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Database: UniProt
Entry: H0UT18_CAVPO
LinkDB: H0UT18_CAVPO
Original site: H0UT18_CAVPO 
ID   H0UT18_CAVPO            Unreviewed;      1214 AA.
AC   H0UT18;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
GN   Name=EGFR {ECO:0000313|Ensembl:ENSCPOP00000000034.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000000034.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000000034.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000000034.3};
RG   Ensembl;
RL   Submitted (NOV-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   -!- 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. EGF receptor subfamily. {ECO:0000256|PIRNR:PIRNR000619}.
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DR   EMBL; AAKN02045428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003465863.2; XM_003465815.3.
DR   AlphaFoldDB; H0UT18; -.
DR   SMR; H0UT18; -.
DR   STRING; 10141.ENSCPOP00000000034; -.
DR   Ensembl; ENSCPOT00000000040.3; ENSCPOP00000000034.3; ENSCPOG00000000040.4.
DR   GeneID; 100725363; -.
DR   KEGG; cpoc:100725363; -.
DR   CTD; 1956; -.
DR   VEuPathDB; HostDB:ENSCPOG00000000040; -.
DR   eggNOG; KOG1025; Eukaryota.
DR   GeneTree; ENSGT00940000155450; -.
DR   HOGENOM; CLU_003384_0_2_1; -.
DR   InParanoid; H0UT18; -.
DR   OMA; KDRYTNC; -.
DR   OrthoDB; 1614410at2759; -.
DR   TreeFam; TF106002; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000000040; Expressed in uterine cervix and 13 other cell types or tissues.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR   GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0097489; C:multivesicular body, internal vesicle lumen; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0048408; F:epidermal growth factor binding; IEA:Ensembl.
DR   GO; GO:0005006; F:epidermal growth factor receptor activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0030235; F:nitric-oxide synthase regulator activity; IEA:Ensembl.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR   GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
DR   GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR   GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IEA:Ensembl.
DR   GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR   GO; GO:0060571; P:morphogenesis of an epithelial fold; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:1905208; P:negative regulation of cardiocyte differentiation; IEA:Ensembl.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR   GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0046328; P:regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0070141; P:response to UV-A; IEA:Ensembl.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IEA:Ensembl.
DR   CDD; cd00064; FU; 3.
DR   CDD; cd05108; PTKc_EGFR; 1.
DR   Gene3D; 6.10.250.2930; -; 1.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR044912; Egfr_JX_dom.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; IPR049328; TM_ErbB1.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   PANTHER; PTHR24416:SF91; EPIDERMAL GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   Pfam; PF21314; TM_ErbB1; 1.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 4.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000619};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000619};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000619, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000619};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000619};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000619};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR000619}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1214
FT                   /note="Receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011614029"
FT   TRANSMEM        652..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          718..985
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1040..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1067..1086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1102..1175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1137..1175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        843
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT   BINDING         724..732
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT   BINDING         751
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1214 AA;  134686 MW;  F6F789F6A007C9AD CRC64;
     MRPYAAAGPA MCALLALLAL LGAHAAPEEK RVCQGTSNKL TQLGTFEDHF LSLQRMFNNC
     EVVLGNLEIT YVQRNYDLSF LKTIQEVAGY VLVALNTVER IPLENLQIVR GNVLYENTYA
     LAVLSNYGSA NSANRTGLRE LPLRSLQEIL HGAVRFSNNP VLCSVDTIQW RDIVNNLFLS
     NMSLDWQSPQ SGCQKCDPSC PNGSCWGPGA ENCQKLTKII CAQQCSGRCR GKSPSDCCHN
     QCAAGCTGPR ESDCLVCRRF RDEATCKDTC PPLMLYNPTT YQMDVNPEGK YSFGATCVKK
     CPRNYVVTDH GSCVRACSSD SYEIEEDGVR KCKKCEGPCR KVCNGIGIGE FKDTLSINAT
     NIKHFRNCTT ISGDLHILPV AFRGDSFTRT QPLDPKELDI LKTVKEITGF LLIQAWPENR
     TNLHAFENLE IIRGRTKQHG QFSLAVVGLN LTSLGLRSLK EISDGDVIVS GNRHLCYANT
     IHWRKLFGTA GQKTKIVNNR NERDCKADGH VCHPLCSSEG CWGPEAQDCV SCQNVSRGRE
     CVARCNIFEG EPREFVENSE CIQCHPECLP QAMNVTCTGR GPDNCVQCAH HIDGPHCVKT
     CPAGVMGENN TLVWKYADAG RVCRLCHPNC TYGCTGPGLQ GCAIEGTKVP SIATGIVGGL
     FLLVLLGLGI GLLMRRRHIV RKRTLRRLLQ ERELVEPLTP SGEAPNQALL RILKETEFKK
     IKVLGSGAFG TVYKGLWIPE GEKVKIPVAI KELREATSPK ANKEILDEAY VMASVDNPHV
     CRLLGICLTS TVQLVTQLMP FGCLLDYVRE HKDNIGSQHL LNWCVQIAKG MNYLEDRRLV
     HRDLAARNVL VKTPQHVKIT DFGLAKLLGA EEKEYHAEGG KVPIKWMALE SILHRIYTHQ
     SDVWSYGVTV WELMTFGSKP YDGIPASEIS SILEKGERLP QPPICTIDVY MIMVKCWMID
     ADSRPKFREL IVEFSKMARD PQRYLVIQGD ERMHLPSPTD SNFYRALMDE EDMEDIVDAD
     EYLIPQQSFF SSPSTSRTPL LSSLSANSNN STGACVPRNG NCPVRSDGFL QRYSSDPTGT
     LTEDNLDDAF LPVPEYINQS FPKRPAGSVQ NPIYHNQPLH PAPGRDPHYQ NPHSHAVGNP
     EYLNTTQSTG VSGSFDSPGP WTQQGNHQLS LDNPDYQQDF FPKEAKPNGI FKGPTAENTE
     YLRVAPPSSE FIGA
//
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