UniProt: A0AAD6A6L9

Database: UniProt
Entry: A0AAD6A6L9_9TELE

LinkDB:  A0AAD6A6L9_9TELE 
Original site:  A0AAD6A6L9_9TELE

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (22)   
   InterPro (12)   
   Pfam (3)   
   PROSITE (5)   
   SMART (2)   
All databases (32)   

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ID   A0AAD6A6L9_9TELE        Unreviewed;      1670 AA.
AC   A0AAD6A6L9;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   ORFNames=JOQ06_000089 {ECO:0000313|EMBL:KAJ4919404.1};
OS   Pogonophryne albipinna.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Pogonophryne.
OX   NCBI_TaxID=1090488 {ECO:0000313|EMBL:KAJ4919404.1, ECO:0000313|Proteomes:UP001219934};
RN   [1] {ECO:0000313|EMBL:KAJ4919404.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SGF0006 {ECO:0000313|EMBL:KAJ4919404.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAJ4919404.1};
RA   Jo E.;
RT   "Chromosome-level genome of Pogonophryne albipinna.";
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00051243};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
CC       protein {ECO:0000256|RuleBase:RU000311}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. CSF-1/PDGF receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000311}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAJ4919404.1}.
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DR   EMBL; JAPTMU010000295; KAJ4919404.1; -; Genomic_DNA.
DR   Proteomes; UP001219934; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; IEA:TreeGrafter.
DR   GO; GO:0048407; F:platelet-derived growth factor binding; IEA:TreeGrafter.
DR   GO; GO:0001525; P:angiogenesis; IEA:TreeGrafter.
DR   GO; GO:0060326; P:cell chemotaxis; IEA:TreeGrafter.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:TreeGrafter.
DR   FunFam; 1.10.510.10:FF:001927; Receptor protein-tyrosine kinase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR050122; RTK.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   PANTHER; PTHR24416:SF53; PLATELET-DERIVED GROWTH FACTOR RECEPTOR BETA; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF25305; Ig_PDGFR_d4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW   ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW   Reference proteome {ECO:0000313|Proteomes:UP001219934};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000311};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1670
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5042283239"
FT   DOMAIN          119..192
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          625..778
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1002..1518
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1170..1221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1539..1573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1586..1670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1179..1190
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1207..1217
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1593..1607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1608..1659
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1036
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1670 AA;  179879 MW;  440C5B5A05864926 CRC64;
     MASTRGRTGS LNLLHFLLGV FLVPSFLSLE LLPSANQVLL NSSSNYSVVS NLSVSLQVCS
     GACLSLQQVC SGACLSLQQV PVCLSAGVFR CLSVSATGVF RYLSVSAATC LSLQQVPVCL
     SAGVFRFLSI SLQVCSGWSQ VTWLLPAVPE GGVVQVEPLG SSSVLRLLNA SWRDSGRYTC
     EEAGSPERRQ VDVFIPGTGP EEWFVPRLSG VVQRSGLSRG SQVQRSGLSR GSQVQRSGLS
     RGSQVWLCYA NPYSLTPLRS RGVVCPEALR CGPEEWFVPR LSGPEEWFVP RLSGPEEWFV
     PRLSGPEEWF VPRLSGVVMQ VGLEDTVPCG VSDPRLNVSL FERHSRTPVT TATYEPGRGF
     TGKLNDTSYT CTATGGGAES QSQVYYVFSI SLSRWRCTCL TTCLSLSPSA GGGVPVSPPV
     CLSVPQRVEV YLSHHLSVSQ SLSRWRCTYL TTCLSPSPSA GGGVPVSPPV CLSVPQQVEV
     YLSHHLSVSQ SLSRWRCTCL TTCLSLSPSA GGGVPVSPPV CLSVPQQVEV YLSHHLSVSQ
     SLSRWRCTCL TTCLSLSPSA GGGVPVSPPV CLPVPQQVEV YLSHHLSVSQ SLSRWRCTCL
     TTCLSLSPSA GGGVPVSPPV CLSVPQQVEV YLSVSRSVLK VGESLMVNCT VRDVDMVFFT
     WDFPRRQEVE PMTDFLPNHI RSFVNISAAT VEDSGETHLS ALLHHTVTLS VEADAHPPPT
     VLWTKDNNTV ATETSAVNTT HLTGSRYLST LTLVGVRLHQ TGSYTASVSN EDEAEEVVFN
     LEVKAPPRIT SLSEVGSQEM LCAAEGAPPP NITWYTCHSS HRCSNATSGW RSQSAASEDN
     VTKDIGITTD LTVLQYFLFG DKPRYEARWK LMESVSPDGP QNILDPHSWE IPRDNVVLVL
     GNTLYLSLYL STCLSTCLPV SLPVSLPVYL SLYLSTCLST CLPVSLPVYL SLYLSTCLTT
     CLTTCLPVSL PLYLSLYLST CLSTCLPVSL PVYLSLYLSL YLSTCQVLGS GAFGRVVEAS
     VSDLIHSHSN TKVAVKMVKQ RSGVQSLVSE LKVLVHIGPH LNLVNLLGAC TRGDLVNYLQ
     RNKHTFLQSD THTKSDGGYM DMTSETQYVA MKELSPAHIQ PAEYEELCTP AGQQEGPPPL
     SDAPPLSLMD LLSFSFQIAQ AMDFLSSRNT PGGDFRAGTP GGDSGWGTPG GDFRAGTSGR
     GLRVGDSGRG PPGGGLRGPL KDWKRCPSED PPHECVSSSV SVSVSPPHEC VSSSVSVCVC
     VLLTECVCVL LSECVSSSVS VECVSSSVSV CPPHECVSSS VSVCVCVLLT ECVCVLLSEC
     VSSSVSVECV SSSLSVCPPH ECVSSSLSVC PPQLVCECVS SSLSVCPPHE CVSSSLSVVH
     RDLAARNVLV CEGKLLKVCD LSLARDLMKD KDYTARGIRF LPVRWMSPES LFQNLFSCQS
     DVWSYGVLLW ELFSLGASPY PELPRTQDFC SSLKTGNRMT RPEHAPLHMY DLMKVCWAES
     PQSRPSFSSL VVSVGNLLTE DYRKRYLQLT EDFLSSPAVL RSRRSSPGAD GGSPDAQVLE
     AGPEEAGSSQ TTYFIPITDV TIETRGGAAQ DAASPQLSQS QDTQKWTSPE DRQEGTSPED
     RQEGTSPEDR QEGTSPEDRQ EGTSPEDRQE GTSPEDRQKG TSPEEEESSL
//

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