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Database: UniProt
Entry: A0A6P6RNP6_CARAU
LinkDB: A0A6P6RNP6_CARAU
Original site: A0A6P6RNP6_CARAU 
ID   A0A6P6RNP6_CARAU        Unreviewed;       976 AA.
AC   A0A6P6RNP6;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   28-JAN-2026, entry version 25.
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=LOC113120987 {ECO:0000313|RefSeq:XP_026146950.1};
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957 {ECO:0000313|Proteomes:UP000515129, ECO:0000313|RefSeq:XP_026146950.1};
RN   [1] {ECO:0000313|RefSeq:XP_026146950.1}
RP   IDENTIFICATION.
RC   STRAIN=Wakin {ECO:0000313|RefSeq:XP_026146950.1};
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_026146950.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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}.
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DR   RefSeq; XP_026146950.1; XM_026291165.1.
DR   AlphaFoldDB; A0A6P6RNP6; -.
DR   GeneID; 113120987; -.
DR   Proteomes; UP000515129; Chromosome 20.
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: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:0030318; P:melanocyte differentiation; IEA:UniProtKB-ARBA.
DR   GO; GO:0097324; P:melanocyte migration; IEA:UniProtKB-ARBA.
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   CDD; cd00096; Ig; 1.
DR   FunFam; 1.10.510.10:FF:000177; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 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; 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:SF46; MAST_STEM CELL GROWTH FACTOR RECEPTOR KIT; 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; 1.
DR   PIRSF; PIRSF500951; SCGF_recepter; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
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:UP000515129};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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..976
FT                   /note="Mast/stem cell growth factor receptor"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT                   /id="PRO_5028556965"
FT   TRANSMEM        512..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT   DOMAIN          23..100
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          205..301
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          399..504
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          580..922
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          932..976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        932..941
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        942..976
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        777
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         559
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         587..594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         662..668
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         781
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         782
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         795
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            921
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ   SEQUENCE   976 AA;  109335 MW;  E71729C72076931B CRC64;
     MEYHYVLFTV LLQLIVQPAR SRPTITPEGP QLTVPLNSDF SLQCQSDSSV RWLREDRPTR
     ILKEQRQGQV TVLKVSKAGP QHMGKYSCQE EESGEKSSIY VYVKADPENP FRRNIVFDFV
     AGQGEMITLP CLATDPRMTD LHLQKCDGQP LPNNLRYSSS IETGITLEDV RKDFEGCYIC
     VGTLEGNTVK SGQYQLNVRL VPDAPPVITL GRPQRVLLVQ GEELALSCST SNVNSDITIR
     WKAPHGVQPS VQQFSRILTE PISHLRNATL NLGSVTMQDA GIYNCEARNE RGTSAKTVMV
     EIFDKGFINV TSVNNSTKRM RAGESLSLRV VMDAYPKPHT FSWSYSGVKL TNTTDHVITS
     RSHGNSYTSE LKLVRLKVLE SGVYTFSCSN RDATVHQTFE VHVISKPQIV SYEGPIDGQV
     RCVAEGYPTP QIKWFYCDQP HSRCSNLLNA TQEEEDVVTV TMTNPPFGKG TVESRLNITK
     NSYATLECVA SANGEIVYTL FAISENTVPH ELFTPLLIGF VAAAVILVLI LIVLSYKYMQ
     KPKYQIQWKV IEGIHGNSYV YIDPTQLPYD HQWEFPRDKL RFGKTLGSGA FGKVVEATAY
     GMSKADTVMT VAVKMLKPSA HATEKEALMS ELKVLSYLGN HINIVNLLGA CTVGGPTLVI
     TEYCCFGDLL NFLRRRRESF YFTTLGEDSY YRNVMLQPEP NESRNGYMTM KPSVMGLLSS
     ENRRSLNKGD SYSDSDAISE ILQEDGMTMD TEDLLSFSYQ VAKGMDFLAS KNCIHRDLAA
     RNILLTQGRV AKICDFGLAR DITTDSNYVV KGNARLPVKW MSPESIFECV YTFESDVWSY
     GILLWEIFSL GSSPYPGMPV DSKFYKMIKE GYRMESPEFA PSEMYEIMHS CWDADPFKRP
     SFGKIVEKIE QQISDSTKHI YLNFSSRLPA ASGSHEGSSS HVQRLNSVGT HSTTTQPLLS
     SNDVYFEGTS SRHPPV
//
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