ID M4A992_XIPMA Unreviewed; 1000 AA.
AC M4A992;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Discoidin domain receptor tyrosine kinase 1 {ECO:0000313|Ensembl:ENSXMAP00000011036.1};
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 {ECO:0000313|Ensembl:ENSXMAP00000011036.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000011036.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000011036.1};
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}.
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DR RefSeq; XP_014324168.1; XM_014468682.1.
DR Ensembl; ENSXMAT00000011050.2; ENSXMAP00000011036.1; ENSXMAG00000010994.2.
DR Ensembl; ENSXMAT00000028573.1; ENSXMAP00000026031.1; ENSXMAG00000010994.2.
DR GeneID; 102233647; -.
DR KEGG; xma:102233647; -.
DR CTD; 780; -.
DR eggNOG; KOG1094; Eukaryota.
DR GeneTree; ENSGT00940000159733; -.
DR HOGENOM; CLU_008873_2_0_1; -.
DR OMA; DVQVFSH; -.
DR OrthoDB; 2999496at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:UniProt.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.60.120.1190; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR048525; DDR1-2_DS-like.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF333; EPITHELIAL DISCOIDIN DOMAIN-CONTAINING RECEPTOR 1; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF21114; DDR1-2_DS-like; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00023137}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Signal {ECO:0000256|SAM:SignalP};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1000
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041118721"
FT TRANSMEM 464..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..190
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 693..992
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 387..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1000 AA; 111200 MW; 82F452CE08CDC978 CRC64;
MASTTTRLLL VSVISVLAEF VVSSEDHKWH FDPTQCRYAM GMEDGTIPDS DITASSAWSD
STEAKHGRLS TGEGDGAWCP AAPVFPNESE YLQIDLHKLH FVALVGTQGR HADGHGQEFV
RSYRLRYSRD GKKWITWQDR WGQEVVSGNE NTYEIVLKDL GPPIVARMVR FYPLADRVMS
VCLRVELYGC VWNDGLNAYT APVGHVMNLP GMPVYLNDST YDGSTEQGMQ FGGLGQLCDG
VLGGDDFIET KELRVWPGYD YLGWSREALG QGSVDIEFHF EKPRRFNNMQ VHSNNRHTQG
VRVFSKVECL FKPGLLQPWS SPALTLPVPL EDLKDPSSRP ISLPLGGRPA QILRCKFYFA
DRWLLISEIS FLSEPFEEDE TDADSFLHNR RKFPDPSPTP VGNVTTSVPT SSHGSFSTSS
KPSEPPTATS LMMDTTANWT LSEFAAFTPR AGLPVAKDDG SNTAILIGCL VGIILLLLAV
IVVILWRQYW KKILGKAQGS LSSSELRVHL SVPSDNVVIN NTHSYSSRYQ RIHTFPDDRD
QDREAEGEYQ EPSALLRPRD QRDSTTLLLN NPAYHVLLPD HRKGSRAVVV PRSAQAQEKS
LNVPQACGLD LDLEKGFPSA HEEPPPYPGS PPYPSLSPPV SPPLPPSVPH YAEADIVSLQ
GVSGNNTYAV PALASSSPGA DALPLPELPR QCLVFKEKLG EGQFGEVHLC EIENPLDLPI
LEFPFNVRKG RPLLVAVKIL RPDASKNARN DFLKEVKILS RLKDPNIIRL LGVCVSSDPL
CMVTEYMECG DLNQYLSQRV LLDKTGPSHN TPTISYPALI SMASQIASGM KFLSSLNFVH
RDLATRNCLV GGEKGESGED RGGERHIKIA DFGMSRNLYA GDYYRIQGRA VLPIRWMAWE
CILMGKFTTA SDVWAFGVTL WEMLSVCQEQ PYSDLTDEQV IDNAGEFFRD QGRQVYLSRP
AVCPQGLYEL MLSCWNRDCK LRPSFANIHS FLTEDAMNMV
//
