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Protein

Coagulation factor VIII

Gene

F8

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor VIII
Alternative name(s):
Procoagulant component
Gene namesi
Name:F8
Synonyms:CF8
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

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_000000297320 – 2133Coagulation factor VIIIAdd BLAST2114

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi173 ↔ 199Curated
Glycosylationi233N-linked (GlcNAc...)Sequence analysis1
Glycosylationi259N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi547 ↔ 573Curated
Glycosylationi601N-linked (GlcNAc...)Sequence analysis1
Modified residuei737SulfotyrosineBy similarity1
Modified residuei738SulfotyrosineBy similarity1
Modified residuei742SulfotyrosineBy similarity1
Glycosylationi929N-linked (GlcNAc...)Sequence analysis1
Glycosylationi985N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1025N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1111N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1181N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1208N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1245N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1265N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1335N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1408N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1611N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1633 ↔ 1659Curated
Disulfide bondi1822 ↔ 1970PROSITE-ProRule annotation
Glycosylationi1919N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1975 ↔ 2127PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei391 – 392Cleavage; by thrombinBy similarity2
Sitei759 – 760Cleavage; by thrombinBy similarity2
Sitei1449 – 1450Cleavage (activation)By similarity2
Sitei1490 – 1491Cleavage; by thrombinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiP12263.
PRIDEiP12263.

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

STRINGi9823.ENSSSCP00000028556.

Structurei

Secondary structure

12133
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni1981 – 1983Combined sources3
Beta strandi1984 – 1986Combined sources3
Helixi1988 – 1990Combined sources3
Beta strandi1991 – 1994Combined sources4
Helixi2006 – 2008Combined sources3
Beta strandi2031 – 2047Combined sources17
Beta strandi2049 – 2051Combined sources3
Beta strandi2054 – 2071Combined sources18
Beta strandi2088 – 2091Combined sources4
Beta strandi2094 – 2117Combined sources24
Beta strandi2120 – 2127Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MO3X-ray1.70M1971-2129[»]
ProteinModelPortaliP12263.
SMRiP12263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 357F5/8 type A 1Add BLAST338
Domaini20 – 199Plastocyanin-like 1Add BLAST180
Domaini207 – 357Plastocyanin-like 2Add BLAST151
Domaini399 – 730F5/8 type A 2Add BLAST332
Domaini399 – 573Plastocyanin-like 3Add BLAST175
Domaini583 – 730Plastocyanin-like 4Add BLAST148
Domaini1495 – 1822F5/8 type A 3Add BLAST328
Domaini1495 – 1659Plastocyanin-like 5Add BLAST165
Domaini1669 – 1822Plastocyanin-like 6Add BLAST154
Domaini1822 – 1970F5/8 type C 1PROSITE-ProRule annotationAdd BLAST149
Domaini1975 – 2127F5/8 type C 2PROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni760 – 1599BAdd BLAST840

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.
HOGENOMiHOG000231686.
HOVERGENiHBG106657.
InParanoidiP12263.
KOiK03899.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR014707. Factor_8.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF50. PTHR10127:SF50. 4 hits.
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
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.

P12263-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLELSTCVF LCLLPLGFSA IRRYYLGAVE LSWDYRQSEL LRELHVDTRF
60 70 80 90 100
PATAPGALPL GPSVLYKKTV FVEFTDQLFS VARPRPPWMG LLGPTIQAEV
110 120 130 140 150
YDTVVVTLKN MASHPVSLHA VGVSFWKSSE GAEYEDHTSQ REKEDDKVLP
160 170 180 190 200
GKSQTYVWQV LKENGPTASD PPCLTYSYLS HVDLVKDLNS GLIGALLVCR
210 220 230 240 250
EGSLTRERTQ NLHEFVLLFA VFDEGKSWHS ARNDSWTRAM DPAPARAQPA
260 270 280 290 300
MHTVNGYVNR SLPGLIGCHK KSVYWHVIGM GTSPEVHSIF LEGHTFLVRH
310 320 330 340 350
HRQASLEISP LTFLTAQTFL MDLGQFLLFC HISSHHHGGM EAHVRVESCA
360 370 380 390 400
EEPQLRRKAD EEEDYDDNLY DSDMDVVRLD GDDVSPFIQI RSVAKKHPKT
410 420 430 440 450
WVHYISAEEE DWDYAPAVPS PSDRSYKSLY LNSGPQRIGR KYKKARFVAY
460 470 480 490 500
TDVTFKTRKA IPYESGILGP LLYGEVGDTL LIIFKNKASR PYNIYPHGIT
510 520 530 540 550
DVSALHPGRL LKGWKHLKDM PILPGETFKY KWTVTVEDGP TKSDPRCLTR
560 570 580 590 600
YYSSSINLEK DLASGLIGPL LICYKESVDQ RGNQMMSDKR NVILFSVFDE
610 620 630 640 650
NQSWYLAENI QRFLPNPDGL QPQDPEFQAS NIMHSINGYV FDSLQLSVCL
660 670 680 690 700
HEVAYWYILS VGAQTDFLSV FFSGYTFKHK MVYEDTLTLF PFSGETVFMS
710 720 730 740 750
MENPGLWVLG CHNSDLRNRG MTALLKVYSC DRDIGDYYDN TYEDIPGFLL
760 770 780 790 800
SGKNVIEPRS FAQNSRPPSA SQKQFQTITS PEDDVELDPQ SGERTQALEE
810 820 830 840 850
LSVPSGDGSM LLGQNPAPHG SSSSDLQEAR NEADDYLPGA RERNTAPSAA
860 870 880 890 900
ARLRPELHHS AERVLTPEPE KELKKLDSKM SSSSDLLKTS PTIPSDTLSA
910 920 930 940 950
ETERTHSLGP PHPQVNFRSQ LGAIVLGKNS SHFIGAGVPL GSTEEDHESS
960 970 980 990 1000
LGENVSPVES DGIFEKERAH GPASLTKDDV LFKVNISLVK TNKARVYLKT
1010 1020 1030 1040 1050
NRKIHIDDAA LLTENRASAT FMDKNTTASG LNHVSNWIKG PLGKNPLSSE
1060 1070 1080 1090 1100
RGPSPELLTS SGSGKSVKGQ SSGQGRIRVA VEEEELSKGK EMMLPNSELT
1110 1120 1130 1140 1150
FLTNSADVQG NDTHSQGKKS REEMERREKL VQEKVDLPQV YTATGTKNFL
1160 1170 1180 1190 1200
RNIFHQSTEP SVEGFDGGSH APVPQDSRSL NDSAERAETH IAHFSAIREE
1210 1220 1230 1240 1250
APLEAPGNRT GPGPRSAVPR RVKQSLKQIR LPLEEIKPER GVVLNATSTR
1260 1270 1280 1290 1300
WSESSPILQG AKRNNLSLPF LTLEMAGGQG KISALGKSAA GPLASGKLEK
1310 1320 1330 1340 1350
AVLSSAGLSE ASGKAEFLPK VRVHREDLLP QKTSNVSCAH GDLGQEIFLQ
1360 1370 1380 1390 1400
KTRGPVNLNK VNRPGRTPSK LLGPPMPKEW ESLEKSPKST ALRTKDIISL
1410 1420 1430 1440 1450
PLDRHESNHS IAAKNEGQAE TQREAAWTKQ GGPGRLCAPK PPVLRRHQRD
1460 1470 1480 1490 1500
ISLPTFQPEE DKMDYDDIFS TETKGEDFDI YGEDENQDPR SFQKRTRHYF
1510 1520 1530 1540 1550
IAAVEQLWDY GMSESPRALR NRAQNGEVPR FKKVVFREFA DGSFTQPSYR
1560 1570 1580 1590 1600
GELNKHLGLL GPYIRAEVED NIMVTFKNQA SRPYSFYSSL ISYPDDQEQG
1610 1620 1630 1640 1650
AEPRHNFVQP NETRTYFWKV QHHMAPTEDE FDCKAWAYFS DVDLEKDVHS
1660 1670 1680 1690 1700
GLIGPLLICR ANTLNAAHGR QVTVQEFALF FTIFDETKSW YFTENVERNC
1710 1720 1730 1740 1750
RAPCHLQMED PTLKENYRFH AINGYVMDTL PGLVMAQNQR IRWYLLSMGS
1760 1770 1780 1790 1800
NENIHSIHFS GHVFSVRKKE EYKMAVYNLY PGVFETVEML PSKVGIWRIE
1810 1820 1830 1840 1850
CLIGEHLQAG MSTTFLVYSK ECQAPLGMAS GRIRDFQITA SGQYGQWAPK
1860 1870 1880 1890 1900
LARLHYSGSI NAWSTKDPHS WIKVDLLAPM IIHGIMTQGA RQKFSSLYIS
1910 1920 1930 1940 1950
QFIIMYSLDG RNWQSYRGNS TGTLMVFFGN VDASGIKHNI FNPPIVARYI
1960 1970 1980 1990 2000
RLHPTHYSIR STLRMELMGC DLNSCSMPLG MQNKAISDSQ ITASSHLSNI
2010 2020 2030 2040 2050
FATWSPSQAR LHLQGRTNAW RPRVSSAEEW LQVDLQKTVK VTGITTQGVK
2060 2070 2080 2090 2100
SLLSSMYVKE FLVSSSQDGR RWTLFLQDGH TKVFQGNQDS STPVVNALDP
2110 2120 2130
PLFTRYLRIH PTSWAQHIAL RLEVLGCEAQ DLY
Length:2,133
Mass (Da):239,305
Last modified:November 1, 1997 - v2
Checksum:i152BBA8997F570DA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti713N → M no nucleotide entry (PubMed:3016730).Curated1
Sequence conflicti734I → T no nucleotide entry (PubMed:3016730).Curated1
Sequence conflicti792G → Q no nucleotide entry (PubMed:3016730).Curated1
Sequence conflicti1133E → F no nucleotide entry (PubMed:3016730).Curated1
Sequence conflicti1191I → L no nucleotide entry (PubMed:3016730).Curated1
Sequence conflicti1209R → F no nucleotide entry (PubMed:3016730).Curated1
Sequence conflicti1437C → G no nucleotide entry (PubMed:3016730).Curated1
Sequence conflicti1456F → R no nucleotide entry (PubMed:3016730).Curated1
Sequence conflicti1539F → R no nucleotide entry (PubMed:3016730).Curated1
Sequence conflicti1546Q → N no nucleotide entry (PubMed:3016730).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49517 mRNA. Translation: AAB06705.1.
PIRiA25945.
T42763.
RefSeqiNP_999332.1. NM_214167.1.
UniGeneiSsc.16043.

Genome annotation databases

GeneIDi397339.
KEGGissc:397339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49517 mRNA. Translation: AAB06705.1.
PIRiA25945.
T42763.
RefSeqiNP_999332.1. NM_214167.1.
UniGeneiSsc.16043.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MO3X-ray1.70M1971-2129[»]
ProteinModelPortaliP12263.
SMRiP12263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028556.

Proteomic databases

PaxDbiP12263.
PRIDEiP12263.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397339.
KEGGissc:397339.

Organism-specific databases

CTDi2157.

Phylogenomic databases

eggNOGiENOG410IJ6Y. Eukaryota.
ENOG4111F6G. LUCA.
HOGENOMiHOG000231686.
HOVERGENiHBG106657.
InParanoidiP12263.
KOiK03899.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR014707. Factor_8.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF50. PTHR10127:SF50. 4 hits.
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
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_PIG
AccessioniPrimary (citable) accession number: P12263
Secondary accession number(s): Q95243
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 120 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.