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Protein

Coagulation factor VIII

Gene

F8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Acute phase, Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-MMU-140875. Common Pathway of Fibrin Clot Formation.
R-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-5694530. Cargo concentration in the ER.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor VIII
Alternative name(s):
Procoagulant component
Gene namesi
Name:F8
Synonyms:Cf8, F8c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:88383. F8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000000297220 – 2319Coagulation factor VIIIAdd BLAST2300

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi61N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi173 ↔ 199Curated
Glycosylationi233N-linked (GlcNAc...)Sequence analysis1
Glycosylationi259N-linked (GlcNAc...)Sequence analysis1
Modified residuei367SulfotyrosineBy similarity1
Glycosylationi423N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi547 ↔ 573Curated
Glycosylationi601N-linked (GlcNAc...)Sequence analysis1
Modified residuei737SulfotyrosineBy similarity1
Modified residuei738SulfotyrosineBy similarity1
Modified residuei742SulfotyrosineBy similarity1
Glycosylationi880N-linked (GlcNAc...)Sequence analysis1
Glycosylationi958N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1015N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1022N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1026N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1044N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1076N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1087N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1136N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1161N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1192N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1255N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1268N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1273N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1274N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1302N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1316N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1340N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1378N-linked (GlcNAc...)Sequence analysis1
Modified residuei1669SulfotyrosineBy similarity1
Modified residuei1687SulfotyrosineBy similarity1
Glycosylationi1797N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1819 ↔ 1845Curated
Disulfide bondi2008 ↔ 2156PROSITE-ProRule annotation
Glycosylationi2105N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2161 ↔ 2313PROSITE-ProRule annotation

Post-translational modificationi

The binding of vWF and activation depend on the sulfation of Tyr-1669.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei391 – 392Cleavage; by thrombinBy similarity2
Sitei759 – 760Cleavage; by thrombinBy similarity2
Sitei1324 – 1325Cleavage (activation)By similarity2
Sitei1640 – 1641Cleavage (activation)By similarity2
Sitei1678 – 1679Cleavage; by thrombinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiQ06194.
PRIDEiQ06194.

PTM databases

iPTMnetiQ06194.
PhosphoSitePlusiQ06194.

Expressioni

Tissue specificityi

Found in most tissues.

Gene expression databases

BgeeiENSMUSG00000031196.
CleanExiMM_F8.
ExpressionAtlasiQ06194. baseline and differential.
GenevisibleiQ06194. MM.

Interactioni

Subunit structurei

Interacts with vWF. vWF binding is essential for the stabilization of F8 in circulation (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033539.

Structurei

3D structure databases

ProteinModelPortaliQ06194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 349F5/8 type A 1Add BLAST330
Domaini20 – 199Plastocyanin-like 1Add BLAST180
Domaini207 – 349Plastocyanin-like 2Add BLAST143
Domaini399 – 730F5/8 type A 2Add BLAST332
Domaini399 – 573Plastocyanin-like 3Add BLAST175
Domaini583 – 730Plastocyanin-like 4Add BLAST148
Domaini1683 – 2008F5/8 type A 3Add BLAST326
Domaini1683 – 1845Plastocyanin-like 5Add BLAST163
Domaini1855 – 2008Plastocyanin-like 6Add BLAST154
Domaini2008 – 2156F5/8 type C 1PROSITE-ProRule annotationAdd BLAST149
Domaini2161 – 2313F5/8 type C 2PROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni760 – 1640BAdd BLAST881

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 F5/8 type A domains.Curated
Contains 2 F5/8 type C domains.PROSITE-ProRule annotation
Contains 6 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IJ6Y. Eukaryota.
ENOG4111F6G. LUCA.
GeneTreeiENSGT00550000074552.
HOGENOMiHOG000231686.
HOVERGENiHBG106657.
InParanoidiQ06194.
KOiK03899.
OMAiKYKKVRF.
OrthoDBiEOG091G00QL.
TreeFamiTF329807.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR024715. Factor_5/8.
IPR014707. Factor_8.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF50. PTHR10127:SF50. 4 hits.
PfamiPF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
PIRSFiPIRSF000354. Factors_V_VIII. 1 hit.
SMARTiSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEiPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q06194-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIALFACFF LSLFNFCSSA IRRYYLGAVE LSWNYIQSDL LSVLHTDSRF
60 70 80 90 100
LPRMSTSFPF NTSIMYKKTV FVEYKDQLFN IAKPRPPWMG LLGPTIWTEV
110 120 130 140 150
HDTVVITLKN MASHPVSLHA VGVSYWKASE GDEYEDQTSQ MEKEDDKVFP
160 170 180 190 200
GESHTYVWQV LKENGPMASD PPCLTYSYMS HVDLVKDLNS GLIGALLVCK
210 220 230 240 250
EGSLSKERTQ MLYQFVLLFA VFDEGKSWHS ETNDSYTQSM DSASARDWPK
260 270 280 290 300
MHTVNGYVNR SLPGLIGCHR KSVYWHVIGM GTTPEIHSIF LEGHTFFVRN
310 320 330 340 350
HRQASLEISP ITFLTAQTLL IDLGQFLLFC HISSHKHDGM EAYVKVDSCP
360 370 380 390 400
EESQWQKKNN NEEMEDYDDD LYSEMDMFTL DYDSSPFIQI RSVAKKYPKT
410 420 430 440 450
WIHYISAEEE DWDYAPSVPT SDNGSYKSQY LSNGPHRIGR KYKKVRFIAY
460 470 480 490 500
TDETFKTRET IQHESGLLGP LLYGEVGDTL LIIFKNQASR PYNIYPHGIT
510 520 530 540 550
DVSPLHARRL PRGIKHVKDL PIHPGEIFKY KWTVTVEDGP TKSDPRCLTR
560 570 580 590 600
YYSSFINPER DLASGLIGPL LICYKESVDQ RGNQMMSDKR NVILFSIFDE
610 620 630 640 650
NQSWYITENM QRFLPNAAKT QPQDPGFQAS NIMHSINGYV FDSLELTVCL
660 670 680 690 700
HEVAYWHILS VGAQTDFLSI FFSGYTFKHK MVYEDTLTLF PFSGETVFMS
710 720 730 740 750
MENPGLWVLG CHNSDFRKRG MTALLKVSSC DKSTSDYYEE IYEDIPTQLV
760 770 780 790 800
NENNVIDPRS FFQNTNHPNT RKKKFKDSTI PKNDMEKIEP QFEEIAEMLK
810 820 830 840 850
VQSVSVSDML MLLGQSHPTP HGLFLSDGQE AIYEAIHDDH SPNAIDSNEG
860 870 880 890 900
PSKVTQLRPE SHHSEKIVFT PQPGLQLRSN KSLETTIEVK WKKLGLQVSS
910 920 930 940 950
LPSNLMTTTI LSDNLKATFE KTDSSGFPDM PVHSSSKLST TAFGKKAYSL
960 970 980 990 1000
VGSHVPLNVS EENSDSNILD STLMYSQESL PRDNILSMEN DRLLREKRFH
1010 1020 1030 1040 1050
GIALLTKDNT LFKDNVSLMK TNKTYNHSTT NEKLHTESPT SIENSTTDLQ
1060 1070 1080 1090 1100
DAILKVNSEI QEVTALIHDG TLLGKNSTYL RLNHMLNRTT STKNKDIFHR
1110 1120 1130 1140 1150
KDEDPIPQDE ENTIMPFSKM LFLSESSNWF KKTNGNNSLN SEQEHSPKQL
1160 1170 1180 1190 1200
VYLMFKKYVK NQSFLSEKNK VTVEQDGFTK NIGLKDMAFP HNMSIFLTTL
1210 1220 1230 1240 1250
SNVHENGRHN QEKNIQEEIE KEALIEEKVV LPQVHEATGS KNFLKDILIL
1260 1270 1280 1290 1300
GTRQNISLYE VHVPVLQNIT SINNSTNTVQ IHMEHFFKRR KDKETNSEGL
1310 1320 1330 1340 1350
VNKTREMVKN YPSQKNITTQ RSKRALGQFR LSTQWLKTIN CSTQCIIKQI
1360 1370 1380 1390 1400
DHSKEMKKFI TKSSLSDSSV IKSTTQTNSS DSHIVKTSAF PPIDLKRSPF
1410 1420 1430 1440 1450
QNKFSHVQAS SYIYDFKTKS SRIQESNNFL KETKINNPSL AILPWNMFID
1460 1470 1480 1490 1500
QGKFTSPGKS NTNSVTYKKR ENIIFLKPTL PEESGKIELL PQVSIQEEEI
1510 1520 1530 1540 1550
LPTETSHGSP GHLNLMKEVF LQKIQGPTKW NKAKRHGESI KGKTESSKNT
1560 1570 1580 1590 1600
RSKLLNHHAW DYHYAAQIPK DMWKSKEKSP EIISIKQEDT ILSLRPHGNS
1610 1620 1630 1640 1650
HSIGANEKQN WPQRETTWVK QGQTQRTCSQ IPPVLKRHQR ELSAFQSEQE
1660 1670 1680 1690 1700
ATDYDDAITI ETIEDFDIYS EDIKQGPRSF QQKTRHYFIA AVERLWDYGM
1710 1720 1730 1740 1750
STSHVLRNRY QSDNVPQFKK VVFQEFTDGS FSQPLYRGEL NEHLGLLGPY
1760 1770 1780 1790 1800
IRAEVEDNIM VTFKNQASRP YSFYSSLISY KEDQRGEEPR RNFVKPNETK
1810 1820 1830 1840 1850
IYFWKVQHHM APTEDEFDCK AWAYFSDVDL ERDMHSGLIG PLLICHANTL
1860 1870 1880 1890 1900
NPAHGRQVSV QEFALLFTIF DETKSWYFTE NVKRNCKTPC NFQMEDPTLK
1910 1920 1930 1940 1950
ENYRFHAING YVMDTLPGLV MAQDQRIRWY LLSMGNNENI QSIHFSGHVF
1960 1970 1980 1990 2000
TVRKKEEYKM AVYNLYPGVF ETLEMIPSRA GIWRVECLIG EHLQAGMSTL
2010 2020 2030 2040 2050
FLVYSKQCQI PLGMASGSIR DFQITASGHY GQWAPNLARL HYSGSINAWS
2060 2070 2080 2090 2100
TKEPFSWIKV DLLAPMIVHG IKTQGARQKF SSLYISQFII MYSLDGKKWL
2110 2120 2130 2140 2150
SYQGNSTGTL MVFFGNVDSS GIKHNSFNPP IIARYIRLHP THSSIRSTLR
2160 2170 2180 2190 2200
MELMGCDLNS CSIPLGMESK VISDTQITAS SYFTNMFATW SPSQARLHLQ
2210 2220 2230 2240 2250
GRTNAWRPQV NDPKQWLQVD LQKTMKVTGI ITQGVKSLFT SMFVKEFLIS
2260 2270 2280 2290 2300
SSQDGHHWTQ ILYNGKVKVF QGNQDSSTPM MNSLDPPLLT RYLRIHPQIW
2310
EHQIALRLEI LGCEAQQQY
Length:2,319
Mass (Da):266,196
Last modified:July 27, 2011 - v2
Checksum:i09CAC4CFBCCECA57
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti959V → A in AAA37385 (PubMed:8314577).Curated1
Sequence conflicti988M → I in AAA37385 (PubMed:8314577).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05573 mRNA. Translation: AAA37385.1.
AL731844, AL808110 Genomic DNA. Translation: CAM15581.1.
AL808110, AL731844 Genomic DNA. Translation: CAM26492.1.
CH466576 Genomic DNA. Translation: EDL29229.1.
CCDSiCCDS30238.1.
PIRiA47004.
RefSeqiNP_032003.2. NM_007977.2.
UniGeneiMm.1805.

Genome annotation databases

EnsembliENSMUST00000033539; ENSMUSP00000033539; ENSMUSG00000031196.
GeneIDi14069.
KEGGimmu:14069.
UCSCiuc009tpt.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05573 mRNA. Translation: AAA37385.1.
AL731844, AL808110 Genomic DNA. Translation: CAM15581.1.
AL808110, AL731844 Genomic DNA. Translation: CAM26492.1.
CH466576 Genomic DNA. Translation: EDL29229.1.
CCDSiCCDS30238.1.
PIRiA47004.
RefSeqiNP_032003.2. NM_007977.2.
UniGeneiMm.1805.

3D structure databases

ProteinModelPortaliQ06194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033539.

PTM databases

iPTMnetiQ06194.
PhosphoSitePlusiQ06194.

Proteomic databases

PaxDbiQ06194.
PRIDEiQ06194.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033539; ENSMUSP00000033539; ENSMUSG00000031196.
GeneIDi14069.
KEGGimmu:14069.
UCSCiuc009tpt.3. mouse.

Organism-specific databases

CTDi2157.
MGIiMGI:88383. F8.

Phylogenomic databases

eggNOGiENOG410IJ6Y. Eukaryota.
ENOG4111F6G. LUCA.
GeneTreeiENSGT00550000074552.
HOGENOMiHOG000231686.
HOVERGENiHBG106657.
InParanoidiQ06194.
KOiK03899.
OMAiKYKKVRF.
OrthoDBiEOG091G00QL.
TreeFamiTF329807.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-MMU-140875. Common Pathway of Fibrin Clot Formation.
R-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-5694530. Cargo concentration in the ER.

Miscellaneous databases

PROiQ06194.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031196.
CleanExiMM_F8.
ExpressionAtlasiQ06194. baseline and differential.
GenevisibleiQ06194. MM.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR024715. Factor_5/8.
IPR014707. Factor_8.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF50. PTHR10127:SF50. 4 hits.
PfamiPF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
PIRSFiPIRSF000354. Factors_V_VIII. 1 hit.
SMARTiSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEiPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFA8_MOUSE
AccessioniPrimary (citable) accession number: Q06194
Secondary accession number(s): A2AN88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.