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Protein

Coagulation factor V

Gene

F5

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

Functioni

Coagulation factor V is a cofactor that participates with factor Xa to activate prothrombin to thrombin.

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi139CalciumBy similarity1
Metal bindingi140CalciumBy similarity1
Metal bindingi1877CopperBy similarity1
Metal bindingi1879CopperBy similarity1
Metal bindingi1919CopperBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor V
Alternative name(s):
Activated protein C cofactor
Cleaved into the following 2 chains:
Gene namesi
Name:F5
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 – 22Sequence analysisAdd BLAST22
ChainiPRO_000000298223 – 2258Coagulation factor VAdd BLAST2236
ChainiPRO_000000298323 – 737Coagulation factor V heavy chainBy similarityAdd BLAST715
PropeptideiPRO_0000002984738 – 1611Activation peptide (connecting region)By similarityAdd BLAST874
ChainiPRO_00000029851612 – 2258Coagulation factor V light chainBy similarityAdd BLAST647

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi153N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi167 ↔ 193PROSITE-ProRule annotation
Glycosylationi225N-linked (GlcNAc...)Sequence analysis1
Glycosylationi239N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi248 ↔ 329PROSITE-ProRule annotation
Glycosylationi297N-linked (GlcNAc...)Sequence analysis1
Glycosylationi382N-linked (GlcNAc...)Sequence analysis1
Glycosylationi460N-linked (GlcNAc...)Sequence analysis1
Glycosylationi467N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi499 ↔ 525PROSITE-ProRule annotation
Glycosylationi553N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi602 ↔ 683PROSITE-ProRule annotation
Modified residuei639PhosphothreonineBy similarity1
Modified residuei692SulfotyrosineSequence analysis1
Modified residuei696SulfotyrosineSequence analysis1
Modified residuei724SulfotyrosineSequence analysis1
Modified residuei726SulfotyrosineSequence analysis1
Glycosylationi741N-linked (GlcNAc...)Sequence analysis1
Modified residuei745SulfotyrosineSequence analysis1
Glycosylationi752N-linked (GlcNAc...)Sequence analysis1
Glycosylationi760N-linked (GlcNAc...)Sequence analysis1
Glycosylationi776N-linked (GlcNAc...)Sequence analysis1
Glycosylationi782N-linked (GlcNAc...)Sequence analysis1
Glycosylationi899N-linked (GlcNAc...)Sequence analysis1
Glycosylationi960N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1048N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1057N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1066N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1073N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1089N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1174N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1480N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1537N-linked (GlcNAc...)Sequence analysis1
Modified residuei1560SulfotyrosineSequence analysis1
Modified residuei1576SulfotyrosineSequence analysis1
Modified residuei1581SulfotyrosineSequence analysis1
Modified residuei1584SulfotyrosineSequence analysis1
Modified residuei1588SulfotyrosineSequence analysis1
Glycosylationi1597N-linked (GlcNAc...)Sequence analysis1
Modified residuei1631SulfotyrosineSequence analysis1
Glycosylationi1737N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1759 ↔ 1785Curated
Glycosylationi1886N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1941 ↔ 2095PROSITE-ProRule annotation
Glycosylationi2044N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2100 ↔ 2255PROSITE-ProRule annotation
Glycosylationi2243N-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).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei737 – 738Cleavage; by thrombinBy similarity2
Sitei1029 – 1030Cleavage; by thrombinBy similarity2
Sitei1611 – 1612Cleavage; by thrombinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

PaxDbiQ9GLP1.
PeptideAtlasiQ9GLP1.
PRIDEiQ9GLP1.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000006704.

Structurei

3D structure databases

ProteinModelPortaliQ9GLP1.
ModBaseiSearch...
MobiDBiSearch...

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 – 683F5/8 type A 2Add BLAST336
Domaini348 – 525Plastocyanin-like 3Add BLAST178
Domaini535 – 683Plastocyanin-like 4Add BLAST149
Repeati1168 – 117619
Repeati1177 – 118529
Repeati1186 – 119439
Repeati1195 – 120349
Repeati1204 – 121259
Repeati1213 – 122169
Repeati1222 – 123079
Repeati1231 – 123989
Repeati1240 – 124899
Repeati1249 – 1257109
Repeati1258 – 1266119
Repeati1267 – 1275129
Repeati1276 – 1284139
Repeati1285 – 1293149
Repeati1294 – 1302159
Repeati1303 – 1311169
Repeati1312 – 1320179
Repeati1321 – 1329189
Repeati1330 – 1338199
Repeati1339 – 1347209
Repeati1348 – 1356219
Repeati1357 – 1365229
Repeati1366 – 1374239
Repeati1375 – 1383249
Repeati1384 – 1392259
Repeati1393 – 1401269
Repeati1402 – 1410279
Repeati1411 – 1419289
Repeati1420 – 1428299
Repeati1429 – 1437309
Repeati1438 – 1446319
Repeati1447 – 1455329
Repeati1456 – 1464339
Repeati1465 – 1473349
Repeati1474 – 1482359
Repeati1483 – 1491369
Repeati1492 – 1500379
Repeati1501 – 1509389
Repeati1510 – 1518399
Repeati1519 – 1527409
Repeati1531 – 1539419
Domaini1616 – 1941F5/8 type A 3Add BLAST326
Domaini1616 – 1785Plastocyanin-like 5Add BLAST170
Domaini1795 – 1941Plastocyanin-like 6Add BLAST147
Domaini1941 – 2095F5/8 type C 1PROSITE-ProRule annotationAdd BLAST155
Domaini2100 – 2255F5/8 type C 2PROSITE-ProRule annotationAdd BLAST156

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni691 – 1611BAdd BLAST921
Regioni1168 – 153941 X 9 AA approximate tandem repeats of T-L-S-P-D-L-[GS]-[HQ]-TAdd BLAST372

Domaini

Domain B contains 41 X 9 AA tandem repeats. Domains C1 and C2 may be involved in membrane binding.

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.
HOGENOMiHOG000082542.
HOVERGENiHBG005631.
InParanoidiQ9GLP1.
KOiK03902.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR009271. Coagulation_factor_V_LSPD.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
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.
PF06049. LSPR. 36 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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9GLP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPALPCPWV LVVLGTSWAA WGNLGTEAAR VRQFYVAAQS ISWNYHPEPT
60 70 80 90 100
HPSSSPFATS FKKIVYREYE AYFQKEKPPS RMSGLLGPTL YADVGDIMKV
110 120 130 140 150
HFRNKADKPL SIHPQGIKYS KFAEGASYPD HTFLVEKMDD AVAPGQEYTY
160 170 180 190 200
EWNISEDSGP THNDPPCLTH IYYSYENLIQ DFNSGLIGPL LICKKGTLTE
210 220 230 240 250
DGIQKMFDKQ YVLMFAVFDE SKSWNQSSSL MYTVNGYVNG TMPDITVCAY
260 270 280 290 300
DHISWHLIGM SSGPELFSIH FSGQVLEQNH HKVSAITLVS ATSTTANMTV
310 320 330 340 350
SPEGKWPISS LIPKHFQAGM QAYIDIKNCA KKTRKPKKLT RDQRRHIKRW
360 370 380 390 400
EYFIAAEEVI WDYAPIIPAN MDKKYRSLHL DNFSNQIGKH YKKVVYKQYQ
410 420 430 440 450
DESFTKRLEN PNNKEDGILG PVIRAQVRDT LKIVFKNMAS RSYSIYPHGV
460 470 480 490 500
TFSPYEDDVN SSSTSDNNTM IRAVQPGETY TYKWNILESD EPTENDAQCL
510 520 530 540 550
TRPYYSNVDI TRDIASGLIG LLLICKSRSL DKRGIQRTAD IEQKAVFAVF
560 570 580 590 600
DENKSWYIED NIYKFCENPE KVKRDDPKFY ESNIMSTING YVPESIPTLG
610 620 630 640 650
FCFDDTVQWH FCSVRTHDNI LTIHFTGHSF IYGKRHEDTL TLFPMRGESV
660 670 680 690 700
TVTMDNVGTW MLTTMNSNPR NKKLQLKFRD VKCIRDDDED SYEIIYEPSS
710 720 730 740 750
STTLTTRKMH DSSENKEEEN DDEYDYQDLL ASVLGIRSFR NSSLYQEDDE
760 770 780 790 800
FNLTALALEN NSEFIPPSTD RAVDSNSSSP GNISRAPANT FTEPRKILPH
810 820 830 840 850
PEATKAGSPR RHTGLVKNLV LNRRRTQHSD PYSEDPIENP LQSVITGISL
860 870 880 890 900
LPFGTEGFRN REHPKHKRFK AGRDQAAKHR FSQMEFPAHK TGRHISQDNS
910 920 930 940 950
SSSSMGPLED LSSDLLLLER KDPSTINGKW HLVSEKGSYE IVQDADEDMA
960 970 980 990 1000
VNKLPNNPQN ASRSWGENIP FTNKHGKQRG HPIFVTRHKL LQERQDEGNS
1010 1020 1030 1040 1050
ILKKGRFFIR TRRKKKERKP VHHVPLSPRS FNPLRGEANT PFSDRRQNHS
1060 1070 1080 1090 1100
LLLHESNETF PPTDLNQTFP SMNLSLIASH PDHNQNLPND THQTSSPLDL
1110 1120 1130 1140 1150
YQTVTPDEPY QTAPIQDLDP THSTAVPSHQ SSLPEPIQMH DYDLRNKASP
1160 1170 1180 1190 1200
TDVSEMFFSL KLKAGHRTTS PDLNQTSLSP ELSQTTLSPD PGHVTLSPDL
1210 1220 1230 1240 1250
SQTTLSPDLS HTTLSPDLGH TTLSPDLSHT TLSPDLSQTT LSPDLSHTTL
1260 1270 1280 1290 1300
SPDLGHTTLS PDLSHTTLSP DLGHATLSPD LSHTTLSPDL GHTTLSPDLG
1310 1320 1330 1340 1350
HTTLSPDFSQ TTLSPDLGHT TLSSDVSHTT LSPDLSHTTL SPDLSHTTLS
1360 1370 1380 1390 1400
PDLGHTTLSP DLSQTTLSPD LGHMTLSPDL SHTTLSPDLG HTTLSPDLSH
1410 1420 1430 1440 1450
TTLSPDLGHM TLSPDLGQTT LSLDFGQTTL SPDLSHMTLS SELSHETLSP
1460 1470 1480 1490 1500
DLSQVTLSPD LSEIPFSPDL WQTTLSSDLN ETTLSPDLRQ TSPHPDPDKT
1510 1520 1530 1540 1550
SYISESSQSV TLPEFGQTSP FPDLGQRPSP PSHSTLNNTF IPREFNPMVV
1560 1570 1580 1590 1600
VGLSRDDGDY VEIIPRQQEE NSEEDYVKID YVEYDDPYQT DVRTDINSSR
1610 1620 1630 1640 1650
NPDNIAAWYL RSNNGNRRNY YIAAEELSWD YSKFTQREDI DDVPEHTIYK
1660 1670 1680 1690 1700
KVVFRKYLDS TFTKLDPRGE YEEHLGILGP IIRAEVDDVI QVRFKNLASR
1710 1720 1730 1740 1750
PYSLHAHGLS YEKSSEGKTY EDDSPEWFKE DNAVQPNSSY TYVWHATERS
1760 1770 1780 1790 1800
GPESPGSACR AWAYYSAVNP EKDIHSGLIG PLLICRKGTL HKENNMPVDM
1810 1820 1830 1840 1850
REFVLLFMVF DEKKSWYYEK KFTRSWRLTS SEVKNSHKFH AINGMIYNLP
1860 1870 1880 1890 1900
GLRMYEQEWV RLHLLNLGGS RDIHVVHFHG QTLLENGTQQ HQLGVWPLLP
1910 1920 1930 1940 1950
GSFKTLEMKT SKAGWWLLDT EVGENQRAGM QTPFLIIDRE CKMPMGLSTG
1960 1970 1980 1990 2000
LIADSQIKAS EFWGHWQPKL ARLNNGGSYN AWITDKFSGE SNSKPWIQVD
2010 2020 2030 2040 2050
MQREVVFTGI QTQGAKYYLK SYYTTEFNVA YSSDQRNWRI FKGNSTKNVM
2060 2070 2080 2090 2100
YFNGNSDAST ITENQFDPPV VARYIRISPT ESYNKPALRL ELQGCEVNGC
2110 2120 2130 2140 2150
STPLGMESGN IKNEQITASS FKKSWWGDYW EPFRARLNAQ GRVNAWQAKA
2160 2170 2180 2190 2200
NNNNQWLQID LLKIKKITAI TTQGCKSLSS EMYVKRYTIQ YSDRGVEWKS
2210 2220 2230 2240 2250
YREKSSMVDK IFEGNNNIKG HVKNFFNPPI ISRFIRIIPK MWNQSIALRL

ELFGCDIY
Length:2,258
Mass (Da):256,080
Last modified:March 1, 2001 - v1
Checksum:i9159B9E0076A2ACC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191308 mRNA. Translation: AAG28381.1.
RefSeqiNP_999285.1. NM_214120.1.
UniGeneiSsc.15822.

Genome annotation databases

GeneIDi397217.
KEGGissc:397217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191308 mRNA. Translation: AAG28381.1.
RefSeqiNP_999285.1. NM_214120.1.
UniGeneiSsc.15822.

3D structure databases

ProteinModelPortaliQ9GLP1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000006704.

Proteomic databases

PaxDbiQ9GLP1.
PeptideAtlasiQ9GLP1.
PRIDEiQ9GLP1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397217.
KEGGissc:397217.

Organism-specific databases

CTDi2153.

Phylogenomic databases

eggNOGiENOG410IJ6Y. Eukaryota.
ENOG4111F6G. LUCA.
HOGENOMiHOG000082542.
HOVERGENiHBG005631.
InParanoidiQ9GLP1.
KOiK03902.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR009271. Coagulation_factor_V_LSPD.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
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.
PF06049. LSPR. 36 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. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFA5_PIG
AccessioniPrimary (citable) accession number: Q9GLP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 1, 2001
Last modified: October 5, 2016
This is version 103 of the entry and version 1 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. 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.