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Reviewed, UniProtKB/Swiss-Prot P12263 (FA8_PIG)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Coagulation factor VIII
Alternative name(s):
    Procoagulant component
Gene names
Name: F8
Synonyms: CF8
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length2133 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Secreted › extracellular space.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 F5/8 type A domains.

Contains 2 F5/8 type C domains.

Contains 6 plastocyanin-like domains.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 21332114Coagulation factor VIII
PRO_0000002973

Regions

Domain20 – 357338F5/8 type A 1
Domain20 – 199180Plastocyanin-like 1
Domain207 – 357151Plastocyanin-like 2
Domain399 – 730332F5/8 type A 2
Domain399 – 573175Plastocyanin-like 3
Domain583 – 730148Plastocyanin-like 4
Domain1495 – 1822328F5/8 type A 3
Domain1495 – 1659165Plastocyanin-like 5
Domain1669 – 1822154Plastocyanin-like 6
Domain1822 – 1970149F5/8 type C 1
Domain1975 – 2127153F5/8 type C 2
Region760 – 1599840B

Sites

Site391 – 3922Cleavage; by thrombin By similarity
Site759 – 7602Cleavage; by thrombin By similarity
Site1449 – 14502Cleavage (activation) By similarity
Site1490 – 14912Cleavage; by thrombin By similarity

Amino acid modifications

Modified residue7371Sulfotyrosine By similarity
Modified residue7381Sulfotyrosine By similarity
Modified residue7421Sulfotyrosine By similarity
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation6011N-linked (GlcNAc...) Potential
Glycosylation9291N-linked (GlcNAc...) Potential
Glycosylation9851N-linked (GlcNAc...) Potential
Glycosylation10251N-linked (GlcNAc...) Potential
Glycosylation11111N-linked (GlcNAc...) Potential
Glycosylation11811N-linked (GlcNAc...) Potential
Glycosylation12081N-linked (GlcNAc...) Potential
Glycosylation12451N-linked (GlcNAc...) Potential
Glycosylation12651N-linked (GlcNAc...) Potential
Glycosylation13351N-linked (GlcNAc...) Potential
Glycosylation14081N-linked (GlcNAc...) Potential
Glycosylation16111N-linked (GlcNAc...) Potential
Glycosylation19191N-linked (GlcNAc...) Potential
Disulfide bond173 ↔ 199 Probable
Disulfide bond547 ↔ 573 Probable
Disulfide bond1633 ↔ 1659 Probable
Disulfide bond1822 ↔ 1970 By similarity
Disulfide bond1975 ↔ 2127 By similarity

Experimental info

Sequence conflict7131N → M Ref.2
Sequence conflict7341I → T Ref.2
Sequence conflict7921G → Q Ref.2
Sequence conflict11331E → F Ref.2
Sequence conflict11911I → L Ref.2
Sequence conflict12091R → F Ref.2
Sequence conflict14371C → G Ref.2
Sequence conflict14561F → R Ref.2
Sequence conflict15391F → R Ref.2
Sequence conflict15461Q → N Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P12263-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 152BBA8997F570DA

FASTA2,133239,305
        10         20         30         40         50         60 
MQLELSTCVF LCLLPLGFSA IRRYYLGAVE LSWDYRQSEL LRELHVDTRF PATAPGALPL 

        70         80         90        100        110        120 
GPSVLYKKTV FVEFTDQLFS VARPRPPWMG LLGPTIQAEV YDTVVVTLKN MASHPVSLHA 

       130        140        150        160        170        180 
VGVSFWKSSE GAEYEDHTSQ REKEDDKVLP GKSQTYVWQV LKENGPTASD PPCLTYSYLS 

       190        200        210        220        230        240 
HVDLVKDLNS GLIGALLVCR EGSLTRERTQ NLHEFVLLFA VFDEGKSWHS ARNDSWTRAM 

       250        260        270        280        290        300 
DPAPARAQPA MHTVNGYVNR SLPGLIGCHK KSVYWHVIGM GTSPEVHSIF LEGHTFLVRH 

       310        320        330        340        350        360 
HRQASLEISP LTFLTAQTFL MDLGQFLLFC HISSHHHGGM EAHVRVESCA EEPQLRRKAD 

       370        380        390        400        410        420 
EEEDYDDNLY DSDMDVVRLD GDDVSPFIQI RSVAKKHPKT WVHYISAEEE DWDYAPAVPS 

       430        440        450        460        470        480 
PSDRSYKSLY LNSGPQRIGR KYKKARFVAY TDVTFKTRKA IPYESGILGP LLYGEVGDTL 

       490        500        510        520        530        540 
LIIFKNKASR PYNIYPHGIT DVSALHPGRL LKGWKHLKDM PILPGETFKY KWTVTVEDGP 

       550        560        570        580        590        600 
TKSDPRCLTR YYSSSINLEK DLASGLIGPL LICYKESVDQ RGNQMMSDKR NVILFSVFDE 

       610        620        630        640        650        660 
NQSWYLAENI QRFLPNPDGL QPQDPEFQAS NIMHSINGYV FDSLQLSVCL HEVAYWYILS 

       670        680        690        700        710        720 
VGAQTDFLSV FFSGYTFKHK MVYEDTLTLF PFSGETVFMS MENPGLWVLG CHNSDLRNRG 

       730        740        750        760        770        780 
MTALLKVYSC DRDIGDYYDN TYEDIPGFLL SGKNVIEPRS FAQNSRPPSA SQKQFQTITS 

       790        800        810        820        830        840 
PEDDVELDPQ SGERTQALEE LSVPSGDGSM LLGQNPAPHG SSSSDLQEAR NEADDYLPGA 

       850        860        870        880        890        900 
RERNTAPSAA ARLRPELHHS AERVLTPEPE KELKKLDSKM SSSSDLLKTS PTIPSDTLSA 

       910        920        930        940        950        960 
ETERTHSLGP PHPQVNFRSQ LGAIVLGKNS SHFIGAGVPL GSTEEDHESS LGENVSPVES 

       970        980        990       1000       1010       1020 
DGIFEKERAH GPASLTKDDV LFKVNISLVK TNKARVYLKT NRKIHIDDAA LLTENRASAT 

      1030       1040       1050       1060       1070       1080 
FMDKNTTASG LNHVSNWIKG PLGKNPLSSE RGPSPELLTS SGSGKSVKGQ SSGQGRIRVA 

      1090       1100       1110       1120       1130       1140 
VEEEELSKGK EMMLPNSELT FLTNSADVQG NDTHSQGKKS REEMERREKL VQEKVDLPQV 

      1150       1160       1170       1180       1190       1200 
YTATGTKNFL RNIFHQSTEP SVEGFDGGSH APVPQDSRSL NDSAERAETH IAHFSAIREE 

      1210       1220       1230       1240       1250       1260 
APLEAPGNRT GPGPRSAVPR RVKQSLKQIR LPLEEIKPER GVVLNATSTR WSESSPILQG 

      1270       1280       1290       1300       1310       1320 
AKRNNLSLPF LTLEMAGGQG KISALGKSAA GPLASGKLEK AVLSSAGLSE ASGKAEFLPK 

      1330       1340       1350       1360       1370       1380 
VRVHREDLLP QKTSNVSCAH GDLGQEIFLQ KTRGPVNLNK VNRPGRTPSK LLGPPMPKEW 

      1390       1400       1410       1420       1430       1440 
ESLEKSPKST ALRTKDIISL PLDRHESNHS IAAKNEGQAE TQREAAWTKQ GGPGRLCAPK 

      1450       1460       1470       1480       1490       1500 
PPVLRRHQRD ISLPTFQPEE DKMDYDDIFS TETKGEDFDI YGEDENQDPR SFQKRTRHYF 

      1510       1520       1530       1540       1550       1560 
IAAVEQLWDY GMSESPRALR NRAQNGEVPR FKKVVFREFA DGSFTQPSYR GELNKHLGLL 

      1570       1580       1590       1600       1610       1620 
GPYIRAEVED NIMVTFKNQA SRPYSFYSSL ISYPDDQEQG AEPRHNFVQP NETRTYFWKV 

      1630       1640       1650       1660       1670       1680 
QHHMAPTEDE FDCKAWAYFS DVDLEKDVHS GLIGPLLICR ANTLNAAHGR QVTVQEFALF 

      1690       1700       1710       1720       1730       1740 
FTIFDETKSW YFTENVERNC RAPCHLQMED PTLKENYRFH AINGYVMDTL PGLVMAQNQR 

      1750       1760       1770       1780       1790       1800 
IRWYLLSMGS NENIHSIHFS GHVFSVRKKE EYKMAVYNLY PGVFETVEML PSKVGIWRIE 

      1810       1820       1830       1840       1850       1860 
CLIGEHLQAG MSTTFLVYSK ECQAPLGMAS GRIRDFQITA SGQYGQWAPK LARLHYSGSI 

      1870       1880       1890       1900       1910       1920 
NAWSTKDPHS WIKVDLLAPM IIHGIMTQGA RQKFSSLYIS QFIIMYSLDG RNWQSYRGNS 

      1930       1940       1950       1960       1970       1980 
TGTLMVFFGN VDASGIKHNI FNPPIVARYI RLHPTHYSIR STLRMELMGC DLNSCSMPLG 

      1990       2000       2010       2020       2030       2040 
MQNKAISDSQ ITASSHLSNI FATWSPSQAR LHLQGRTNAW RPRVSSAEEW LQVDLQKTVK 

      2050       2060       2070       2080       2090       2100 
VTGITTQGVK SLLSSMYVKE FLVSSSQDGR RWTLFLQDGH TKVFQGNQDS STPVVNALDP 

      2110       2120       2130 
PLFTRYLRIH PTSWAQHIAL RLEVLGCEAQ DLY

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References

[1]Healey J.F., Lubin I.M., Lollar P.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A large region (approximately equal to 95 kDa) of human factor VIII is dispensable for in vitro procoagulant activity."
Toole J.J., Pittman D.D., Orr E.C., Murtha P., Wasley L.C., Kaufman R.J.
Proc. Natl. Acad. Sci. U.S.A. 83:5939-5942(1986) [PubMed: 3016730] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 705-1573.
[3]"Elimination of a major inhibitor epitope in factor VIII."
Lubin I.M., Healey J.F., Scandella D., Runge M.S., Lollar P.
J. Biol. Chem. 269:8639-8641(1994) [PubMed: 7510693] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 392-759.

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Cross-references

Sequence databases

U49517 mRNA. Translation: AAB06705.1.
PIRA25945.
T42763.
RefSeqNP_999332.1.
UniGeneSsc.16043

3D structure databases

HSSPHSSP built from PDB template 1D7P based on UniProtKB P00451.
ModBaseSearch...

Genome annotation databases

GeneID397339.
KEGGssc:397339.

Phylogenomic databases

HOVERGENP12263.

Family and domain databases

InterProIPR000421. Coagulation_factor_5/8-type_C.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR014707. Factor_VIII.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 6 hits.
PANTHERPTHR10127:SF50. Factor_VIII. 1 hit.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
SMARTSM00231. FA58C. 2 hits.
[Graphical view]
PROSITEPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 3 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameFA8_PIG
AccessionPrimary (citable) accession number: P12263
Secondary accession number(s): Q95243
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents