XMRK_XIPMA
ID XMRK_XIPMA Reviewed; 1167 AA.
AC P13388;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Melanoma receptor tyrosine-protein kinase;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=xmrk; Synonyms=tu;
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2797166; DOI=10.1038/341415a0;
RA Wittbrodt J., Adam D., Malitschek B., Maueler W., Raulf F., Telling A.,
RA Robertson S.M., Schartl M.;
RT "Novel putative receptor tyrosine kinase encoded by the melanoma-inducing
RT Tu locus in Xiphophorus.";
RL Nature 341:415-421(1989).
RN [2]
RP SEQUENCE REVISION TO 515.
RA Schartl M.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=1846957;
RA Adam D., Maueler W., Schartl M.;
RT "Transcriptional activation of the melanoma inducing Xmrk oncogene in
RT Xiphophorus.";
RL Oncogene 6:73-80(1991).
CC -!- FUNCTION: Probable receptor with tyrosine-protein kinase activity.
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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DISEASE: Note=Involved in pigment cells malignant melanomas.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X16891; CAA34770.2; -; mRNA.
DR PIR; S06142; S06142.
DR AlphaFoldDB; P13388; -.
DR SMR; P13388; -.
DR STRING; 8083.ENSXMAP00000008832; -.
DR PRIDE; P13388; -.
DR InParanoid; P13388; -.
DR BRENDA; 2.7.10.1; 6733.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00064; FU; 3.
DR Gene3D; 3.80.20.20; -; 2.
DR Gene3D; 6.10.250.2930; -; 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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
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 PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 5.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..25
FT CHAIN 26..1167
FT /note="Melanoma receptor tyrosine-protein kinase"
FT /id="PRO_0000016678"
FT TOPO_DOM 26..642
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..1167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 710..977
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 835
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 716..724
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 743
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 195..204
FT /evidence="ECO:0000250"
FT DISULFID 199..212
FT /evidence="ECO:0000250"
FT DISULFID 220..228
FT /evidence="ECO:0000250"
FT DISULFID 224..236
FT /evidence="ECO:0000250"
FT DISULFID 237..245
FT /evidence="ECO:0000250"
FT DISULFID 241..253
FT /evidence="ECO:0000250"
FT DISULFID 256..265
FT /evidence="ECO:0000250"
FT DISULFID 269..296
FT /evidence="ECO:0000250"
FT DISULFID 300..311
FT /evidence="ECO:0000250"
FT DISULFID 315..330
FT /evidence="ECO:0000250"
FT DISULFID 333..337
FT /evidence="ECO:0000250"
FT DISULFID 504..513
FT /evidence="ECO:0000250"
FT DISULFID 508..521
FT /evidence="ECO:0000250"
FT DISULFID 524..533
FT /evidence="ECO:0000250"
FT DISULFID 537..553
FT /evidence="ECO:0000250"
FT DISULFID 556..569
FT /evidence="ECO:0000250"
FT DISULFID 560..577
FT /evidence="ECO:0000250"
FT DISULFID 593..615
FT /evidence="ECO:0000250"
FT DISULFID 618..626
FT /evidence="ECO:0000250"
FT DISULFID 622..634
FT /evidence="ECO:0000250"
SQ SEQUENCE 1167 AA; 129934 MW; 4793E0749DC1D55A CRC64;
MEFLRGGAAL LQLLLVLSIS RCCSTDPDRK VCQGTSNQMT MLDNHYLKMK KMYSGCNVVL
ENLEITYTQE NQDLSFLQSI QEVGGYVLIA MNEVSTIPLV NLRLIRGQNL YEGNFTLLVM
SNYQKNPSSP DVYQVGLKQL QLSNLTEILS GGVKVSHNPL LCNVETINWW DIVDKTSNPT
MNLIPHAFER QCQKCDHGCV NGSCWAPGPG HCQKFTKLLC AEQCNRRCRG PKPIDCCNEH
CAGGCTGPRA TDCLACRDFN DDGTCKDTCP PPKIYDIVSH QVVDNPNIKY TFGAACVKEC
PSNYVVTEGA CVRSCSAGML EVDENGKRSC KPCDGVCPKV CDGIGIGSLS NTIAVNSTNI
RSFSNCTKIN GDIILNRNSF EGDPHYKIGT MDPEHLWNLT TVKEITGYLV IMWWPENMTS
LSVFQNLEII RGRTTFSRGF SFVVVQVRHL QWLGLRSLKE VSAGNVILKN TLQLRYANTI
NWRRLFRSED QSIEYDARTE NQTCNNECSE DGCWGPGPTM CVSCLHVDRG GRCVASCNLL
QGEPREAQVD GRCVQCHQEC LVQTDSLTCY GPGPANCSKS AHFQDGPQCI PRCPHGILGD
GDTLIWKYAD KMGQCQPCHQ NCTQGCSGPG LSGCRGDIVS HSSLAVGLVS GLLITVIVAL
LIVVLLRRRR IKRKRTIRCL LQEKELVEPL TPSGQAPNQA FLRILKETEF KKDRVLGSGA
FGTVYKGLWN PDGENIRIPV AIKVLREATS PKVNQEVLDE AYVMASVDHP HVCRLLGICL
TSAVQLVTQL MPYGCLLDYV RQHQERICGQ WLLNWCVQIA KGMNYLEERH LVHRDLAARN
VLLKNPNHVK ITDFGLSKLL TADEKEYQAD GGKVPIKWMA LESILQWTYT HQSDVWSYGV
TVWELMTFGS KPYDGIPAKE IASVLENGER LPQPPICTIE VYMIILKCWM IDPSSRPRFR
ELVGEFSQMA RDPSRYLVIQ GNLPSLSDRR LFSRLLSSDD DVVDADEYLL PYKRINRQGS
EPCIPPTGHP VRENSITLRN ISDPTQNALE KDLDGHEYVN QPGSETSSRL SDIYNPNYED
LTDGWGPVSL SSQEAETNFS RPEYLNTNQN SLPLVSSGSM DDPDYQAGYQ AAFLPQTGAL
TGNGMFLPAA ENLEYLGQGG ALYTPVR
