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Database: UniProt
Entry: A0A3Q1HM16_9TELE
LinkDB: A0A3Q1HM16_9TELE
Original site: A0A3Q1HM16_9TELE 
ID   A0A3Q1HM16_9TELE        Unreviewed;      1266 AA.
AC   A0A3Q1HM16;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000029185.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000029185.1}
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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane 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   AlphaFoldDB; A0A3Q1HM16; -.
DR   Ensembl; ENSAPOT00000020050.1; ENSAPOP00000029185.1; ENSAPOG00000014890.1.
DR   GeneTree; ENSGT00940000157842; -.
DR   Proteomes; UP000257200; Unplaced.
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   CDD; cd00603; IPT_PCSR; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
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; 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; 3.
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|PROSITE-
KW   ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200};
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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1266
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018651497"
FT   TRANSMEM        940..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..505
FT                   /note="Sema"
FT                   /evidence="ECO:0000259|PROSITE:PS51004"
FT   DOMAIN          1032..1266
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         1064
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1266 AA;  141366 MW;  A8676F4E33F17D8A CRC64;
     MVTLSALLTV YLWIQTQTAS GQQKCPPSPP WLVDFTMTYS LPYFQTDKPI QNIEVNSQVQ
     PTELYVACQN VIIAVNDSLQ KTWELKTGPV GHPECETCQV CDIETDPKDP VNTDSQVLFL
     DPDQHYLPYL YFCGSTRHGI CYIINIDEPK PETKCLYKKE RNSPTYCPDC LASPLGTKVT
     FVQEGATSLF FTAASVNESL RQKYPRRSIS VMRPLSTEDG FDVIMDVTVL PGLRDSYSID
     YIYSFSTKDH VYFLSLQREN PFNSNSTFQT RLGRLPILIP EMWMYREVVL ECRYEPKRRR
     RREAYRDIVY NGLQAAYFGR AGKDLADELR VHETEDILYG VFAEVNERGQ PQKNSALCAF
     PLTKVNHAID RGVEACCKSG PEQLSRGLCH FQPCESCPHE SNDGNDACTA KATLVSQPYY
     RVDLFNSQMR NVLFTSVLVT TTGNHTLGHF GTSDGRILQV ILTLYKPIIF ANYSVGETAV
     SRTAAVYSKD LLLFVAGNKM FRVPSAGPGC SHFMTCSMCL TAPRFMNCCW CSGSCLRENE
     CTSEWNKDSC APVITEFFPK TIPAGGETEL TLCGSEFQSP LRPAIISGKT HIITVGSAMC
     SVLSEKSSND ELVCKIHEKN PNLNLNITLQ VHEGEVEGRY SIEGTAQTSG LSFVEPTITE
     IKPGYGPMFG ETAVTLTGKY LNSGKQRDVY FGEKKCKIQT VSEETGDLSS IICYTAAAAA
     VGPVPVKVII DNFEVTATKM FLYKKDPVIH SVRPQCGFQR GSKLLIEGQN LDSAYKTVVQ
     YTSQNPVVTL QQVCNGTTNT THMECWTPAF PEEMAEEKSV PGVISIHTDG KNNLFKRRFD
     YHPDAKVIPF ENDDKVLLLK PGDTEVSLHH SKLITVSSCM KITMTIGGVP CKAQVLLNEL
     TCRIPKSLVI PSEGLPVKVS VNREVYDVGT VVYDDSSNTV IAGIVLGIVA ALVVGAGLAL
     LVMIHLRKKK RVDLSSQTSG SGMAFQGLLY TASYDHLAVP LMARDNISMV SLSSDLLEEV
     KDVLIPAEML RIEDSQIIGK GHFGTVYHGY LIDSNKQETH CAVKSLNRIT DLGEVDQFLR
     EGIIMKAFHH SNILSLLGIM LPKEGLPLVV LPYMKHGDVR HFIRSEKRNP TVKDLIGFGL
     QVAKGMEYLA QKKFVHRDLA ARNCMLDETY TVKVADFGMA RDIYDKEYYS IQDHKRVKLP
     VKWMAIESLQ TQKFTTKSDV WSYGILLWEL LTRGASPYPD VDPYDITHYL LKGRRLPQPQ
     FCPDTL
//
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