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Tyrosine-protein kinase transforming protein fms (EC 2.7.10.1)

 KFMS_FSVMD              Reviewed;         978 AA.
P00545; Q86597;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 2.
20-JUN-2018, entry version 132.
RecName: Full=Tyrosine-protein kinase transforming protein fms;
EC=2.7.10.1;
Name=V-FMS;
Feline sarcoma virus (strain McDonough).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Gammaretrovirus.
NCBI_TaxID=11778;
NCBI_TaxID=9681; Felidae (cat family).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6582485; DOI=10.1073/pnas.81.1.85;
Hampe A., Gobet M., Sherr C.J., Galibert F.;
"Nucleotide sequence of the feline retroviral oncogene v-fms shows
unexpected homology with oncogenes encoding tyrosine-specific protein
kinases.";
Proc. Natl. Acad. Sci. U.S.A. 81:85-89(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, AND
PHOSPHORYLATION AT THR-973.
PubMed=1833563;
Smola U., Hennig D., Hadwiger-Fangmeier A., Schuetz B., Pfaff E.,
Niemann H., Tamura T.;
"Reassessment of the v-fms sequence: threonine phosphorylation of the
COOH-terminal domain.";
J. Virol. 65:6181-6187(1991).
-!- FUNCTION: Truncated version of the receptor for colony-stimulating
factor 1 (CSF-1).
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- MISCELLANEOUS: This protein is synthesized as a Gag-Fms
polyprotein.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; K01643; AAA43045.1; -; Genomic_RNA.
EMBL; S59588; AAB20028.1; -; Genomic_DNA.
PIR; A00654; TVMVMD.
ProteinModelPortal; P00545; -.
SMR; P00545; -.
iPTMnet; P00545; -.
BRENDA; 2.7.10.2; 2234.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019955; F:cytokine binding; IEA:InterPro.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:InterPro.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR030658; CSF-1_receptor.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500947; CSF-1_receptor; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 4.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 5.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
ATP-binding; Disulfide bond; Glycoprotein; Immunoglobulin domain;
Kinase; Membrane; Nucleotide-binding; Oncogene; Phosphoprotein;
Receptor; Repeat; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
CHAIN 1 978 Tyrosine-protein kinase transforming
protein fms.
/FTId=PRO_0000155209.
TOPO_DOM 1 543 Extracellular. {ECO:0000255}.
TRANSMEM 544 568 Helical. {ECO:0000255}.
TOPO_DOM 569 978 Cytoplasmic. {ECO:0000255}.
DOMAIN 55 134 Ig-like C2-type 1.
DOMAIN 141 231 Ig-like C2-type 2.
DOMAIN 236 331 Ig-like C2-type 3.
DOMAIN 333 431 Ig-like C2-type 4.
DOMAIN 434 533 Ig-like C2-type 5.
DOMAIN 613 942 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 619 627 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 810 810 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 647 647 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 841 841 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 973 973 Phosphothreonine.
{ECO:0000269|PubMed:1833563}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 369 369 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 511 511 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 76 118 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 161 211 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 258 312 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 451 516 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 714 714 L -> P (in Ref. 1; AAA43045).
{ECO:0000305}.
CONFLICT 971 978 QRTPPVAR -> RGPPL (in Ref. 1; AAA43045).
{ECO:0000305}.
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


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