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Protein

Coagulation factor V

Gene

F5

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

Functioni

Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.

Enzyme regulationi

Inhibited by SERPINA5.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi139CalciumBy similarity1
Metal bindingi140CalciumBy similarity1
Metal bindingi1843CopperBy similarity1
Metal bindingi1845CopperBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Copper, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:G66-30677-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.
SIGNORiP12259.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor V
Alternative name(s):
Activated protein C cofactor
Proaccelerin, labile factor
Cleaved into the following 2 chains:
Gene namesi
Name:F5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3542. F5.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: Reactome
  • endoplasmic reticulum lumen Source: Reactome
  • ER to Golgi transport vesicle Source: Reactome
  • extracellular region Source: UniProtKB
  • extracellular space Source: Ensembl
  • extracellular vesicle Source: UniProtKB
  • Golgi membrane Source: GOC
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor V deficiency (FA5D)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA blood coagulation disorder leading to a hemorrhagic diathesis known as parahemophilia.
See also OMIM:227400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0327001730Y → C in FA5D; Seoul 2. 2 PublicationsCorresponds to variant rs118203907dbSNPEnsembl.1
Natural variantiVAR_0327012102R → C in FA5D; impairs both factor V secretion and activity. 1 PublicationCorresponds to variant rs118203910dbSNPEnsembl.1
Thrombophilia due to activated protein C resistance (THPH2)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hemostatic disorder due to defective degradation of factor V by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis.
See also OMIM:188055
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013621334R → T in THPH2; Cambridge. 1 PublicationCorresponds to variant rs118203906dbSNPEnsembl.1
Natural variantiVAR_032698387I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. 2 PublicationsCorresponds to variant rs118203911dbSNPEnsembl.1
Natural variantiVAR_032699613C → R in THPH2; Nijkerk. 1 Publication1
Natural variantiVAR_0173292102R → H in THPH2. 1 Publication1
Budd-Chiari syndrome (BDCHS)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera.
See also OMIM:600880
Ischemic stroke (ISCHSTR)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
See also OMIM:601367
Pregnancy loss, recurrent, 1 (RPRGL1)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.
See also OMIM:614389

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

DisGeNETi2153.
MalaCardsiF5.
MIMi188055. phenotype.
227400. phenotype.
600880. phenotype.
601367. phenotype.
614389. phenotype.
OpenTargetsiENSG00000198734.
Orphaneti131. Budd-Chiari syndrome.
329217. Cerebral sinovenous thrombosis.
326. Congenital factor V deficiency.
391320. East Texas bleeding disorder.
64738. Non rare thrombophilia.
PharmGKBiPA159.

Chemistry databases

ChEMBLiCHEMBL3618.
DrugBankiDB05777. ART-123.
DB00055. Drotrecogin alfa.

Polymorphism and mutation databases

BioMutaiF5.
DMDMi308153653.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Add BLAST28
ChainiPRO_000000297829 – 2224Coagulation factor VAdd BLAST2196
ChainiPRO_000000297929 – 737Coagulation factor V heavy chainAdd BLAST709
PropeptideiPRO_0000002980738 – 1573Activation peptide (connecting region)Add BLAST836
ChainiPRO_00000029811574 – 2224Coagulation factor V light chainAdd BLAST651

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi51N-linked (GlcNAc...)Sequence analysis1
Glycosylationi55N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi167 ↔ 193PROSITE-ProRule annotation
Glycosylationi239N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi248 ↔ 329PROSITE-ProRule annotation
Glycosylationi297N-linked (GlcNAc...)2 Publications1
Glycosylationi382N-linked (GlcNAc...)Sequence analysis1
Glycosylationi460N-linked (GlcNAc...)1 Publication1
Glycosylationi468N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi500 ↔ 526PROSITE-ProRule annotation
Glycosylationi554N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi603 ↔ 684PROSITE-ProRule annotation
Modified residuei640PhosphothreonineCombined sources1
Modified residuei693SulfotyrosineSequence analysis1
Modified residuei724SulfotyrosineSequence analysis1
Modified residuei726SulfotyrosineSequence analysis1
Glycosylationi741N-linked (GlcNAc...)Sequence analysis1
Glycosylationi752N-linked (GlcNAc...)Sequence analysis1
Glycosylationi760N-linked (GlcNAc...)Sequence analysis1
Glycosylationi776N-linked (GlcNAc...)Sequence analysis1
Glycosylationi782N-linked (GlcNAc...)Sequence analysis1
Glycosylationi821N-linked (GlcNAc...)1 Publication1
Modified residuei859Phosphoserine; by FAM20C1 Publication1
Glycosylationi938N-linked (GlcNAc...)Sequence analysis1
Glycosylationi977N-linked (GlcNAc...)1 Publication1
Glycosylationi1074N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1083N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1103N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1106N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1479N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1499N-linked (GlcNAc...)Sequence analysis1
Modified residuei1522SulfotyrosineSequence analysis1
Modified residuei1538SulfotyrosineSequence analysis1
Modified residuei1543SulfotyrosineSequence analysis1
Glycosylationi1559N-linked (GlcNAc...)1 Publication1
Modified residuei1593SulfotyrosineSequence analysis1
Glycosylationi1703N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1725 ↔ 1751Curated
Disulfide bondi1907 ↔ 2061PROSITE-ProRule annotation
Glycosylationi2010N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2066 ↔ 2221PROSITE-ProRule annotation
Glycosylationi2209N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus).
Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity.3 Publications
Activated protein C inactivates factor V and factor Va by proteolytic degradation.
Phosphorylated by FAM20C in the extracellular medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei334 – 335Cleavage; by activated protein C2
Sitei534 – 535Cleavage; by activated protein C2
Sitei707 – 708Cleavage; by activated protein C2
Sitei737 – 738Cleavage; by thrombin2
Sitei1022 – 1023Cleavage; by activated protein C2
Sitei1046 – 1047Cleavage; by thrombin2
Sitei1573 – 1574Cleavage; by thrombin2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

MaxQBiP12259.
PaxDbiP12259.
PeptideAtlasiP12259.
PRIDEiP12259.

PTM databases

iPTMnetiP12259.
PhosphoSitePlusiP12259.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSG00000198734.
CleanExiHS_F5.
ExpressionAtlasiP12259. baseline and differential.
GenevisibleiP12259. HS.

Organism-specific databases

HPAiHPA002036.

Interactioni

Subunit structurei

Factor Va, the activated form of factor V, is composed of a heavy chain and a light chain, non-covalently bound. The interaction between the two chains is calcium-dependent. Forms heterodimer with SERPINA5.

Protein-protein interaction databases

BioGridi108452. 13 interactors.
DIPiDIP-47331N.
IntActiP12259. 2 interactors.
STRINGi9606.ENSP00000356771.

Chemistry databases

BindingDBiP12259.

Structurei

Secondary structure

12224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni1569 – 1571Combined sources3
Turni2072 – 2074Combined sources3
Beta strandi2075 – 2077Combined sources3
Helixi2079 – 2081Combined sources3
Beta strandi2082 – 2085Combined sources4
Beta strandi2093 – 2095Combined sources3
Helixi2098 – 2100Combined sources3
Beta strandi2107 – 2109Combined sources3
Beta strandi2111 – 2113Combined sources3
Beta strandi2123 – 2139Combined sources17
Beta strandi2141 – 2143Combined sources3
Beta strandi2146 – 2163Combined sources18
Beta strandi2182 – 2185Combined sources4
Beta strandi2188 – 2211Combined sources24
Beta strandi2213 – 2222Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CZSX-ray1.90A2065-2224[»]
1CZTX-ray1.87A2065-2224[»]
1CZVX-ray2.40A/B2065-2224[»]
1FV4model-H29-691[»]
L1574-2224[»]
1Y61model-H29-737[»]
L1574-2224[»]
3P6ZX-ray1.70C/I685-737[»]
3P70X-ray2.55M/N/O/P685-737[»]
3S9CX-ray1.80B1561-1574[»]
ProteinModelPortaliP12259.
SMRiP12259.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12259.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 329F5/8 type A 1Add BLAST300
Domaini30 – 193Plastocyanin-like 1Add BLAST164
Domaini203 – 329Plastocyanin-like 2Add BLAST127
Domaini348 – 684F5/8 type A 2Add BLAST337
Domaini348 – 526Plastocyanin-like 3Add BLAST179
Domaini536 – 684Plastocyanin-like 4Add BLAST149
Repeati895 – 9111-1Add BLAST17
Repeati912 – 9281-2Add BLAST17
Repeati1185 – 11932-19
Repeati1194 – 12022-29
Repeati1203 – 12112-39
Repeati1212 – 12202-49
Repeati1221 – 12292-59
Repeati1230 – 12382-69
Repeati1239 – 12472-79
Repeati1248 – 12562-89
Repeati1257 – 12652-99
Repeati1266 – 12742-109
Repeati1275 – 12832-119
Repeati1284 – 12922-129
Repeati1293 – 13012-139
Repeati1302 – 13102-149
Repeati1311 – 13192-159
Repeati1320 – 13282-169
Repeati1329 – 13372-179
Repeati1338 – 13462-189
Repeati1347 – 13552-199
Repeati1356 – 13642-209
Repeati1365 – 13732-219
Repeati1374 – 13822-229
Repeati1383 – 13912-239
Repeati1392 – 14002-249
Repeati1401 – 14092-259
Repeati1410 – 14182-269
Repeati1419 – 14272-279
Repeati1428 – 14362-289
Repeati1437 – 14452-299
Repeati1446 – 14542-309
Repeati1455 – 14632-319
Repeati1464 – 14722-329
Repeati1473 – 14812-339
Repeati1482 – 14902-349
Repeati1493 – 15012-359
Domaini1578 – 1907F5/8 type A 3Add BLAST330
Domaini1578 – 1751Plastocyanin-like 5Add BLAST174
Domaini1761 – 1907Plastocyanin-like 6Add BLAST147
Domaini1907 – 2061F5/8 type C 1PROSITE-ProRule annotationAdd BLAST155
Domaini2066 – 2221F5/8 type C 2PROSITE-ProRule annotationAdd BLAST156

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni692 – 1573BAdd BLAST882
Regioni895 – 9282 X 17 AA tandem repeatsAdd BLAST34
Regioni1185 – 150135 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-TAdd BLAST317

Domaini

Domain B contains 35 x 9 AA tandem repeats, and 2 x 17 AA repeats.

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.
HOVERGENiHBG005631.
InParanoidiP12259.
KOiK03902.
PhylomeDBiP12259.
TreeFamiTF329807.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR024715. Factor_5/8.
IPR029821. Factor_V.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF597. PTHR10127:SF597. 3 hits.
PfamiPF07732. 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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12259-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPGCPRLWV LVVLGTSWVG WGSQGTEAAQ LRQFYVAAQG ISWSYRPEPT
60 70 80 90 100
NSSLNLSVTS FKKIVYREYE PYFKKEKPQS TISGLLGPTL YAEVGDIIKV
110 120 130 140 150
HFKNKADKPL SIHPQGIRYS KLSEGASYLD HTFPAEKMDD AVAPGREYTY
160 170 180 190 200
EWSISEDSGP THDDPPCLTH IYYSHENLIE DFNSGLIGPL LICKKGTLTE
210 220 230 240 250
GGTQKTFDKQ IVLLFAVFDE SKSWSQSSSL MYTVNGYVNG TMPDITVCAH
260 270 280 290 300
DHISWHLLGM SSGPELFSIH FNGQVLEQNH HKVSAITLVS ATSTTANMTV
310 320 330 340 350
GPEGKWIISS LTPKHLQAGM QAYIDIKNCP KKTRNLKKIT REQRRHMKRW
360 370 380 390 400
EYFIAAEEVI WDYAPVIPAN MDKKYRSQHL DNFSNQIGKH YKKVMYTQYE
410 420 430 440 450
DESFTKHTVN PNMKEDGILG PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV
460 470 480 490 500
TFSPYEDEVN SSFTSGRNNT MIRAVQPGET YTYKWNILEF DEPTENDAQC
510 520 530 540 550
LTRPYYSDVD IMRDIASGLI GLLLICKSRS LDRRGIQRAA DIEQQAVFAV
560 570 580 590 600
FDENKSWYLE DNINKFCENP DEVKRDDPKF YESNIMSTIN GYVPESITTL
610 620 630 640 650
GFCFDDTVQW HFCSVGTQNE ILTIHFTGHS FIYGKRHEDT LTLFPMRGES
660 670 680 690 700
VTVTMDNVGT WMLTSMNSSP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE
710 720 730 740 750
STVMATRKMH DRLEPEDEES DADYDYQNRL AAALGIRSFR NSSLNQEEEE
760 770 780 790 800
FNLTALALEN GTEFVSSNTD IIVGSNYSSP SNISKFTVNN LAEPQKAPSH
810 820 830 840 850
QQATTAGSPL RHLIGKNSVL NSSTAEHSSP YSEDPIEDPL QPDVTGIRLL
860 870 880 890 900
SLGAGEFKSQ EHAKHKGPKV ERDQAAKHRF SWMKLLAHKV GRHLSQDTGS
910 920 930 940 950
PSGMRPWEDL PSQDTGSPSR MRPWKDPPSD LLLLKQSNSS KILVGRWHLA
960 970 980 990 1000
SEKGSYEIIQ DTDEDTAVNN WLISPQNASR AWGESTPLAN KPGKQSGHPK
1010 1020 1030 1040 1050
FPRVRHKSLQ VRQDGGKSRL KKSQFLIKTR KKKKEKHTHH APLSPRTFHP
1060 1070 1080 1090 1100
LRSEAYNTFS ERRLKHSLVL HKSNETSLPT DLNQTLPSMD FGWIASLPDH
1110 1120 1130 1140 1150
NQNSSNDTGQ ASCPPGLYQT VPPEEHYQTF PIQDPDQMHS TSDPSHRSSS
1160 1170 1180 1190 1200
PELSEMLEYD RSHKSFPTDI SQMSPSSEHE VWQTVISPDL SQVTLSPELS
1210 1220 1230 1240 1250
QTNLSPDLSH TTLSPELIQR NLSPALGQMP ISPDLSHTTL SPDLSHTTLS
1260 1270 1280 1290 1300
LDLSQTNLSP ELSQTNLSPA LGQMPLSPDL SHTTLSLDFS QTNLSPELSH
1310 1320 1330 1340 1350
MTLSPELSQT NLSPALGQMP ISPDLSHTTL SLDFSQTNLS PELSQTNLSP
1360 1370 1380 1390 1400
ALGQMPLSPD PSHTTLSLDL SQTNLSPELS QTNLSPDLSE MPLFADLSQI
1410 1420 1430 1440 1450
PLTPDLDQMT LSPDLGETDL SPNFGQMSLS PDLSQVTLSP DISDTTLLPD
1460 1470 1480 1490 1500
LSQISPPPDL DQIFYPSESS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND
1510 1520 1530 1540 1550
TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDDPY
1560 1570 1580 1590 1600
KTDVRTNINS SRDPDNIAAW YLRSNNGNRR NYYIAAEEIS WDYSEFVQRE
1610 1620 1630 1640 1650
TDIEDSDDIP EDTTYKKVVF RKYLDSTFTK RDPRGEYEEH LGILGPIIRA
1660 1670 1680 1690 1700
EVDDVIQVRF KNLASRPYSL HAHGLSYEKS SEGKTYEDDS PEWFKEDNAV
1710 1720 1730 1740 1750
QPNSSYTYVW HATERSGPES PGSACRAWAY YSAVNPEKDI HSGLIGPLLI
1760 1770 1780 1790 1800
CQKGILHKDS NMPMDMREFV LLFMTFDEKK SWYYEKKSRS SWRLTSSEMK
1810 1820 1830 1840 1850
KSHEFHAING MIYSLPGLKM YEQEWVRLHL LNIGGSQDIH VVHFHGQTLL
1860 1870 1880 1890 1900
ENGNKQHQLG VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQRAGMQTPF
1910 1920 1930 1940 1950
LIMDRDCRMP MGLSTGIISD SQIKASEFLG YWEPRLARLN NGGSYNAWSV
1960 1970 1980 1990 2000
EKLAAEFASK PWIQVDMQKE VIITGIQTQG AKHYLKSCYT TEFYVAYSSN
2010 2020 2030 2040 2050
QINWQIFKGN STRNVMYFNG NSDASTIKEN QFDPPIVARY IRISPTRAYN
2060 2070 2080 2090 2100
RPTLRLELQG CEVNGCSTPL GMENGKIENK QITASSFKKS WWGDYWEPFR
2110 2120 2130 2140 2150
ARLNAQGRVN AWQAKANNNK QWLEIDLLKI KKITAIITQG CKSLSSEMYV
2160 2170 2180 2190 2200
KSYTIHYSEQ GVEWKPYRLK SSMVDKIFEG NTNTKGHVKN FFNPPIISRF
2210 2220
IRVIPKTWNQ SIALRLELFG CDIY
Length:2,224
Mass (Da):251,703
Last modified:October 5, 2010 - v4
Checksum:i24AEF3FEA7332E37
GO

Sequence cautioni

The sequence ABD23003 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI23065 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti741N → S in ABD23003 (Ref. 7) Curated1
Sequence conflicti908E → K in AAA52424 (PubMed:3110773).Curated1
Sequence conflicti908E → K in CAC82573 (PubMed:11758222).Curated1
Sequence conflicti991K → E in BAF84302 (PubMed:14702039).Curated1
Sequence conflicti2213A → T in AAA52424 (PubMed:3110773).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02129715G → S.1 PublicationCorresponds to variant rs9332485dbSNPEnsembl.1
Natural variantiVAR_013886107D → H.2 PublicationsCorresponds to variant rs6019dbSNPEnsembl.1
Natural variantiVAR_013620334R → G in Hong Kong; does not predispose to clinical thrombosis. 2 PublicationsCorresponds to variant rs118203905dbSNPEnsembl.1
Natural variantiVAR_013621334R → T in THPH2; Cambridge. 1 PublicationCorresponds to variant rs118203906dbSNPEnsembl.1
Natural variantiVAR_032698387I → T in THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain. 2 PublicationsCorresponds to variant rs118203911dbSNPEnsembl.1
Natural variantiVAR_013887413M → T.2 PublicationsCorresponds to variant rs6033dbSNPEnsembl.1
Natural variantiVAR_013622513R → K.4 PublicationsCorresponds to variant rs6020dbSNPEnsembl.1
Natural variantiVAR_001213534R → Q in Leiden; associated with thrombophilia; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke. 5 PublicationsCorresponds to variant rs6025dbSNPEnsembl.1
Natural variantiVAR_032699613C → R in THPH2; Nijkerk. 1 Publication1
Natural variantiVAR_035817775S → A in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_047740781S → R.Corresponds to variant rs13306350dbSNPEnsembl.1
Natural variantiVAR_013888809P → S.2 PublicationsCorresponds to variant rs6031dbSNPEnsembl.1
Natural variantiVAR_013889817N → T.2 PublicationsCorresponds to variant rs6018dbSNPEnsembl.1
Natural variantiVAR_001214858K → R.5 PublicationsCorresponds to variant rs4524dbSNPEnsembl.1
Natural variantiVAR_001215865H → R.5 PublicationsCorresponds to variant rs4525dbSNPEnsembl.1
Natural variantiVAR_021298915T → S.1 PublicationCorresponds to variant rs9332695dbSNPEnsembl.1
Natural variantiVAR_013890925K → E.5 PublicationsCorresponds to variant rs6032dbSNPEnsembl.1
Natural variantiVAR_021299969N → S.1 PublicationCorresponds to variant rs9332604dbSNPEnsembl.1
Natural variantiVAR_021300980R → L.1 PublicationCorresponds to variant rs9332605dbSNPEnsembl.1
Natural variantiVAR_0138911146H → Q.2 PublicationsCorresponds to variant rs6005dbSNPEnsembl.1
Natural variantiVAR_0138921285L → I.3 PublicationsCorresponds to variant rs1046712dbSNPEnsembl.1
Natural variantiVAR_0138931327H → R.2 PublicationsCorresponds to variant rs1800595dbSNPEnsembl.1
Natural variantiVAR_0477411397L → F.2 PublicationsCorresponds to variant rs13306334dbSNPEnsembl.1
Natural variantiVAR_0213011404P → S.1 PublicationCorresponds to variant rs9332608dbSNPEnsembl.1
Natural variantiVAR_0138941530E → A.2 PublicationsCorresponds to variant rs6007dbSNPEnsembl.1
Natural variantiVAR_0138951685T → S.1 PublicationCorresponds to variant rs6011dbSNPEnsembl.1
Natural variantiVAR_0327001730Y → C in FA5D; Seoul 2. 2 PublicationsCorresponds to variant rs118203907dbSNPEnsembl.1
Natural variantiVAR_0138961749L → V.1 PublicationCorresponds to variant rs6034dbSNPEnsembl.1
Natural variantiVAR_0138971764M → V.3 PublicationsCorresponds to variant rs6030dbSNPEnsembl.1
Natural variantiVAR_0138981820M → I.1 PublicationCorresponds to variant rs6026dbSNPEnsembl.1
Natural variantiVAR_0327012102R → C in FA5D; impairs both factor V secretion and activity. 1 PublicationCorresponds to variant rs118203910dbSNPEnsembl.1
Natural variantiVAR_0173292102R → H in THPH2. 1 Publication1
Natural variantiVAR_0213022148M → T.1 PublicationCorresponds to variant rs9332701dbSNPEnsembl.1
Natural variantiVAR_0346032185K → R.Corresponds to variant rs6679078dbSNPEnsembl.1
Natural variantiVAR_0138992222D → G.1 PublicationCorresponds to variant rs6027dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16967 mRNA. Translation: AAA52424.1.
L32779
, L32755, L32756, L32757, L32758, L32759, L32760, L32761, L32762, L32763, L32764, L32765, L32766, L32767, L32768, L32769, L32770, L32771, L32772, L32773, L32774, L32775, L32776, L32777, L32778 Genomic DNA. Translation: AAB59401.1.
AY364535 Genomic DNA. Translation: AAQ55063.1.
Z99572 Genomic DNA. Translation: CAB16748.1.
Z99572 Genomic DNA. Translation: CAI23065.1. Sequence problems.
AK291613 mRNA. Translation: BAF84302.1.
M14335 mRNA. Translation: AAB59532.1.
DQ377944 Genomic DNA. Translation: ABD23003.1. Sequence problems.
AJ297255 mRNA. Translation: CAC82573.1.
CCDSiCCDS1281.1.
PIRiA56172. KFHU5.
RefSeqiNP_000121.2. NM_000130.4.
UniGeneiHs.30054.

Genome annotation databases

EnsembliENST00000367797; ENSP00000356771; ENSG00000198734.
GeneIDi2153.
KEGGihsa:2153.
UCSCiuc001ggg.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Factor V entry

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16967 mRNA. Translation: AAA52424.1.
L32779
, L32755, L32756, L32757, L32758, L32759, L32760, L32761, L32762, L32763, L32764, L32765, L32766, L32767, L32768, L32769, L32770, L32771, L32772, L32773, L32774, L32775, L32776, L32777, L32778 Genomic DNA. Translation: AAB59401.1.
AY364535 Genomic DNA. Translation: AAQ55063.1.
Z99572 Genomic DNA. Translation: CAB16748.1.
Z99572 Genomic DNA. Translation: CAI23065.1. Sequence problems.
AK291613 mRNA. Translation: BAF84302.1.
M14335 mRNA. Translation: AAB59532.1.
DQ377944 Genomic DNA. Translation: ABD23003.1. Sequence problems.
AJ297255 mRNA. Translation: CAC82573.1.
CCDSiCCDS1281.1.
PIRiA56172. KFHU5.
RefSeqiNP_000121.2. NM_000130.4.
UniGeneiHs.30054.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CZSX-ray1.90A2065-2224[»]
1CZTX-ray1.87A2065-2224[»]
1CZVX-ray2.40A/B2065-2224[»]
1FV4model-H29-691[»]
L1574-2224[»]
1Y61model-H29-737[»]
L1574-2224[»]
3P6ZX-ray1.70C/I685-737[»]
3P70X-ray2.55M/N/O/P685-737[»]
3S9CX-ray1.80B1561-1574[»]
ProteinModelPortaliP12259.
SMRiP12259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108452. 13 interactors.
DIPiDIP-47331N.
IntActiP12259. 2 interactors.
STRINGi9606.ENSP00000356771.

Chemistry databases

BindingDBiP12259.
ChEMBLiCHEMBL3618.
DrugBankiDB05777. ART-123.
DB00055. Drotrecogin alfa.

PTM databases

iPTMnetiP12259.
PhosphoSitePlusiP12259.

Polymorphism and mutation databases

BioMutaiF5.
DMDMi308153653.

Proteomic databases

MaxQBiP12259.
PaxDbiP12259.
PeptideAtlasiP12259.
PRIDEiP12259.

Protocols and materials databases

DNASUi2153.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367797; ENSP00000356771; ENSG00000198734.
GeneIDi2153.
KEGGihsa:2153.
UCSCiuc001ggg.2. human.

Organism-specific databases

CTDi2153.
DisGeNETi2153.
GeneCardsiF5.
GeneReviewsiF5.
HGNCiHGNC:3542. F5.
HPAiHPA002036.
MalaCardsiF5.
MIMi188055. phenotype.
227400. phenotype.
600880. phenotype.
601367. phenotype.
612309. gene.
614389. phenotype.
neXtProtiNX_P12259.
OpenTargetsiENSG00000198734.
Orphaneti131. Budd-Chiari syndrome.
329217. Cerebral sinovenous thrombosis.
326. Congenital factor V deficiency.
391320. East Texas bleeding disorder.
64738. Non rare thrombophilia.
PharmGKBiPA159.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ6Y. Eukaryota.
ENOG4111F6G. LUCA.
GeneTreeiENSGT00550000074552.
HOVERGENiHBG005631.
InParanoidiP12259.
KOiK03902.
PhylomeDBiP12259.
TreeFamiTF329807.

Enzyme and pathway databases

BioCyciZFISH:G66-30677-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.
SIGNORiP12259.

Miscellaneous databases

EvolutionaryTraceiP12259.
GeneWikiiFactor_V.
GenomeRNAii2153.
PROiP12259.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198734.
CleanExiHS_F5.
ExpressionAtlasiP12259. baseline and differential.
GenevisibleiP12259. HS.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR024715. Factor_5/8.
IPR029821. Factor_V.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF597. PTHR10127:SF597. 3 hits.
PfamiPF07732. 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. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFA5_HUMAN
AccessioniPrimary (citable) accession number: P12259
Secondary accession number(s): A8K6E8
, Q14285, Q2EHR5, Q5R346, Q5R347, Q6UPU6, Q8WWQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 5, 2010
Last modified: November 2, 2016
This is version 206 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.