KFMS_FSVMD
ID KFMS_FSVMD Reviewed; 978 AA.
AC P00545; Q86597;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Tyrosine-protein kinase transforming protein fms;
DE EC=2.7.10.1;
GN Name=V-FMS;
OS Feline sarcoma virus (strain McDonough).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11778;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6582485; DOI=10.1073/pnas.81.1.85;
RA Hampe A., Gobet M., Sherr C.J., Galibert F.;
RT "Nucleotide sequence of the feline retroviral oncogene v-fms shows
RT unexpected homology with oncogenes encoding tyrosine-specific protein
RT kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:85-89(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, AND PHOSPHORYLATION
RP AT THR-973.
RX PubMed=1833563; DOI=10.1128/jvi.65.11.6181-6187.1991;
RA Smola U., Hennig D., Hadwiger-Fangmeier A., Schuetz B., Pfaff E.,
RA Niemann H., Tamura T.;
RT "Reassessment of the v-fms sequence: threonine phosphorylation of the COOH-
RT terminal domain.";
RL J. Virol. 65:6181-6187(1991).
CC -!- FUNCTION: Truncated version of the receptor for colony-stimulating
CC factor 1 (CSF-1).
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- MISCELLANEOUS: This protein is synthesized as a Gag-Fms polyprotein.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; K01643; AAA43045.1; -; Genomic_RNA.
DR EMBL; S59588; AAB20028.1; -; Genomic_DNA.
DR PIR; A00654; TVMVMD.
DR SMR; P00545; -.
DR iPTMnet; P00545; -.
DR BRENDA; 2.7.10.2; 2234.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR030658; CSF-1_receptor.
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; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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 Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500947; CSF-1_receptor; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase;
KW Membrane; Nucleotide-binding; Oncogene; Phosphoprotein; Receptor; Repeat;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN 1..978
FT /note="Tyrosine-protein kinase transforming protein fms"
FT /id="PRO_0000155209"
FT TOPO_DOM 1..543
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..978
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..134
FT /note="Ig-like C2-type 1"
FT DOMAIN 141..231
FT /note="Ig-like C2-type 2"
FT DOMAIN 236..331
FT /note="Ig-like C2-type 3"
FT DOMAIN 333..431
FT /note="Ig-like C2-type 4"
FT DOMAIN 434..533
FT /note="Ig-like C2-type 5"
FT DOMAIN 613..942
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 952..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 810
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 619..627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 841
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 973
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:1833563"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 76..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 161..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 258..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 451..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 714
FT /note="L -> P (in Ref. 1; AAA43045)"
FT /evidence="ECO:0000305"
FT CONFLICT 971..978
FT /note="QRTPPVAR -> RGPPL (in Ref. 1; AAA43045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 978 AA; 108492 MW; 4C7CAC4835185EBF CRC64;
RMPSGPGHYG ASAETPGPRP PLCPASSCCL PTEAMGPRAL LVLLMATAWH AQGVPVIQPS
GPELVVEPGT TVTLRCVGNG SVEWDGPISP HWNLDLDPPS SILTTNNATF QNTGTYHCTE
PGNPRGGNAT IHLYVKDPAR PWKVLAQEVT VLEGQDALLP CLLTDPALEA GVSLVRVRGR
PVLRQTNYSF SPWHGFTIHK AKFIENHVYQ CSARVDGRTV TSMGIWLKVQ KDISGPATLT
LEPAELVRIQ GEAAQIVCSA SNIDVNFDVS LRHGDTKLTI SQQSDFHDNR YQKVLTLNLD
HVSFQDAGNY SCTATNAWGN HSASMVFRVV ESAYSNLTSE QSLLQEVTVG EKVDLQVKVE
AYPGLESFNW TYLGPFSDYQ DKLDFVTIKD TYRYTSTLSL PRLKRSESGR YSFLARNAGG
QNALTFELTL RYPPEVRVTM TLINGSDTLL CEASGYPQPS VTWVQCRSHT DRCDESAGLV
LEDSHSEVLS QVPFYEVIVH SLLAIGTLEH NRTYECRAFN SVGNSSQTFW PISIGAHTPL
PDELLFTPVL LTCMSIMALL LLLLLLLLYK YKQKPKYQVR WKIIESYEGN SYTFIDPTQL
PYNEKWEFPR NNLQFGKTLG TGAFGKVVEA TAFGLGKEDA VLKVAVKMLK STAHADEKEA
LMSELKIMSH LGQHENIVNL LGACTHGGPV LVITEYCCYG DLLNFLRRQA EAMLGPSLSV
GQDPEAGAGY KNIHLEKKYV RRDSGFSSQG VDTYVEMRPV STSSSNDSFS EEDLGKEDGR
PLELRDLLHF SSQVAQGMAF LASKNCIHRD VAARNVLLTS GRVAKIGDFG LARDIMNDSN
YIVKGNARLP VKWMAPESIF DCVYTVQSDV WSYGILLWEI FSLGLNPYPG ILVNSKFYKL
VKDGYQMAQP AFAPKNIYSI MQACWALEPT RRPTFQQICS LLQKQAQEDR RVPNYTNLPS
SSSSRLLRPW QRTPPVAR
