ID A0A2K6EBT9_MACNE Unreviewed; 1253 AA.
AC A0A2K6EBT9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|PIRNR:PIRNR000619};
DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000619};
GN Name=ERBB2 {ECO:0000313|Ensembl:ENSMNEP00000045618.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000045618.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000045618.1}
RP IDENTIFICATION.
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}.
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 AlphaFoldDB; A0A2K6EBT9; -.
DR Ensembl; ENSMNET00000070131.1; ENSMNEP00000045618.1; ENSMNEG00000045300.1.
DR GeneTree; ENSGT00940000158232; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000045300; Expressed in adult mammalian kidney and 11 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; IEA:UniProt.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR CDD; cd00064; FU; 3.
DR CDD; cd05109; PTKc_HER2; 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; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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:SF137; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2; 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; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 3.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000233120};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
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 TRANSMEM 649..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 1032..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1155
FT /note="Pro 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 1253 AA; 138130 MW; 1558E49883BD872B CRC64;
PYTPSVCGWG IPVSLEWSVT LWVWEMCTGT DMKLRLPASP ETHLDMLRHL YQGCQVVQGN
LELTYLPTNA SLSFLQDIQE VQGYVLIAHN QVRQVPLQRL RIVRGTQLFE DNYALAVLDN
GDPLNNTTPV TGASPGGLRE LQLRSLTEIL KGGVLIQRNP QLCYQDTILW KDIFHKNNQL
ALTLIDTNRS RACHPCSPVC KGSRCWGESS EDCQSLTRTV CAGGCARCKG PLPTDCCHEQ
CAAGCTGPKH SDCLACLHFN HSGICELHCP ALVTYNTDTF ESMPNPEGRY TFGASCVTAC
PYNYLSTDVG SCTLVCPLHN QEVTAEDGTQ RCEKCSKPCA RVCYGLGMEH LREVRAVTSA
NIQEFAGCKK IFGSLAFLPE SFDGDPASNT APLQPEQLRV FETLEEITGY LYISAWPDSL
PDLSVLQNLQ VIRGRILHNG AYSLTLQGLG ISWLGLRSLR ELGSGLALIH HNTRLCFVHT
VPWDQLFRNP HQALLHTANR PEDECVGEGL ACHQLCARGH CWGPGPTQCV NCSQFLRGQE
CVEECRVLQG LPREYVNARH CLPCHPECQP QNGSVTCFGP EADQCVACAH YKDPPFCVAR
CPSGVKPDLS YMPIWKFPDE EGTCQPCPIN CTHSISLGCP SWSQTRGPLT SIISAVVGIL
LVVVLGVVFG ILIKRRQQKI RKYTMRRLLQ ETELVEPLTP SGAMPNQAQM RILKETELRK
VKVLGSGAFG TVYKGIWIPD GENVKIPVAI KVLRENTSPK ANKEILDEAY VMAGVGSPYV
SRLLGICLTS TVQLVTQLMP YGCLLDHVRE NRGRLGSQDL LNWCMQIAKG MSYLEDVRLV
HRDLAARNVL VKSPNHVKIT DFGLARLLDI DETEYHADGG KVPIKWMALE SILRRRFTHQ
SDVWSYGVTV WELMTFGAKP YDGIPAREIP DLLEKGERLP QPPICTIDVY MIMVKCWMID
SECRPRFREL VSEFSRMARD PQRFVVIQNE DLGPASPLDS TFYRSLLEDD DMGDLVDAEE
YLVPQQGFFC PDPAPGTGGM VHHRHRSSST RSGGGDLTLG LEPSEEEAPR SPRAPSEGTG
SDVFDGDLGM GAAKGLQSLP AHDPSPLQRY SEDPTVPLPS ETDGYVAPLT CSPQPEYVNQ
PDVRPQPPSP QEGPLSPARP TGATLERPKT LSPGKNGVVK DVFAFGGAVE NPEYLAPRGG
AAPQPHLPPA FSPAFDNLYY WDQDPSERGA PPSTFKGTPT AENPEYLGLD VPV
//
