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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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 21332114Coagulation factor VIIIPRO_0000002973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi173 ↔ 199Curated
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence analysis
Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi547 ↔ 573Curated
Glycosylationi601 – 6011N-linked (GlcNAc...)Sequence analysis
Modified residuei737 – 7371SulfotyrosineBy similarity
Modified residuei738 – 7381SulfotyrosineBy similarity
Modified residuei742 – 7421SulfotyrosineBy similarity
Glycosylationi929 – 9291N-linked (GlcNAc...)Sequence analysis
Glycosylationi985 – 9851N-linked (GlcNAc...)Sequence analysis
Glycosylationi1025 – 10251N-linked (GlcNAc...)Sequence analysis
Glycosylationi1111 – 11111N-linked (GlcNAc...)Sequence analysis
Glycosylationi1181 – 11811N-linked (GlcNAc...)Sequence analysis
Glycosylationi1208 – 12081N-linked (GlcNAc...)Sequence analysis
Glycosylationi1245 – 12451N-linked (GlcNAc...)Sequence analysis
Glycosylationi1265 – 12651N-linked (GlcNAc...)Sequence analysis
Glycosylationi1335 – 13351N-linked (GlcNAc...)Sequence analysis
Glycosylationi1408 – 14081N-linked (GlcNAc...)Sequence analysis
Glycosylationi1611 – 16111N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1633 ↔ 1659Curated
Disulfide bondi1822 ↔ 1970PROSITE-ProRule annotation
Glycosylationi1919 – 19191N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1975 ↔ 2127PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei391 – 3922Cleavage; by thrombinBy similarity
Sitei759 – 7602Cleavage; by thrombinBy similarity
Sitei1449 – 14502Cleavage (activation)By similarity
Sitei1490 – 14912Cleavage; by thrombinBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiP12263.

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

1
2133
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1981 – 19833Combined sources
Beta strandi1984 – 19863Combined sources
Helixi1988 – 19903Combined sources
Beta strandi1991 – 19944Combined sources
Helixi2006 – 20083Combined sources
Beta strandi2031 – 204717Combined sources
Beta strandi2049 – 20513Combined sources
Beta strandi2054 – 207118Combined sources
Beta strandi2088 – 20914Combined sources
Beta strandi2094 – 211724Combined sources
Beta strandi2120 – 21278Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MO3X-ray1.70M1971-2129[»]
ProteinModelPortaliP12263.
SMRiP12263. Positions 20-744, 1490-2133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 357338F5/8 type A 1Add
BLAST
Domaini20 – 199180Plastocyanin-like 1Add
BLAST
Domaini207 – 357151Plastocyanin-like 2Add
BLAST
Domaini399 – 730332F5/8 type A 2Add
BLAST
Domaini399 – 573175Plastocyanin-like 3Add
BLAST
Domaini583 – 730148Plastocyanin-like 4Add
BLAST
Domaini1495 – 1822328F5/8 type A 3Add
BLAST
Domaini1495 – 1659165Plastocyanin-like 5Add
BLAST
Domaini1669 – 1822154Plastocyanin-like 6Add
BLAST
Domaini1822 – 1970149F5/8 type C 1PROSITE-ProRule annotationAdd
BLAST
Domaini1975 – 2127153F5/8 type C 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni760 – 1599840BAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti713 – 7131N → M no nucleotide entry (PubMed:3016730).Curated
Sequence conflicti734 – 7341I → T no nucleotide entry (PubMed:3016730).Curated
Sequence conflicti792 – 7921G → Q no nucleotide entry (PubMed:3016730).Curated
Sequence conflicti1133 – 11331E → F no nucleotide entry (PubMed:3016730).Curated
Sequence conflicti1191 – 11911I → L no nucleotide entry (PubMed:3016730).Curated
Sequence conflicti1209 – 12091R → F no nucleotide entry (PubMed:3016730).Curated
Sequence conflicti1437 – 14371C → G no nucleotide entry (PubMed:3016730).Curated
Sequence conflicti1456 – 14561F → R no nucleotide entry (PubMed:3016730).Curated
Sequence conflicti1539 – 15391F → R no nucleotide entry (PubMed:3016730).Curated
Sequence conflicti1546 – 15461Q → N no nucleotide entry (PubMed:3016730).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4MO3X-ray1.70M1971-2129[»]
ProteinModelPortaliP12263.
SMRiP12263. Positions 20-744, 1490-2133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028556.

Proteomic databases

PaxDbiP12263.

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: March 16, 2016
This is version 118 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.