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Protein

Complement factor H

Gene

CFH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • heparan sulfate proteoglycan binding Source: BHF-UCL
  • heparin binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Complement alternate pathway, Immunity, Innate immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000000971-MONOMER.
ReactomeiR-HSA-977606. Regulation of Complement cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement factor H
Alternative name(s):
H factor 1
Gene namesi
Name:CFH
Synonyms:HF, HF1, HF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4883. CFH.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Basal laminar drusen (BLD)1 Publication
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionDrusen are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to a serous pigment epithelial detachment of the macula that may result in vision loss.
See also OMIM:126700
Complement factor H deficiency (CFHD)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder that can manifest as several different phenotypes, including asymptomatic, recurrent bacterial infections, and renal failure. Laboratory features usually include decreased serum levels of factor H, complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome.
See also OMIM:609814
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031978127R → L in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_031979224Missing in CFHD; with membranoproliferative glomerulonephritis; affects binding of factor H to C3b and shows defective complement regulation. 1 Publication1
Natural variantiVAR_031981431C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_019405536C → R in CFHD. 1 Publication1
Natural variantiVAR_031982673C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_019406959C → Y in CFHD; variant confirmed at protein level. 2 Publications1
Natural variantiVAR_0258731076Q → E in CFHD. 2 Publications1
Natural variantiVAR_0258741119D → G in CFHD. 2 Publications1
Natural variantiVAR_0258811184T → R in CFHD. 2 Publications1
Natural variantiVAR_0258851210R → C in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration. 3 Publications1
Natural variantiVAR_0258871215R → Q in CFHD. 2 Publications1
Hemolytic uremic syndrome atypical 1 (AHUS1)8 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
Disease descriptionAn atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease.
See also OMIM:235400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02586478R → G in AHUS1. 1 Publication1
Natural variantiVAR_063648325C → Y in AHUS1. 1 Publication1
Natural variantiVAR_031980400Q → K in AHUS1. 1 Publication1
Natural variantiVAR_063649609V → I in AHUS1. 1 Publication1
Natural variantiVAR_025865630C → W in AHUS1. 1 Publication1
Natural variantiVAR_031983673C → Y in AHUS1. 1 Publication1
Natural variantiVAR_025866850E → K in AHUS1; variant confirmed at protein level. 2 Publications1
Natural variantiVAR_031984893H → R in AHUS1. 1 Publication1
Natural variantiVAR_031985915C → S in AHUS1. 1 Publication1
Natural variantiVAR_025867950Q → H in AHUS1. 1 PublicationCorresponds to variant rs149474608dbSNPEnsembl.1
Natural variantiVAR_025868951Y → H in AHUS1. 1 Publication1
Natural variantiVAR_025869956T → M in AHUS1. 2 PublicationsCorresponds to variant rs145975787dbSNPEnsembl.1
Natural variantiVAR_025870978W → C in AHUS1. 1 Publication1
Natural variantiVAR_0258711021Y → F in AHUS1. 1 Publication1
Natural variantiVAR_0258721043C → R in AHUS1. 1 Publication1
Natural variantiVAR_0258751134V → G in AHUS1. 1 Publication1
Natural variantiVAR_0258761142Y → D in AHUS1. 1 Publication1
Natural variantiVAR_0258771157W → R in AHUS1. 1 Publication1
Natural variantiVAR_0258781163C → W in AHUS1. 1 Publication1
Natural variantiVAR_0636501169I → L in AHUS1. 1 Publication1
Natural variantiVAR_0636511183W → C in AHUS1. 1 Publication1
Natural variantiVAR_0258791183W → L in AHUS1. 3 Publications1
Natural variantiVAR_0258801183W → R in AHUS1. 2 Publications1
Natural variantiVAR_0194071189L → R in AHUS1. 2 Publications1
Natural variantiVAR_0194081191S → L in AHUS1. 2 PublicationsCorresponds to variant rs460897dbSNPEnsembl.1
Natural variantiVAR_0258821194G → D in AHUS1. 1 Publication1
Natural variantiVAR_0258831197V → A in AHUS1. 2 PublicationsCorresponds to variant rs460184dbSNPEnsembl.1
Natural variantiVAR_0258841198E → A in AHUS1. 1 Publication1
Natural variantiVAR_0319861199F → S in AHUS1. 1 Publication1
Natural variantiVAR_0258861215R → G in AHUS1. 2 Publications1
Natural variantiVAR_0194091225 – 1231YPTCAKR → FQS in AHUS1. 1 Publication7
Natural variantiVAR_0258881226P → S in AHUS1; atypical. 1 Publication1
Macular degeneration, age-related, 4 (ARMD4)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
See also OMIM:610698
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001979402Y → H Polymorphism associated with ARMD4. 5 PublicationsCorresponds to variant rs1061170dbSNPEnsembl.1
Natural variantiVAR_0258851210R → C in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration. 3 Publications1

Keywords - Diseasei

Age-related macular degeneration, Disease mutation, Hemolytic uremic syndrome

Organism-specific databases

DisGeNETi3075.
MalaCardsiCFH.
MIMi126700. phenotype.
235400. phenotype.
609814. phenotype.
610698. phenotype.
Orphaneti279. Age-related macular degeneration.
93579. Atypical hemolytic-uremic syndrome with H factor anomaly.
244275. De novo thrombotic microangiopathy after kidney transplantation.
93571. Dense deposit disease.
75376. Familial drusen.
244242. HELLP syndrome.
200421. Immunodeficiency with factor H anomaly.
329903. Immunoglobulin-mediated membranoproliferative glomerulonephritis.
PharmGKBiPA29261.

Chemistry databases

ChEMBLiCHEMBL4629.

Polymorphism and mutation databases

BioMutaiCFH.
DMDMi158517847.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
ChainiPRO_000000589419 – 1231Complement factor HAdd BLAST1213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi21 ↔ 66PROSITE-ProRule annotation
Disulfide bondi52 ↔ 80PROSITE-ProRule annotation
Disulfide bondi85 ↔ 129PROSITE-ProRule annotation
Disulfide bondi114 ↔ 141PROSITE-ProRule annotation
Disulfide bondi146 ↔ 192PROSITE-ProRule annotation
Disulfide bondi178 ↔ 205PROSITE-ProRule annotation
Disulfide bondi210 ↔ 251PROSITE-ProRule annotation
Glycosylationi217N-linked (GlcNAc...) (complex)1 Publication1
Disulfide bondi237 ↔ 262PROSITE-ProRule annotation
Disulfide bondi267 ↔ 309PROSITE-ProRule annotation
Disulfide bondi294 ↔ 320PROSITE-ProRule annotation
Disulfide bondi325 ↔ 374PROSITE-ProRule annotation
Disulfide bondi357 ↔ 385PROSITE-ProRule annotation
Disulfide bondi389 ↔ 431PROSITE-ProRule annotation
Disulfide bondi416 ↔ 442PROSITE-ProRule annotation
Disulfide bondi448 ↔ 494PROSITE-ProRule annotation
Disulfide bondi477 ↔ 505PROSITE-ProRule annotation
Disulfide bondi509 ↔ 553PROSITE-ProRule annotation
Glycosylationi529N-linked (GlcNAc...)4 Publications1
Disulfide bondi536 ↔ 564PROSITE-ProRule annotation
Disulfide bondi569 ↔ 611PROSITE-ProRule annotation
Disulfide bondi597 ↔ 623PROSITE-ProRule annotation
Disulfide bondi630 ↔ 673PROSITE-ProRule annotation
Disulfide bondi659 ↔ 684PROSITE-ProRule annotation
Disulfide bondi691 ↔ 733PROSITE-ProRule annotation
Glycosylationi718N-linked (GlcNAc...)1 Publication1
Disulfide bondi719 ↔ 744PROSITE-ProRule annotation
Disulfide bondi753 ↔ 792PROSITE-ProRule annotation
Disulfide bondi781 ↔ 803PROSITE-ProRule annotation
Glycosylationi802N-linked (GlcNAc...)2 Publications1
Disulfide bondi811 ↔ 853PROSITE-ProRule annotation
Glycosylationi822N-linked (GlcNAc...)1 Publication1
Disulfide bondi839 ↔ 864PROSITE-ProRule annotation
Disulfide bondi870 ↔ 915PROSITE-ProRule annotation
Glycosylationi882N-linked (GlcNAc...) (complex)5 Publications1
Disulfide bondi901 ↔ 926PROSITE-ProRule annotation
Glycosylationi911N-linked (GlcNAc...) (complex)4 Publications1
Disulfide bondi931 ↔ 973PROSITE-ProRule annotation
Disulfide bondi959 ↔ 984PROSITE-ProRule annotation
Disulfide bondi989 ↔ 1032PROSITE-ProRule annotation
Disulfide bondi1018 ↔ 1043PROSITE-ProRule annotation
Glycosylationi1029N-linked (GlcNAc...) (complex)3 Publications1
Disulfide bondi1048 ↔ 1091PROSITE-ProRule annotation
Disulfide bondi1077 ↔ 1102PROSITE-ProRule annotation
Glycosylationi1095N-linked (GlcNAc...)1 Publication1
Disulfide bondi1109 ↔ 1152PROSITE-ProRule annotation
Disulfide bondi1138 ↔ 1163PROSITE-ProRule annotation
Disulfide bondi1167 ↔ 1218PROSITE-ProRule annotation
Disulfide bondi1201 ↔ 1228PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP08603.
PaxDbiP08603.
PeptideAtlasiP08603.
PRIDEiP08603.

PTM databases

iPTMnetiP08603.
PhosphoSitePlusiP08603.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiENSG00000000971.
ExpressionAtlasiP08603. baseline and differential.
GenevisibleiP08603. HS.

Organism-specific databases

HPAiCAB016385.
CAB016769.
HPA038922.
HPA049176.
HPA053326.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
C3P010242EBI-1223708,EBI-6863145
ennXP169462EBI-1223708,EBI-6403567From a different organism.
lphA0A024A2C92EBI-1223708,EBI-12498321From a different organism.

Protein-protein interaction databases

BioGridi109324. 18 interactors.
DIPiDIP-38303N.
IntActiP08603. 18 interactors.
STRINGi9606.ENSP00000356399.

Chemistry databases

BindingDBiP08603.

Structurei

Secondary structure

11231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 23Combined sources3
Beta strandi29 – 33Combined sources5
Beta strandi47 – 52Combined sources6
Beta strandi62 – 66Combined sources5
Beta strandi68 – 74Combined sources7
Beta strandi94 – 105Combined sources12
Beta strandi109 – 114Combined sources6
Beta strandi118 – 123Combined sources6
Beta strandi126 – 129Combined sources4
Beta strandi131 – 134Combined sources4
Beta strandi140 – 143Combined sources4
Beta strandi155 – 158Combined sources4
Beta strandi159 – 162Combined sources4
Beta strandi172 – 175Combined sources4
Beta strandi182 – 186Combined sources5
Beta strandi188 – 192Combined sources5
Beta strandi196 – 200Combined sources5
Beta strandi204 – 207Combined sources4
Beta strandi218 – 222Combined sources5
Beta strandi232 – 237Combined sources6
Beta strandi241 – 245Combined sources5
Beta strandi247 – 252Combined sources6
Beta strandi255 – 258Combined sources4
Beta strandi262 – 264Combined sources3
Beta strandi333 – 335Combined sources3
Helixi338 – 341Combined sources4
Helixi342 – 344Combined sources3
Beta strandi352 – 357Combined sources6
Beta strandi366 – 375Combined sources10
Beta strandi378 – 383Combined sources6
Beta strandi386 – 390Combined sources5
Turni400 – 403Combined sources4
Beta strandi405 – 407Combined sources3
Beta strandi411 – 413Combined sources3
Beta strandi415 – 417Combined sources3
Beta strandi420 – 422Combined sources3
Helixi423 – 425Combined sources3
Beta strandi428 – 432Combined sources5
Beta strandi435 – 438Combined sources4
Beta strandi447 – 449Combined sources3
Helixi450 – 452Combined sources3
Beta strandi456 – 459Combined sources4
Beta strandi465 – 468Combined sources4
Beta strandi472 – 477Combined sources6
Beta strandi484 – 486Combined sources3
Beta strandi488 – 495Combined sources8
Beta strandi498 – 500Combined sources3
Beta strandi508 – 510Combined sources3
Beta strandi515 – 518Combined sources4
Beta strandi524 – 527Combined sources4
Beta strandi531 – 536Combined sources6
Beta strandi547 – 554Combined sources8
Beta strandi557 – 560Combined sources4
Beta strandi578 – 581Combined sources4
Beta strandi585 – 587Combined sources3
Beta strandi592 – 597Combined sources6
Beta strandi602 – 605Combined sources4
Beta strandi607 – 612Combined sources6
Beta strandi615 – 618Combined sources4
Beta strandi622 – 626Combined sources5
Beta strandi637 – 641Combined sources5
Beta strandi654 – 658Combined sources5
Beta strandi663 – 665Combined sources3
Beta strandi669 – 674Combined sources6
Beta strandi675 – 678Combined sources4
Beta strandi684 – 686Combined sources3
Beta strandi700 – 703Combined sources4
Beta strandi714 – 718Combined sources5
Beta strandi723 – 727Combined sources5
Beta strandi729 – 732Combined sources4
Beta strandi737 – 739Combined sources3
Beta strandi743 – 746Combined sources4
Beta strandi757 – 760Combined sources4
Helixi765 – 767Combined sources3
Beta strandi769 – 771Combined sources3
Beta strandi790 – 792Combined sources3
Beta strandi797 – 799Combined sources3
Beta strandi870 – 872Combined sources3
Beta strandi879 – 881Combined sources3
Beta strandi883 – 887Combined sources5
Beta strandi889 – 891Combined sources3
Beta strandi895 – 904Combined sources10
Beta strandi906 – 909Combined sources4
Beta strandi911 – 916Combined sources6
Beta strandi925 – 927Combined sources3
Beta strandi940 – 943Combined sources4
Beta strandi950 – 952Combined sources3
Beta strandi957 – 959Combined sources3
Beta strandi965 – 967Combined sources3
Beta strandi971 – 974Combined sources4
Beta strandi977 – 979Combined sources3
Beta strandi1057 – 1059Combined sources3
Beta strandi1065 – 1067Combined sources3
Beta strandi1072 – 1077Combined sources6
Beta strandi1082 – 1085Combined sources4
Beta strandi1087 – 1092Combined sources6
Beta strandi1101 – 1103Combined sources3
Beta strandi1118 – 1122Combined sources5
Beta strandi1126 – 1128Combined sources3
Beta strandi1133 – 1138Combined sources6
Beta strandi1143 – 1146Combined sources4
Beta strandi1148 – 1153Combined sources6
Beta strandi1154 – 1157Combined sources4
Beta strandi1162 – 1164Combined sources3
Beta strandi1167 – 1169Combined sources3
Helixi1171 – 1177Combined sources7
Beta strandi1179 – 1181Combined sources3
Turni1182 – 1186Combined sources5
Beta strandi1189 – 1191Combined sources3
Beta strandi1196 – 1201Combined sources6
Turni1202 – 1204Combined sources3
Beta strandi1205 – 1207Combined sources3
Beta strandi1214 – 1217Combined sources4
Beta strandi1228 – 1230Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FHCmodel-A1105-1231[»]
1HAQX-ray-A19-1231[»]
1HCCNMR-A927-985[»]
1HFHNMR-A866-985[»]
1HFINMR-A866-927[»]
1KOVmodel-A321-443[»]
2BZMNMR-A1107-1231[»]
2G7IX-ray1.75A1107-1231[»]
2IC4X-ray-A321-506[»]
2JGWNMR-A386-446[»]
2JGXNMR-A386-446[»]
2KMSNMR-A690-804[»]
2QFGX-ray-A19-322[»]
2QFHX-ray-A928-1231[»]
2RLPNMR-A20-142[»]
2RLQNMR-A84-206[»]
2UWNX-ray2.35A322-506[»]
2V8EX-ray2.50A322-506[»]
2W80X-ray2.35A/B/E/G321-443[»]
2W81X-ray2.35A/B/E321-443[»]
2WIIX-ray2.70C18-264[»]
2XQWX-ray2.31C1103-1231[»]
3GAUX-ray-A19-1231[»]
3GAVX-ray-A19-1231[»]
3GAWX-ray-A19-1231[»]
3KXVX-ray2.00A1103-1231[»]
3KZJX-ray1.65A1103-1231[»]
3OXUX-ray2.10D/E/F1107-1231[»]
3R62X-ray1.52A/B1107-1231[»]
3RJ3X-ray2.35D/E/F1107-1231[»]
3SW0X-ray1.80X1046-1231[»]
4AYDX-ray2.40A/B/E321-443[»]
4AYEX-ray2.80A/B/E321-443[»]
4AYIX-ray2.31A/E321-443[»]
4AYMX-ray3.00A/B/E/F321-443[»]
4B2RNMR-A566-687[»]
4B2SNMR-A627-747[»]
4J38X-ray2.83B1103-1231[»]
4K12X-ray1.08A508-567[»]
4ONTX-ray2.15D/E/F1107-1231[»]
4ZH1X-ray2.24D/E/F1107-1231[»]
ProteinModelPortaliP08603.
SMRiP08603.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08603.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 82Sushi 1PROSITE-ProRule annotationAdd BLAST64
Domaini83 – 143Sushi 2PROSITE-ProRule annotationAdd BLAST61
Domaini144 – 207Sushi 3PROSITE-ProRule annotationAdd BLAST64
Domaini208 – 264Sushi 4PROSITE-ProRule annotationAdd BLAST57
Domaini265 – 322Sushi 5PROSITE-ProRule annotationAdd BLAST58
Domaini324 – 386Sushi 6PROSITE-ProRule annotationAdd BLAST63
Domaini387 – 444Sushi 7PROSITE-ProRule annotationAdd BLAST58
Domaini446 – 507Sushi 8PROSITE-ProRule annotationAdd BLAST62
Domaini515 – 566Sushi 9PROSITE-ProRule annotationAdd BLAST52
Domaini567 – 625Sushi 10PROSITE-ProRule annotationAdd BLAST59
Domaini628 – 686Sushi 11PROSITE-ProRule annotationAdd BLAST59
Domaini689 – 746Sushi 12PROSITE-ProRule annotationAdd BLAST58
Domaini751 – 805Sushi 13PROSITE-ProRule annotationAdd BLAST55
Domaini809 – 866Sushi 14PROSITE-ProRule annotationAdd BLAST58
Domaini868 – 928Sushi 15PROSITE-ProRule annotationAdd BLAST61
Domaini929 – 986Sushi 16PROSITE-ProRule annotationAdd BLAST58
Domaini987 – 1045Sushi 17PROSITE-ProRule annotationAdd BLAST59
Domaini1046 – 1104Sushi 18PROSITE-ProRule annotationAdd BLAST59
Domaini1107 – 1165Sushi 19PROSITE-ProRule annotationAdd BLAST59
Domaini1170 – 1230Sushi 20PROSITE-ProRule annotationAdd BLAST61

Sequence similaritiesi

Contains 20 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiENOG410IVQ9. Eukaryota.
ENOG410YBAR. LUCA.
HOVERGENiHBG005665.
InParanoidiP08603.
KOiK04004.
OrthoDBiEOG091G00V4.
PhylomeDBiP08603.
TreeFamiTF326157.

Family and domain databases

CDDicd00033. CCP. 16 hits.
InterProiIPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00084. Sushi. 19 hits.
[Graphical view]
SMARTiSM00032. CCP. 20 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 18 hits.
PROSITEiPS50923. SUSHI. 19 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08603-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRLLAKIICL MLWAICVAED CNELPPRRNT EILTGSWSDQ TYPEGTQAIY
60 70 80 90 100
KCRPGYRSLG NVIMVCRKGE WVALNPLRKC QKRPCGHPGD TPFGTFTLTG
110 120 130 140 150
GNVFEYGVKA VYTCNEGYQL LGEINYRECD TDGWTNDIPI CEVVKCLPVT
160 170 180 190 200
APENGKIVSS AMEPDREYHF GQAVRFVCNS GYKIEGDEEM HCSDDGFWSK
210 220 230 240 250
EKPKCVEISC KSPDVINGSP ISQKIIYKEN ERFQYKCNMG YEYSERGDAV
260 270 280 290 300
CTESGWRPLP SCEEKSCDNP YIPNGDYSPL RIKHRTGDEI TYQCRNGFYP
310 320 330 340 350
ATRGNTAKCT STGWIPAPRC TLKPCDYPDI KHGGLYHENM RRPYFPVAVG
360 370 380 390 400
KYYSYYCDEH FETPSGSYWD HIHCTQDGWS PAVPCLRKCY FPYLENGYNQ
410 420 430 440 450
NYGRKFVQGK SIDVACHPGY ALPKAQTTVT CMENGWSPTP RCIRVKTCSK
460 470 480 490 500
SSIDIENGFI SESQYTYALK EKAKYQCKLG YVTADGETSG SITCGKDGWS
510 520 530 540 550
AQPTCIKSCD IPVFMNARTK NDFTWFKLND TLDYECHDGY ESNTGSTTGS
560 570 580 590 600
IVCGYNGWSD LPICYERECE LPKIDVHLVP DRKKDQYKVG EVLKFSCKPG
610 620 630 640 650
FTIVGPNSVQ CYHFGLSPDL PICKEQVQSC GPPPELLNGN VKEKTKEEYG
660 670 680 690 700
HSEVVEYYCN PRFLMKGPNK IQCVDGEWTT LPVCIVEEST CGDIPELEHG
710 720 730 740 750
WAQLSSPPYY YGDSVEFNCS ESFTMIGHRS ITCIHGVWTQ LPQCVAIDKL
760 770 780 790 800
KKCKSSNLII LEEHLKNKKE FDHNSNIRYR CRGKEGWIHT VCINGRWDPE
810 820 830 840 850
VNCSMAQIQL CPPPPQIPNS HNMTTTLNYR DGEKVSVLCQ ENYLIQEGEE
860 870 880 890 900
ITCKDGRWQS IPLCVEKIPC SQPPQIEHGT INSSRSSQES YAHGTKLSYT
910 920 930 940 950
CEGGFRISEE NETTCYMGKW SSPPQCEGLP CKSPPEISHG VVAHMSDSYQ
960 970 980 990 1000
YGEEVTYKCF EGFGIDGPAI AKCLGEKWSH PPSCIKTDCL SLPSFENAIP
1010 1020 1030 1040 1050
MGEKKDVYKA GEQVTYTCAT YYKMDGASNV TCINSRWTGR PTCRDTSCVN
1060 1070 1080 1090 1100
PPTVQNAYIV SRQMSKYPSG ERVRYQCRSP YEMFGDEEVM CLNGNWTEPP
1110 1120 1130 1140 1150
QCKDSTGKCG PPPPIDNGDI TSFPLSVYAP ASSVEYQCQN LYQLEGNKRI
1160 1170 1180 1190 1200
TCRNGQWSEP PKCLHPCVIS REIMENYNIA LRWTAKQKLY SRTGESVEFV
1210 1220 1230
CKRGYRLSSR SHTLRTTCWD GKLEYPTCAK R
Length:1,231
Mass (Da):139,096
Last modified:September 11, 2007 - v4
Checksum:i3C26D62A2BF9BFEE
GO
Isoform 2 (identifier: P08603-2) [UniParc]FASTAAdd to basket
Also known as: FHL-1

The sequence of this isoform differs from the canonical sequence as follows:
     446-449: KTCS → SFTL
     450-1231: Missing.

Show »
Length:449
Mass (Da):51,034
Checksum:iC2AAD47F155343E3
GO

Sequence cautioni

The sequence CAB41739 differs from that shown. Reason: Frameshift at position 341.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21C → Q AA sequence (PubMed:6215918).Curated1
Sequence conflicti30T → V AA sequence (PubMed:6215918).Curated1
Sequence conflicti34T → Q AA sequence (PubMed:6215918).Curated1
Sequence conflicti53 – 54RP → IL in CAB41739 (PubMed:2946589).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02383662V → I Polymorphism; confirmed at protein level. 4 PublicationsCorresponds to variant rs800292dbSNPEnsembl.1
Natural variantiVAR_02586478R → G in AHUS1. 1 Publication1
Natural variantiVAR_031978127R → L in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_031979224Missing in CFHD; with membranoproliferative glomerulonephritis; affects binding of factor H to C3b and shows defective complement regulation. 1 Publication1
Natural variantiVAR_063648325C → Y in AHUS1. 1 Publication1
Natural variantiVAR_031980400Q → K in AHUS1. 1 Publication1
Natural variantiVAR_001979402Y → H Polymorphism associated with ARMD4. 5 PublicationsCorresponds to variant rs1061170dbSNPEnsembl.1
Natural variantiVAR_031981431C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_043892493T → R.1 PublicationCorresponds to variant rs1061171dbSNPEnsembl.1
Natural variantiVAR_019405536C → R in CFHD. 1 Publication1
Natural variantiVAR_025092551I → T.1 PublicationCorresponds to variant rs35453854dbSNPEnsembl.1
Natural variantiVAR_043893567R → G Associated with basal laminar drusen. 1 Publication1
Natural variantiVAR_063649609V → I in AHUS1. 1 Publication1
Natural variantiVAR_025865630C → W in AHUS1. 1 Publication1
Natural variantiVAR_031982673C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_031983673C → Y in AHUS1. 1 Publication1
Natural variantiVAR_025866850E → K in AHUS1; variant confirmed at protein level. 2 Publications1
Natural variantiVAR_025093890S → I.1 PublicationCorresponds to variant rs515299dbSNPEnsembl.1
Natural variantiVAR_031984893H → R in AHUS1. 1 Publication1
Natural variantiVAR_031985915C → S in AHUS1. 1 Publication1
Natural variantiVAR_020261936E → D Polymorphism associated with hemolytic uremic syndrome and basal laminar drusen. 4 PublicationsCorresponds to variant rs1065489dbSNPEnsembl.1
Natural variantiVAR_025867950Q → H in AHUS1. 1 PublicationCorresponds to variant rs149474608dbSNPEnsembl.1
Natural variantiVAR_025868951Y → H in AHUS1. 1 Publication1
Natural variantiVAR_025869956T → M in AHUS1. 2 PublicationsCorresponds to variant rs145975787dbSNPEnsembl.1
Natural variantiVAR_019406959C → Y in CFHD; variant confirmed at protein level. 2 Publications1
Natural variantiVAR_025870978W → C in AHUS1. 1 Publication1
Natural variantiVAR_055683997N → T.Corresponds to variant rs17575212dbSNPEnsembl.1
Natural variantiVAR_0250941007V → I.1 Publication1
Natural variantiVAR_0438941007V → L.Corresponds to variant rs534399dbSNPEnsembl.1
Natural variantiVAR_0556841010A → T.Corresponds to variant rs11539862dbSNPEnsembl.1
Natural variantiVAR_0250951017T → I.1 PublicationCorresponds to variant rs34362004dbSNPEnsembl.1
Natural variantiVAR_0258711021Y → F in AHUS1. 1 Publication1
Natural variantiVAR_0258721043C → R in AHUS1. 1 Publication1
Natural variantiVAR_0250961050N → Y Polymorphism associated with basal laminar drusen. 2 PublicationsCorresponds to variant rs35274867dbSNPEnsembl.1
Natural variantiVAR_0250971059I → T.1 PublicationCorresponds to variant rs35343172dbSNPEnsembl.1
Natural variantiVAR_0258731076Q → E in CFHD. 2 Publications1
Natural variantiVAR_0438951078R → S Associated with basal laminar drusen. 1 Publication1
Natural variantiVAR_0258741119D → G in CFHD. 2 Publications1
Natural variantiVAR_0258751134V → G in AHUS1. 1 Publication1
Natural variantiVAR_0258761142Y → D in AHUS1. 1 Publication1
Natural variantiVAR_0438961143Q → E Polymorphism; confirmed at protein level. 1 PublicationCorresponds to variant rs34247141dbSNPEnsembl.1
Natural variantiVAR_0258771157W → R in AHUS1. 1 Publication1
Natural variantiVAR_0258781163C → W in AHUS1. 1 Publication1
Natural variantiVAR_0636501169I → L in AHUS1. 1 Publication1
Natural variantiVAR_0636511183W → C in AHUS1. 1 Publication1
Natural variantiVAR_0258791183W → L in AHUS1. 3 Publications1
Natural variantiVAR_0258801183W → R in AHUS1. 2 Publications1
Natural variantiVAR_0258811184T → R in CFHD. 2 Publications1
Natural variantiVAR_0194071189L → R in AHUS1. 2 Publications1
Natural variantiVAR_0194081191S → L in AHUS1. 2 PublicationsCorresponds to variant rs460897dbSNPEnsembl.1
Natural variantiVAR_0258821194G → D in AHUS1. 1 Publication1
Natural variantiVAR_0258831197V → A in AHUS1. 2 PublicationsCorresponds to variant rs460184dbSNPEnsembl.1
Natural variantiVAR_0258841198E → A in AHUS1. 1 Publication1
Natural variantiVAR_0319861199F → S in AHUS1. 1 Publication1
Natural variantiVAR_0258851210R → C in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration. 3 Publications1
Natural variantiVAR_0258861215R → G in AHUS1. 2 Publications1
Natural variantiVAR_0258871215R → Q in CFHD. 2 Publications1
Natural variantiVAR_0194091225 – 1231YPTCAKR → FQS in AHUS1. 1 Publication7
Natural variantiVAR_0258881226P → S in AHUS1; atypical. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001190446 – 449KTCS → SFTL in isoform 2. 2 Publications4
Alternative sequenceiVSP_001191450 – 1231Missing in isoform 2. 2 PublicationsAdd BLAST782

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00716 mRNA. Translation: CAA68704.1.
DQ233256 Genomic DNA. Translation: ABB02180.1.
AL049744 Genomic DNA. Translation: CAI19672.1.
BC037285 mRNA. Translation: AAH37285.1.
BC110643 mRNA. Translation: AAI10644.1.
BC142699 mRNA. Translation: AAI42700.1.
X04697 mRNA. Translation: CAB41739.1. Frameshift.
X07523 mRNA. Translation: CAA30403.1.
M12383 mRNA. Translation: AAA52013.1.
M65294 mRNA. Translation: AAA35948.1.
U56979 Genomic DNA. Translation: AAB01987.1.
Z29665 Genomic DNA. Translation: CAA82763.1.
CCDSiCCDS1385.1. [P08603-1]
CCDS53452.1. [P08603-2]
PIRiS00254. NBHUH.
S03013. NBHUHS.
RefSeqiNP_000177.2. NM_000186.3.
UniGeneiHs.363396.

Genome annotation databases

EnsembliENST00000367429; ENSP00000356399; ENSG00000000971.
GeneIDi3075.
KEGGihsa:3075.
UCSCiuc001gtj.4. human. [P08603-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

CFHbase

CFH mutation db

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00716 mRNA. Translation: CAA68704.1.
DQ233256 Genomic DNA. Translation: ABB02180.1.
AL049744 Genomic DNA. Translation: CAI19672.1.
BC037285 mRNA. Translation: AAH37285.1.
BC110643 mRNA. Translation: AAI10644.1.
BC142699 mRNA. Translation: AAI42700.1.
X04697 mRNA. Translation: CAB41739.1. Frameshift.
X07523 mRNA. Translation: CAA30403.1.
M12383 mRNA. Translation: AAA52013.1.
M65294 mRNA. Translation: AAA35948.1.
U56979 Genomic DNA. Translation: AAB01987.1.
Z29665 Genomic DNA. Translation: CAA82763.1.
CCDSiCCDS1385.1. [P08603-1]
CCDS53452.1. [P08603-2]
PIRiS00254. NBHUH.
S03013. NBHUHS.
RefSeqiNP_000177.2. NM_000186.3.
UniGeneiHs.363396.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FHCmodel-A1105-1231[»]
1HAQX-ray-A19-1231[»]
1HCCNMR-A927-985[»]
1HFHNMR-A866-985[»]
1HFINMR-A866-927[»]
1KOVmodel-A321-443[»]
2BZMNMR-A1107-1231[»]
2G7IX-ray1.75A1107-1231[»]
2IC4X-ray-A321-506[»]
2JGWNMR-A386-446[»]
2JGXNMR-A386-446[»]
2KMSNMR-A690-804[»]
2QFGX-ray-A19-322[»]
2QFHX-ray-A928-1231[»]
2RLPNMR-A20-142[»]
2RLQNMR-A84-206[»]
2UWNX-ray2.35A322-506[»]
2V8EX-ray2.50A322-506[»]
2W80X-ray2.35A/B/E/G321-443[»]
2W81X-ray2.35A/B/E321-443[»]
2WIIX-ray2.70C18-264[»]
2XQWX-ray2.31C1103-1231[»]
3GAUX-ray-A19-1231[»]
3GAVX-ray-A19-1231[»]
3GAWX-ray-A19-1231[»]
3KXVX-ray2.00A1103-1231[»]
3KZJX-ray1.65A1103-1231[»]
3OXUX-ray2.10D/E/F1107-1231[»]
3R62X-ray1.52A/B1107-1231[»]
3RJ3X-ray2.35D/E/F1107-1231[»]
3SW0X-ray1.80X1046-1231[»]
4AYDX-ray2.40A/B/E321-443[»]
4AYEX-ray2.80A/B/E321-443[»]
4AYIX-ray2.31A/E321-443[»]
4AYMX-ray3.00A/B/E/F321-443[»]
4B2RNMR-A566-687[»]
4B2SNMR-A627-747[»]
4J38X-ray2.83B1103-1231[»]
4K12X-ray1.08A508-567[»]
4ONTX-ray2.15D/E/F1107-1231[»]
4ZH1X-ray2.24D/E/F1107-1231[»]
ProteinModelPortaliP08603.
SMRiP08603.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109324. 18 interactors.
DIPiDIP-38303N.
IntActiP08603. 18 interactors.
STRINGi9606.ENSP00000356399.

Chemistry databases

BindingDBiP08603.
ChEMBLiCHEMBL4629.

PTM databases

iPTMnetiP08603.
PhosphoSitePlusiP08603.

Polymorphism and mutation databases

BioMutaiCFH.
DMDMi158517847.

Proteomic databases

MaxQBiP08603.
PaxDbiP08603.
PeptideAtlasiP08603.
PRIDEiP08603.

Protocols and materials databases

DNASUi3075.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367429; ENSP00000356399; ENSG00000000971.
GeneIDi3075.
KEGGihsa:3075.
UCSCiuc001gtj.4. human. [P08603-1]

Organism-specific databases

CTDi3075.
DisGeNETi3075.
GeneCardsiCFH.
GeneReviewsiCFH.
HGNCiHGNC:4883. CFH.
HPAiCAB016385.
CAB016769.
HPA038922.
HPA049176.
HPA053326.
MalaCardsiCFH.
MIMi126700. phenotype.
134370. gene.
235400. phenotype.
609814. phenotype.
610698. phenotype.
neXtProtiNX_P08603.
Orphaneti279. Age-related macular degeneration.
93579. Atypical hemolytic-uremic syndrome with H factor anomaly.
244275. De novo thrombotic microangiopathy after kidney transplantation.
93571. Dense deposit disease.
75376. Familial drusen.
244242. HELLP syndrome.
200421. Immunodeficiency with factor H anomaly.
329903. Immunoglobulin-mediated membranoproliferative glomerulonephritis.
PharmGKBiPA29261.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IVQ9. Eukaryota.
ENOG410YBAR. LUCA.
HOVERGENiHBG005665.
InParanoidiP08603.
KOiK04004.
OrthoDBiEOG091G00V4.
PhylomeDBiP08603.
TreeFamiTF326157.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000000971-MONOMER.
ReactomeiR-HSA-977606. Regulation of Complement cascade.

Miscellaneous databases

ChiTaRSiCFH. human.
EvolutionaryTraceiP08603.
GeneWikiiFactor_H.
GenomeRNAii3075.
PROiP08603.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000000971.
ExpressionAtlasiP08603. baseline and differential.
GenevisibleiP08603. HS.

Family and domain databases

CDDicd00033. CCP. 16 hits.
InterProiIPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00084. Sushi. 19 hits.
[Graphical view]
SMARTiSM00032. CCP. 20 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 18 hits.
PROSITEiPS50923. SUSHI. 19 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCFAH_HUMAN
AccessioniPrimary (citable) accession number: P08603
Secondary accession number(s): A5PL14
, P78435, Q14570, Q2TAZ5, Q38G77, Q5TFM3, Q8N708, Q9NU86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: September 11, 2007
Last modified: November 30, 2016
This is version 207 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

According to a report, Asn-217 is not glycosylated (PubMed:17591618). Another study observed glycosylation at this position (PubMed:19139490).2 Publications