ID A0A6A5FMI8_PERFL Unreviewed; 956 AA.
AC A0A6A5FMI8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 08-OCT-2025, 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 ORFNames=PFLUV_G00008540 {ECO:0000313|EMBL:KAF1395148.1};
OS Perca fluviatilis (European perch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8168 {ECO:0000313|EMBL:KAF1395148.1, ECO:0000313|Proteomes:UP000465112};
RN [1] {ECO:0000313|EMBL:KAF1395148.1, ECO:0000313|Proteomes:UP000465112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:KAF1395148.1};
RA Roques C., Zahm M., Cabau C., Klopp C., Bouchez O., Donnadieu C., Kuhl H.,
RA Gislard M., Guendouz S., Journot L., Haffray P., Bestin A., Morvezen R.,
RA Feron R., Wen M., Jouanno E., Herpin A., Schartl M., Postlethwait J.,
RA Schaerlinger B., Chardard D., Lecocq T., Poncet C., Jaffrelo L.,
RA Lampietro C., Guiguen Y.;
RT "A chromosome-scale genome assembly of the European perch, Perca
RT fluviatilis.";
RL Submitted (JUN-2019) 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:KAF1395148.1}.
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DR EMBL; VHII01000001; KAF1395148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A5FMI8; -.
DR OrthoDB; 6077854at2759; -.
DR Proteomes; UP000465112; Chromosome 1.
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 CDD; cd00096; Ig; 1.
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; 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; 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; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 1.
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:UP000465112};
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..956
FT /note="Mast/stem cell growth factor receptor"
FT /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT /id="PRO_5025720811"
FT TRANSMEM 519..543
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT DOMAIN 210..306
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 587..902
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 698..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 767
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 566
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 594..601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 669..675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 771
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 772
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 785
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 911
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 956 AA; 107241 MW; DAC8ECD9E395C6A3 CRC64;
MKCHWVVFVS HFVLLPLTVR CQPVISPNGP YIVVPKTGKL ELRCRDNATT SGALSKLRWQ
WERARRLEGE VEEGGVAYVK VAAAQAYHMG RYVCVNNSTQ EHSSIYVYVK DPQNVFQRTM
VNNILVRSGE NCTIPCLVTD PDVTLVALES CDGQPLPSSM SYHSNLQRGV IISNVRKEYD
GCFVCVGQLA GVKVKSSQYT VDVRLVPEVP PVITLSRKDP VILRKGEQFE ITCSSVNINP
DFSVKWNFPS TAHPDKSQTS HILSGARGYQ RATSLLITAV NQSDSGTYRC HAQNERGTSA
TAVQLDVRDQ GFITILGPPG PVQADVKEGE SLGLRVEFDA YPAPSSMFWS YNGIQILNTT
EHVITIHRHK YRLISKLRLV RVLSSEGGIY KFSASHEDAS EEHSFHIYVI SKPVIIAQEG
PVDGQVRCIA AGYPVPKISW YFCELPHTRC SHLPNATQWE TTDVSMVTES TFGRSEVVSR
LNVSKEHAHY HTLECVASTV GEEAYTLFSI SERIVPHRLF TPLLTGMVAT GVFLCLTLVV
LLYKYMQKPK FQIQWKVIES IHGNNYIYID PTQLPYDSKW EFPRQKLRFG KTLGSGAFGK
VVRATAYGLC SADTITTVAV KMLKPNAHAT EKEALMSELK VLSYLGNHVN IVNLLGACTV
GGPILVITEY CCYGDLLNFL RRKRESFLNS QVGDGYHRNV SNQTEPTTSR EVTRPGYVPM
LPSEKERSSQ SADVEELSLD TEDLLSFSYQ VAKGMEYITS KNCIHRDLAA RNILLTHGRV
AKICDFGLAR DITTDASYVL RGNARLPVKW MSPESIFDCV YTFESDVWSY GILLWEIFSL
GNSPYPGMQV GSVFYRMIQD GHRMSRPEFA PIEMYDMMLS CWNQDPLKRP SFRKLVERTE
LMLSENTRNV YLTLSNAPGH PEHQRTPSRR LSSVCSTTAP TQPLLQSTAD VFLDYV
//
