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Database: UniProt
Entry: A0A337S1T7_FELCA
LinkDB: A0A337S1T7_FELCA
Original site: A0A337S1T7_FELCA 
ID   A0A337S1T7_FELCA        Unreviewed;       984 AA.
AC   A0A337S1T7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Receptor tyrosine-protein kinase erbB-2 {ECO:0000256|ARBA:ARBA00040669};
DE   AltName: Full=Proto-oncogene c-ErbB-2 {ECO:0000256|ARBA:ARBA00041969};
DE   AltName: Full=p185erbB2 {ECO:0000256|ARBA:ARBA00042465};
GN   Name=ERBB2 {ECO:0000313|Ensembl:ENSFCAP00000044040.1,
GN   ECO:0000313|VGNC:VGNC:61927};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000044040.1, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000044040.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000044040.1,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000044040.1, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000044040.1,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000044040.1}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000044040.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: In the nucleus is involved in transcriptional regulation.
CC       Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter
CC       and activates its transcription. Implicated in transcriptional
CC       activation of CDKN1A; the function involves STAT3 and SRC. Involved in
CC       the transcription of rRNA genes by RNA Pol I and enhances protein
CC       synthesis and cell growth. {ECO:0000256|ARBA:ARBA00037619}.
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: Cell projection, ruffle membrane
CC       {ECO:0000256|ARBA:ARBA00004199}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004199}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; AANG04003358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A337S1T7; -.
DR   Ensembl; ENSFCAT00000051413.2; ENSFCAP00000044040.1; ENSFCAG00000009903.6.
DR   VGNC; VGNC:61927; ERBB2.
DR   GeneTree; ENSGT00940000158232; -.
DR   Proteomes; UP000011712; Chromosome E1.
DR   Bgee; ENSFCAG00000009903; Expressed in tip of external ear and 10 other cell types or tissues.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR   CDD; cd00064; FU; 2.
DR   CDD; cd05109; PTKc_HER2; 1.
DR   CDD; cd12094; TM_ErbB2; 1.
DR   Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR   Gene3D; 4.10.1140.10; membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor like domain; 1.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24416:SF137; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 1.
DR   Pfam; PF21314; TM_ErbB1; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..984
FT                   /note="Receptor tyrosine-protein kinase erbB-2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016379530"
FT   TRANSMEM        378..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          444..711
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          753..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..883
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         477
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   984 AA;  108184 MW;  AC60DB0A4915C549 CRC64;
     MELAAWCRWG LLLALLPSGA TGTQDNYLST DVGSCTLVCP LNNQEVTAED GTQRCEKCSK
     PCARVCYGLG MEHLREARAV TSANIQEFVG CKKIFGSLAF LPESFEGDPA SNTAPLQPEQ
     LRVFEALEEI TGYLYISAWP DSLPNLSVFQ NLRVIRGRVL HDGAYSLTLQ GLGISWLGLR
     SLRELGSGLA LIHRNSRLCF VHTVPWDQLF RNPHQALLHS ANRPEDECAG EGLACYPLCA
     HGHCWGPGPT QCVNCSQFLR GQECVEECRV LQGLPREYVK DRFCLPCHPE CQPQNGSVTC
     LGSEADQCVA CAHYKDPPFC VARCPSGVKP DLSFMPIWKF ADEEGTCQPC PINCTHSCAD
     LDEKGCPAEQ RASPVTSIIA AVVGILLVVV VGLVLGILIK RRRQKIRKYT MRRLLQETEL
     VEPLTPSGAM PNQAQMRILK ETELRKVKVL GSGAFGTVYK GIWIPDGENV KIPVAIKVLR
     ENTSPKANKE ILDEAYVMAG VGSPYVSRLL GICLTSTVQL VTQLMPYGCL LDHVREHRGR
     LGSQDLLNWC VQIAKGMSYL EDVRLVHRDL AARNVLVKSP NHVKITDFGL ARLLDIDETE
     YHADGGKVPI KWMALESILR RRFTHQSDVW SYGVTVWELM TFGAKPYDGI PAREIPDLLE
     KGERLPQPPI CTIDVYMIMV KCWMIDSECR PRFRELVAEF SRMARDPQRF VVIQNEDLGP
     ASPLDSTFYR SLLEDEDMGD LVDAEEYLVP QQGFFCPDPA PGAGGTAHRR HRSSSTRSGG
     GELTLGLEPS EEEPPKSPLA PSEGAGSDVF DGDLGMGAAK GLQSLSPQDP SPLQRYSEDP
     TVPLPPETDG YVAPLTCSPQ PEYVNQPEVW PKPPSPLEGP LPPSRPAGAT LERPKTLSPK
     TLSPGKNGVV KDVFAFGGAV ENPEYLAPRG RAAPQPHPPP AFSPAFDNLY YWDQDTSERG
     SPPSTFEGTP TAENPEYLGL DVPV
//
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