ID S9YT31_CAMFR Unreviewed; 1253 AA.
AC S9YT31;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|PIRNR:PIRNR000619};
DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000619};
GN ORFNames=CB1_000261013 {ECO:0000313|EMBL:EPY87155.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY87155.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY87155.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
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 EMBL; KB016554; EPY87155.1; -; Genomic_DNA.
DR AlphaFoldDB; S9YT31; -.
DR Proteomes; UP000030684; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 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; 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; 2.
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:UP000030684};
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 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 1037..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1157
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; 137846 MW; F18C3ED45581134F CRC64;
MSVFLLSPPV WQGTEGRSGA EARGTYRAVV CTGTDMKLRL PASPETHLDM LRYLYQGCQV
VQGNLELTYL PANASLSFLQ DIQEVQGYVL IAHNQVSRVP LQRLRIVRGT QLFEDNYALA
VLDNADLLES ATPAVGATPG GLQELQLRSL TEILKGGVLI QRNPQLCYQD TILWKDIFHK
NNQPALMLID TNRSRDLTGT VCASGCARCK GPQPTDCCHE QCAAGCTGPK HSDCLACLHF
NHSGICELHC PALVTYNTDT FESMPNPEGR YTFGASCVTA CPLTQLKVEH EHMILISSDN
YLSTDVGSCT LVCPLNNQEV TAEDGTQRCE KCSKPCARVC YGLGMEHLRE VRAVTSANIQ
EFTGCKKIFG SLAFLPESFE GDPASNTGPL QPEQLRVFES LEEITGYLYI SAWPDSLPDL
SVFQNLRVIR GRILHEGAYS LTLQGLGISW LGLRSLRELG SGLALIHRNA HLCFVHTVPW
DQLFRNPHQA LLHSANRPED ECVGKGLTCH SLCAHGHCWG PGPTQCVNCS QFLRGQECVE
ECRVLQGVPR EYVKDRHCLP CHPECQPQNG SVTCSGSEAD QCVACTHYKD PPFCVARCPS
GVKPDLSFMP IWKFPDEEGT CQPCPINCTH SCVDLDDKGC PAEQRASPVT SIIAAVVGIL
LAVVMGLVFG ILIKRRRQKI RKYTMRRLLQ ETELVEPLTP SGAMPNQAQM RILKETELRK
VKVLGSGAFG TVYKGIWIPD GENVKIPVAI KVLRENTSPK ANKEILDEAY VMAGVGSPYV
SRLLGICLTS TVQLVTQLMP YGCLLDHVRE HRGRLGSQDL LNWCVQIAKG MSYLEDVRLV
HRDLAARNVL VKSPNHVKIT DFGLARLLDI DETEYHADGG KVPIKWMALE SILRRRFTHQ
SDVWSYGVTV WELMTFGAKP YDGIPAREIP DLLEKGERLP QPPICTIDVY MIMVKCWMID
SECRPRFREL VAEFSRMARD PQRFVVIQNE DLGPASPLDS TFYRSLLEDD DMGDLVDAEE
YLVPQQGFFC PDPALGAGGT AHRRHRSTST RSGGGELMLG LEPSEEEPPK SPLAPSEGAG
SDVFDGDLGM GAAKGLQTLP QHDSSPLQRY SEDPTGPLPP ETDGYVAPLT CSPQPEYVNQ
PEVRPQPPSP LEGPLPPSRP AGATLERPKT LSPGKNGVVK DVFAFGAAVE NPEYLAPQGR
AAPQSRPSPA FSPAFDNLYY WDQDPSERGA PPSTFEGTPT AENPEYLGLD APV
//
