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P00545 (KFMS_FSVMD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase transforming protein fms

EC=2.7.10.1
Gene names
Name:V-FMS
OrganismFeline sarcoma virus (strain McDonough)
Taxonomic identifier11778 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostFelidae (cat family) [TaxID: 9681]

Protein attributes

Sequence length978 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subcellular location

Membrane; Single-pass type I membrane protein.

Miscellaneous

This protein is synthesized as a Gag-Fms polyprotein.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 978978Tyrosine-protein kinase transforming protein fms
PRO_0000155209

Regions

Topological domain1 – 543543Extracellular Potential
Transmembrane544 – 56825Helical; Potential
Topological domain569 – 978410Cytoplasmic Potential
Domain55 – 13480Ig-like C2-type 1
Domain141 – 23191Ig-like C2-type 2
Domain236 – 33196Ig-like C2-type 3
Domain333 – 43199Ig-like C2-type 4
Domain434 – 533100Ig-like C2-type 5
Domain613 – 942330Protein kinase
Nucleotide binding619 – 6279ATP By similarity

Sites

Active site8101Proton acceptor By similarity
Binding site6471ATP By similarity

Amino acid modifications

Modified residue8411Phosphotyrosine; by autocatalysis By similarity
Modified residue9731Phosphothreonine Ref.2
Glycosylation791N-linked (GlcNAc...); by host Potential
Glycosylation1071N-linked (GlcNAc...); by host Potential
Glycosylation1281N-linked (GlcNAc...); by host Potential
Glycosylation1871N-linked (GlcNAc...); by host Potential
Glycosylation3091N-linked (GlcNAc...); by host Potential
Glycosylation3201N-linked (GlcNAc...); by host Potential
Glycosylation3361N-linked (GlcNAc...); by host Potential
Glycosylation3691N-linked (GlcNAc...); by host Potential
Glycosylation4441N-linked (GlcNAc...); by host Potential
Glycosylation5111N-linked (GlcNAc...); by host Potential
Glycosylation5241N-linked (GlcNAc...); by host Potential
Disulfide bond76 ↔ 118 Potential
Disulfide bond161 ↔ 211 Potential
Disulfide bond258 ↔ 312 Potential
Disulfide bond451 ↔ 516 Potential

Experimental info

Sequence conflict7141L → P in AAA43045. Ref.1
Sequence conflict971 – 9788QRTPPVAR → RGPPL in AAA43045. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00545 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: 4C7CAC4835185EBF

FASTA978108,492
        10         20         30         40         50         60 
RMPSGPGHYG ASAETPGPRP PLCPASSCCL PTEAMGPRAL LVLLMATAWH AQGVPVIQPS 

        70         80         90        100        110        120 
GPELVVEPGT TVTLRCVGNG SVEWDGPISP HWNLDLDPPS SILTTNNATF QNTGTYHCTE 

       130        140        150        160        170        180 
PGNPRGGNAT IHLYVKDPAR PWKVLAQEVT VLEGQDALLP CLLTDPALEA GVSLVRVRGR 

       190        200        210        220        230        240 
PVLRQTNYSF SPWHGFTIHK AKFIENHVYQ CSARVDGRTV TSMGIWLKVQ KDISGPATLT 

       250        260        270        280        290        300 
LEPAELVRIQ GEAAQIVCSA SNIDVNFDVS LRHGDTKLTI SQQSDFHDNR YQKVLTLNLD 

       310        320        330        340        350        360 
HVSFQDAGNY SCTATNAWGN HSASMVFRVV ESAYSNLTSE QSLLQEVTVG EKVDLQVKVE 

       370        380        390        400        410        420 
AYPGLESFNW TYLGPFSDYQ DKLDFVTIKD TYRYTSTLSL PRLKRSESGR YSFLARNAGG 

       430        440        450        460        470        480 
QNALTFELTL RYPPEVRVTM TLINGSDTLL CEASGYPQPS VTWVQCRSHT DRCDESAGLV 

       490        500        510        520        530        540 
LEDSHSEVLS QVPFYEVIVH SLLAIGTLEH NRTYECRAFN SVGNSSQTFW PISIGAHTPL 

       550        560        570        580        590        600 
PDELLFTPVL LTCMSIMALL LLLLLLLLYK YKQKPKYQVR WKIIESYEGN SYTFIDPTQL 

       610        620        630        640        650        660 
PYNEKWEFPR NNLQFGKTLG TGAFGKVVEA TAFGLGKEDA VLKVAVKMLK STAHADEKEA 

       670        680        690        700        710        720 
LMSELKIMSH LGQHENIVNL LGACTHGGPV LVITEYCCYG DLLNFLRRQA EAMLGPSLSV 

       730        740        750        760        770        780 
GQDPEAGAGY KNIHLEKKYV RRDSGFSSQG VDTYVEMRPV STSSSNDSFS EEDLGKEDGR 

       790        800        810        820        830        840 
PLELRDLLHF SSQVAQGMAF LASKNCIHRD VAARNVLLTS GRVAKIGDFG LARDIMNDSN 

       850        860        870        880        890        900 
YIVKGNARLP VKWMAPESIF DCVYTVQSDV WSYGILLWEI FSLGLNPYPG ILVNSKFYKL 

       910        920        930        940        950        960 
VKDGYQMAQP AFAPKNIYSI MQACWALEPT RRPTFQQICS LLQKQAQEDR RVPNYTNLPS 

       970 
SSSSRLLRPW QRTPPVAR 

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References

[1]"Nucleotide sequence of the feline retroviral oncogene v-fms shows unexpected homology with oncogenes encoding tyrosine-specific protein kinases."
Hampe A., Gobet M., Sherr C.J., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 81:85-89(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Reassessment of the v-fms sequence: threonine phosphorylation of the COOH-terminal domain."
Smola U., Hennig D., Hadwiger-Fangmeier A., Schuetz B., Pfaff E., Niemann H., Tamura T.
J. Virol. 65:6181-6187(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, PHOSPHORYLATION AT THR-973.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01643 Genomic RNA. Translation: AAA43045.1.
S59588 Genomic DNA. Translation: AAB20028.1.
PIRTVMVMD. A00654.

3D structure databases

ProteinModelPortalP00545.
SMRP00545. Positions 578-951.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.7.10.2. 2234.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PfamPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF500947. CSF-1_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTSM00409. IG. 3 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKFMS_FSVMD
AccessionPrimary (citable) accession number: P00545
Secondary accession number(s): Q86597
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families