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Database: UniProt
Entry: W5KIA4_ASTMX
LinkDB: W5KIA4_ASTMX
Original site: W5KIA4_ASTMX 
ID   W5KIA4_ASTMX            Unreviewed;      1375 AA.
AC   W5KIA4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000007316.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000007316.2}
RP   IDENTIFICATION.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR   STRING; 7994.ENSAMXP00000007316; -.
DR   Ensembl; ENSAMXT00000007316.2; ENSAMXP00000007316.2; ENSAMXG00000007117.2.
DR   eggNOG; KOG1095; Eukaryota.
DR   eggNOG; KOG3610; Eukaryota.
DR   GeneTree; ENSGT00940000157842; -.
DR   HOGENOM; CLU_005158_0_0_1; -.
DR   InParanoid; W5KIA4; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000007117; Expressed in testis and 8 other cell types or tissues.
DR   GO; GO:0016020; C: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:0007411; P:axon guidance; IEA:UniProt.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00603; IPT_PCSR; 1.
DR   CDD; cd01179; IPT_plexin_repeat2; 1.
DR   CDD; cd05058; PTKc_Met_Ron; 1.
DR   CDD; cd11248; Sema_MET_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR001627; Semap_dom.
DR   InterPro; IPR036352; Semap_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; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR24416:SF614; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01403; Sema; 1.
DR   Pfam; PF01833; TIG; 2.
DR   PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00429; IPT; 3.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF81296; E set domains; 3.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF101912; Sema domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000617-
KW   2};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR000617-3};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000617-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, 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   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1375
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017383663"
FT   TRANSMEM        939..960
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..507
FT                   /note="Sema"
FT                   /evidence="ECO:0000259|PROSITE:PS51004"
FT   DOMAIN          1067..1330
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1356..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-1"
FT   BINDING         1073..1081
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT   BINDING         1099
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1146..1149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT   BINDING         1197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-2"
FT   MOD_RES         1223
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT   MOD_RES         1224
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT   MOD_RES         1338
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT   MOD_RES         1345
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-4"
FT   DISULFID        93..96
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT   DISULFID        99..152
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT   DISULFID        127..135
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT   DISULFID        164..167
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT   DISULFID        290..359
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT   DISULFID        377..398
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT   DISULFID        512..530
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT   DISULFID        518..552
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT   DISULFID        521..537
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
FT   DISULFID        533..543
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000617-3"
SQ   SEQUENCE   1375 AA;  154219 MW;  7FBDABF527F326C8 CRC64;
     MVQWTSPLVT CIWIQAIATV ASDTCPSTTL AAVNFSVPYP LPILLTRNPI QNIVINPVYH
     EIYVASQNLI EAVNFTLGKV WELHTGPVGS PECKVCNLCD IEKDPFPEDT DSEVLLLDTY
     LMYLYSCGSS QYGVCYFHQL HENGQPPRPS KCLFRKKFNS PAFCPDCIAS PLGTKVSMVE
     EGHHVYFYVA ATVNDSVTQR YSRKSVSVRR PLATEDGFHT DFQGLTVLPK LRRVYRIDYV
     YTFFTADFVY FLSVQREKAD QDSSPYQTRL GRLPRHEWET RRYREVVLEC RFEPKRRRRR
     NTSEAFKDIV YNVVQAAHFG KAGRDLADEL GAEEEDDILY GVFAVTDDSG VPEHDSALCA
     FPMDSVNSFI DEGVDDCCMS GPEQLSRGLC HFQPCESCPH ESMEHNASCR DQPTLVAQPY
     YRVDLFNRQM RDTLLTSLLV TRLENKTLAH IGTAEGRLLQ LVLRRSSPVI FANYSLVENQ
     RVSATAAVLP PDHLLFVVGD KMIKVPQRGP GCRHFLTCAA CLTAPAFMSC GWCSGYCSWE
     SECPADWAKE SCPPVITQFF PETAPLDGQT ELTLCGWEFQ SPSRPAISTR THEVKLGETA
     CVVQPLKSNS TLLMCKIRSL VTEPLFQPVN ITAKVHEDRV EGSYSIEGKA EMPGFTFVLP
     NISEVQPDYG PVNGGTLITI TGPYLHSGKN RKVTLDGESC PIQSVSVIEG NVSSIVCLSQ
     PVTEVKDVVL QVYIDKSRVV TTRVFRYKQT PEILSVLPDC SFDIGSIITI EGKNLDSVFK
     TIIHFKPKES HLKPVSTECL GKAKPTRMEC TTPVFHRDET EEGELSFDMD GALGLWKQDF
     SYHPYGRPIP FETEGHVLQL YPGFDEVSLH HQKLNLVNSC MKITMTVGGV DCGAKVLDNE
     ITCRIPKNLT IPNEGLPVKI TVNGYVHNVG TVRLVSNHYM VGVVLGILTA LIVGAVLAFI
     TMKHLRKKKT DSLAETRLSH YSHNHNLTGN GSVELLPIGD YRRGEIPLST TPVTPGGVAF
     PSLVYSSTLD PSLTPLMPPE KISLTSFRPE LLEEVKDVLI PAAMLNIQHH QIIGKGHFGT
     VYHGYLTDHN NREIHCAVKS LNRITDVEEV EQFLKEGILM KGFHHSNVLS LLGVLLPEEG
     LPLVVLPYMK HGDLRHFIRC ENRNPTVKDL IGFGLQVAKG MEYLAMKKFV HRDLAARNCM
     LDESYTVKVA DFGMARDVFD KEYYSIQDHR KAKLPVKWMA IESLQTQKFT SKSDVWSFGV
     LMWELLTRGA SPYPEVDPYD ITHYLLRGRR LPQPQYCPDP LFAVMLQCWD PDPERRPSFT
     TLVSEVMAIL SSLEGEHYIS LKVTYVNLDH PRPYPALTDS ADEYESSDAE EAGSD
//
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