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P06909 (CFAH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement factor H
Alternative name(s):
Protein beta-1-H
Gene names
Name:Cfh
Synonyms:Hf1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Polymorphism

Two codominant alleles of factor H are present in mice.

Sequence similarities

Contains 20 Sushi (CCP/SCR) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 12341216Complement factor H
PRO_0000005895

Regions

Domain19 – 8264Sushi 1
Domain83 – 14361Sushi 2
Domain144 – 20764Sushi 3
Domain208 – 26457Sushi 4
Domain265 – 32258Sushi 5
Domain324 – 38663Sushi 6
Domain387 – 44458Sushi 7
Domain446 – 50762Sushi 8
Domain508 – 56659Sushi 9
Domain567 – 62458Sushi 10
Domain627 – 68559Sushi 11
Domain688 – 74558Sushi 12
Domain750 – 80455Sushi 13
Domain806 – 86358Sushi 14
Domain865 – 93369Sushi 15
Domain934 – 99158Sushi 16
Domain992 – 105059Sushi 17
Domain1051 – 110959Sushi 18
Domain1112 – 117059Sushi 19
Domain1171 – 123464Sushi 20

Amino acid modifications

Modified residue11981Phosphoserine Ref.8
Glycosylation6761N-linked (GlcNAc...) Potential
Glycosylation7211N-linked (GlcNAc...) Potential
Glycosylation7731N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation8011N-linked (GlcNAc...) Ref.7
Glycosylation10301N-linked (GlcNAc...) Ref.7
Glycosylation10611N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation12251N-linked (GlcNAc...) Ref.7
Disulfide bond21 ↔ 66 By similarity
Disulfide bond52 ↔ 80 By similarity
Disulfide bond85 ↔ 129 By similarity
Disulfide bond114 ↔ 141 By similarity
Disulfide bond146 ↔ 192 By similarity
Disulfide bond178 ↔ 205 By similarity
Disulfide bond210 ↔ 251 By similarity
Disulfide bond237 ↔ 262 By similarity
Disulfide bond267 ↔ 309 By similarity
Disulfide bond294 ↔ 320 By similarity
Disulfide bond325 ↔ 374 By similarity
Disulfide bond357 ↔ 385 By similarity
Disulfide bond389 ↔ 431 By similarity
Disulfide bond416 ↔ 442 By similarity
Disulfide bond448 ↔ 494 By similarity
Disulfide bond477 ↔ 505 By similarity
Disulfide bond509 ↔ 553 By similarity
Disulfide bond536 ↔ 564 By similarity
Disulfide bond569 ↔ 610 By similarity
Disulfide bond597 ↔ 622 By similarity
Disulfide bond629 ↔ 672 By similarity
Disulfide bond658 ↔ 683 By similarity
Disulfide bond690 ↔ 732 By similarity
Disulfide bond718 ↔ 743 By similarity
Disulfide bond752 ↔ 791 By similarity
Disulfide bond780 ↔ 802 By similarity
Disulfide bond808 ↔ 850 By similarity
Disulfide bond836 ↔ 861 By similarity
Disulfide bond867 ↔ 920 By similarity
Disulfide bond906 ↔ 931 By similarity
Disulfide bond936 ↔ 978 By similarity
Disulfide bond964 ↔ 989 By similarity
Disulfide bond994 ↔ 1037 By similarity
Disulfide bond1023 ↔ 1048 By similarity
Disulfide bond1053 ↔ 1096 By similarity
Disulfide bond1082 ↔ 1107 By similarity
Disulfide bond1114 ↔ 1157 By similarity
Disulfide bond1143 ↔ 1168 By similarity
Disulfide bond1172 ↔ 1223 By similarity
Disulfide bond1206 ↔ 1233 By similarity

Experimental info

Sequence conflict11581R → T in AAA37759. Ref.1

Secondary structure

........................ 1234
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06909 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 0A5722F34620C9F0

FASTA1,234139,138
        10         20         30         40         50         60 
MRLSARIIWL ILWTVCAAED CKGPPPRENS EILSGSWSEQ LYPEGTQATY KCRPGYRTLG 

        70         80         90        100        110        120 
TIVKVCKNGK WVASNPSRIC RKKPCGHPGD TPFGSFRLAV GSQFEFGAKV VYTCDDGYQL 

       130        140        150        160        170        180 
LGEIDYRECG ADGWINDIPL CEVVKCLPVT ELENGRIVSG AAETDQEYYF GQVVRFECNS 

       190        200        210        220        230        240 
GFKIEGHKEI HCSENGLWSN EKPRCVEILC TPPRVENGDG INVKPVYKEN ERYHYKCKHG 

       250        260        270        280        290        300 
YVPKERGDAV CTGSGWSSQP FCEEKRCSPP YILNGIYTPH RIIHRSDDEI RYECNYGFYP 

       310        320        330        340        350        360 
VTGSTVSKCT PTGWIPVPRC TLKPCEFPQF KYGRLYYEES LRPNFPVSIG NKYSYKCDNG 

       370        380        390        400        410        420 
FSPPSGYSWD YLRCTAQGWE PEVPCVRKCV FHYVENGDSA YWEKVYVQGQ SLKVQCYNGY 

       430        440        450        460        470        480 
SLQNGQDTMT CTENGWSPPP KCIRIKTCSA SDIHIDNGFL SESSSIYALN RETSYRCKQG 

       490        500        510        520        530        540 
YVTNTGEISG SITCLQNGWS PQPSCIKSCD MPVFENSITK NTRTWFKLND KLDYECLVGF 

       550        560        570        580        590        600 
ENEYKHTKGS ITCTYYGWSD TPSCYERECS VPTLDRKLVV SPRKEKYRVG DLLEFSCHSG 

       610        620        630        640        650        660 
HRVGPDSVQC YHFGWSPGFP TCKGQVASCA PPLEILNGEI NGAKKVEYSH GEVVKYDCKP 

       670        680        690        700        710        720 
RFLLKGPNKI QCVDGNWTTL PVCIEEERTC GDIPELEHGS AKCSVPPYHH GDSVEFICEE 

       730        740        750        760        770        780 
NFTMIGHGSV SCISGKWTQL PKCVATDQLE KCRVLKSTGI EAIKPKLTEF THNSTMDYKC 

       790        800        810        820        830        840 
RDKQEYERSI CINGKWDPEP NCTSKTSCPP PPQIPNTQVI ETTVKYLDGE KLSVLCQDNY 

       850        860        870        880        890        900 
LTQDSEEMVC KDGRWQSLPR CIEKIPCSQP PTIEHGSINL PRSSEERRDS IESSSHEHGT 

       910        920        930        940        950        960 
TFSYVCDDGF RIPEENRITC YMGKWSTPPR CVGLPCGPPP SIPLGTVSLE LESYQHGEEV 

       970        980        990       1000       1010       1020 
TYHCSTGFGI DGPAFIICEG GKWSDPPKCI KTDCDVLPTV KNAIIRGKSK KSYRTGEQVT 

      1030       1040       1050       1060       1070       1080 
FRCQSPYQMN GSDTVTCVNS RWIGQPVCKD NSCVDPPHVP NATIVTRTKN KYLHGDRVRY 

      1090       1100       1110       1120       1130       1140 
ECNKPLELFG QVEVMCENGI WTEKPKCRDS TGKCGPPPPI DNGDITSLSL PVYEPLSSVE 

      1150       1160       1170       1180       1190       1200 
YQCQKYYLLK GKKTITCRNG KWSEPPTCLH ACVIPENIME SHNIILKWRH TEKIYSHSGE 

      1210       1220       1230 
DIEFGCKYGY YKARDSPPFR TKCINGTINY PTCV 

« Hide

References

« Hide 'large scale' references
[1]"Murine protein H is comprised of 20 repeating units, 61 amino acids in length."
Kristensen T., Tack B.F.
Proc. Natl. Acad. Sci. U.S.A. 83:3963-3967(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"Analysis of complement factor H mRNA expression: dexamethasone and IFN-gamma increase the level of H in L cells."
Munoz-Canoves P., Tack B.F., Vik D.P.
Biochemistry 28:9891-9897(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-19.
Strain: BALB/c.
[5]"Demonstration of an unusual allelic variation of mouse factor H by the complete cDNA sequence of the H.2 allotype."
Natsuume-Sakai S., Nonaka M., Nonaka M., Harada Y.N., Shreffler D.C., Moriwaki K.
J. Immunol. 144:358-362(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-18.
[6]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-773 AND ASN-1061.
Strain: C57BL/6.
Tissue: Plasma.
[7]"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
Bernhard O.K., Kapp E.A., Simpson R.J.
J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-773; ASN-801; ASN-1030; ASN-1061 AND ASN-1225.
Strain: C57BL/6.
Tissue: Plasma.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12660 mRNA. Translation: AAA37759.1.
AC161408 Genomic DNA. No translation available.
BC066092 mRNA. Translation: AAH66092.1.
J02891 mRNA. Translation: AAA37795.1.
AH001909 mRNA. Translation: AAA37762.1.
PIRNBMSH. A26154.
RefSeqNP_034018.2. NM_009888.3.
UniGeneMm.8655.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YBYX-ray1.58A321-444[»]
ProteinModelPortalP06909.
SMRP06909. Positions 20-1233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP06909. 2 interactions.
MINTMINT-1858780.
STRING10090.ENSMUSP00000066677.

PTM databases

PhosphoSiteP06909.

Proteomic databases

PaxDbP06909.
PRIDEP06909.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066859; ENSMUSP00000066677; ENSMUSG00000026365.
GeneID12628.
KEGGmmu:12628.

Organism-specific databases

CTD3075.
MGIMGI:88385. Cfh.

Phylogenomic databases

eggNOGNOG148800.
GeneTreeENSGT00740000115024.
HOGENOMHOG000049040.
HOVERGENHBG005665.
InParanoidP06909.
KOK04004.
OrthoDBEOG75XGK1.

Gene expression databases

ArrayExpressP06909.
CleanExMM_CFH.
GenevestigatorP06909.

Family and domain databases

InterProIPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00084. Sushi. 16 hits.
[Graphical view]
SMARTSM00032. CCP. 20 hits.
[Graphical view]
SUPFAMSSF57535. SSF57535. 18 hits.
PROSITEPS50923. SUSHI. 18 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio281808.
PROP06909.
SOURCESearch...

Entry information

Entry nameCFAH_MOUSE
AccessionPrimary (citable) accession number: P06909
Secondary accession number(s): Q6NZK3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot