRSEVT ELRRLENCSV VEGHLQILLM
     FAATGEDFRG LSFPRLTQVT DYLLLFRVYG LESLRDLFPN LAVIRGARLF LGYALIIFEM
     PHLRDIGLPS LGAVLRGAVR VEKNQELCHL STIDWGLLQP APGANHIVGN KLGEECADVC
     PGVLGAAGEP CVRTTFGGHT DYRCWTSSHC QRVCPCPRGL ACTVGGECCH SECLGGCSQP
     EDPRACVACR HLYFQGVCLP TCPPGTYQYE SWRCVTAELC GHLREVPGHA TAFGIYEGSC
     LAQCPPGFTR NGSSIFCHKC EGLCPKECKV GTKTIDSVQA TQDLVGCTHV EGSLILNLRQ
     GYNLEPELQR NLGLVETITG FLKIKHSFAL VTLGFFKNLK LIRGDSMVDG NYTLYVLDNQ
     NLQQLGSWVA AGLTIPVGKI YFAFNPRLCL EHIYQLEEVT GTRGRQSKAE INPRTNGDRA
     ACQTRTLRFV FNLTEEDRIL LRWERYEPLE ARDLLSFIVY YKESPFQNAT EHVGPDACGT
     QSWNLLDVEL PLSRTQEPGV TLAPLKPWTQ YAVFVRAITL TTAEDSPHQG AQSPIVYLRT
     LPAAPTVPQD VISTSNSSSH LLVRWKPPVQ RNGNITYYLV LWQRLAEDGD LYINDYCHRG
     LRLPTSSHDT RFDREDPALE AEPEQGCCPC QHSPPGQALP ALEAQEVTFQ KKFENFLHHA
     ITIPKAPWKV TSINKNPQRD SERHRRETGL LRLGKNNSDF EIHEDKVPRE RAVLSGLRHF
     TEYRIDIHAC NHAAHTVGCS AATFVFARTM PHREADGIPG KVVWKAVGKS SVILHWLEPP
     DPNGLILKYE IKYRRLGEEA TVLCVSRLRY AKVGGVHLAL LPPGNYSAKV RATSLAGNGS
     WTDGVAFYIT GPEEEDTGGL RILLTVTPVG FMLLVMLAAL GFFYSKKRNS TLYTSVNPEY
     FSASHMYVPD EWEVPREQIA IIRELGQGSF GMVYEGLARG LEAGEESTPV ALKTVNELAS
     ARERVEFLKE ASVMKAFKCH HVVRLLGVVS QGQPTLVIME LMTRGDLKSH LRSLRPEAEN
     NPGLPQPALS DMIQMAGEIA DGMAYLAAKK FVHRDLAARN CMVSQDFTVK IGDFGMTRDV
     YETDYYRKGG KGLLPVRWMA PESLKDGIFT THSDVWSFGV VLWEIVTLAE QPYQGLSNEQ
     VLKFVMDGGV LEEQEDCPIQ LQELMRRCWQ HTPRLRPTFV HILDRIQDEL RPSFRLCSFY
     YSPECQRGQA SLLPTEAEPD SPPTLNGASD YGPPNGDPGH
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024