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Database: UniProt
Entry: A0A8J4X526_CLAMG
LinkDB: A0A8J4X526_CLAMG
Original site: A0A8J4X526_CLAMG 
ID   A0A8J4X526_CLAMG        Unreviewed;       962 AA.
AC   A0A8J4X526;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   RecName: Full=Mast/stem cell growth factor receptor {ECO:0000256|PIRNR:PIRNR500951};
DE            EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR500951};
GN   Name=kitb {ECO:0000313|EMBL:KAF5902251.1};
GN   ORFNames=DAT39_008018 {ECO:0000313|EMBL:KAF5902251.1};
OS   Clarias magur (Asian catfish) (Macropteronotus magur).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Clariidae; Clarias.
OX   NCBI_TaxID=1594786 {ECO:0000313|EMBL:KAF5902251.1, ECO:0000313|Proteomes:UP000727407};
RN   [1] {ECO:0000313|EMBL:KAF5902251.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CIFAMagur01 {ECO:0000313|EMBL:KAF5902251.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:KAF5902251.1};
RA   Kushwaha B., Kumar R., Das P., Joshi C.G., Kumar D., Nagpure N.S.,
RA   Pandey M., Agarwal S., Srivastava S., Singh M., Sahoo L., Jayasankar P.,
RA   Meher P.K., Koringa P.G., Iquebal M.A., Das S.P., Bit A., Patnaik S.,
RA   Patel N., Shah T.M., Hinsu A., Jena J.K.;
RT   "Clarias magur genome sequencing, assembly and annotation.";
RL   Submitted (JUL-2020) 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         ECO:0000256|PIRNR:PIRNR500951};
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|PIRNR:PIRNR500951, 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:KAF5902251.1}.
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DR   EMBL; QNUK01000094; KAF5902251.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8J4X526; -.
DR   OrthoDB; 6077854at2759; -.
DR   Proteomes; UP000727407; 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:0019955; F:cytokine binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019838; F:growth factor binding; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001667; P:ameboidal-type cell migration; IEA:UniProtKB-ARBA.
DR   GO; GO:0030183; P:B cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0038093; P:Fc receptor signaling pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:TreeGrafter.
DR   FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR   FunFam; 1.10.510.10:FF:000140; Platelet-derived growth factor receptor beta; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
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; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
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; IPR027263; SCGF_receptor.
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:SF599; MAST_STEM CELL GROWTH FACTOR RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF25305; Ig_PDGFR_d4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF500951; SCGF_recepter; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   PRINTS; PR01832; VEGFRECEPTOR.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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|PIRNR:PIRNR500951};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR500951};
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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR500951};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR500951};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR500951};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR500951};
KW   Reference proteome {ECO:0000313|Proteomes:UP000727407};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|PIRNR:PIRNR500951};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR500951};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT   CHAIN           22..962
FT                   /note="Mast/stem cell growth factor receptor"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT                   /id="PRO_5035350880"
FT   TRANSMEM        515..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT   DOMAIN          23..104
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          205..304
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          583..908
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          917..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..947
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        763
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         562
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         590..597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         665..671
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         767
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         768
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         781
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            907
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ   SEQUENCE   962 AA;  107978 MW;  7CC8F1F5CBB6D812 CRC64;
     MARAWILFAV TLLFTLPTGL FKPVITPSVP HLVILKGGQL ELRCEDNTRF YAGRLRWHRD
     KSRRVEGERM EDGAAVINLA SIQPQHMGRY TCESTQTGEK SSIYIYVKDP ESAFVRSMMN
     GLLAKEGEDC TLPCLVTDPA ITHLSPVTCS GSALPADLSF TADPQKGIII HNISKALEGC
     YVCTGLMGGT AVKSSQYDVN VRRVPESVPL INLSRSERVI LIKGEPLELI CTTSNINHDF
     SLMWSFPSGA NALESHASHI LPGSWGYKRL STLSISSALT SDSGMYRCQA RNEKGVTTAT
     IHLDVYERGF INVTEGQNRA VDVREGESLT LRVEMTSYPK PSAAYWSYNN QELKNTSEHV
     ITLHNQHYRY INELKLVRVH GSEGGIYTFS ASHNHMSVNK SFFVHVNCKP MIVSQEGPID
     GQVKCVASGY PVPKISWYYC EPRHTRCSQL MNATQEDEDT AIVTVSTSRF GRTEVESRLN
     VTRGRYHTLE CVATTQGEQA YTLFSISERT VPHKLFTPLL TGVVTASVVL MLFLIVLLYK
     YMQKPKYQIH WKVIDSIHGN NYTYIDPTQL PYDPKWEFPR ERLRFGKILG AGAFGKVVAA
     TAYGLSSPDT VTTVAVKMLK PSAHSTEKEA LMSELKVLSY LGNHMNIVNL LGACTVGGPT
     LVITEYCCYG DLLNFLRRKR DAFFSSKTGD GYYKNLLSQT QFSREDPENG YMPMRSYQKK
     SSQTEWTDDK DDLSIDTEDL LSFSYQVAKG MDFLTSKNCI HRDLAARNIL LTKGRVAKIC
     DFGLARDITK DSNYVLRGNA RLPVKWMSPE SLFSCVYTFE SDVWSYGILL WEIFSLGNSP
     YPGVPVGSMF YKMIQDGYRM SEPEFAPSEI YEVMRWCWSS DPLKRPTFRK LVERTEMLLS
     EATKHDYLNL HANGDRSISE SSDCTGLQRT PSQRLSSVDS TTASTQPLLL ATNDDQPGPK
     TF
//
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