Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391CalciumBy similarity
Metal bindingi140 – 1401CalciumBy similarity
Metal bindingi1877 – 18771CopperBy similarity
Metal bindingi1879 – 18791CopperBy similarity
Metal bindingi1919 – 19191CopperBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 22582236Coagulation factor VPRO_0000002982Add
BLAST
Chaini23 – 737715Coagulation factor V heavy chainBy similarityPRO_0000002983Add
BLAST
Propeptidei738 – 1611874Activation peptide (connecting region)By similarityPRO_0000002984Add
BLAST
Chaini1612 – 2258647Coagulation factor V light chainBy similarityPRO_0000002985Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence analysis
Disulfide bondi167 ↔ 193PROSITE-ProRule annotation
Glycosylationi225 – 2251N-linked (GlcNAc...)Sequence analysis
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence analysis
Disulfide bondi248 ↔ 329PROSITE-ProRule annotation
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence analysis
Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence analysis
Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence analysis
Glycosylationi467 – 4671N-linked (GlcNAc...)Sequence analysis
Disulfide bondi499 ↔ 525PROSITE-ProRule annotation
Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence analysis
Disulfide bondi602 ↔ 683PROSITE-ProRule annotation
Modified residuei639 – 6391PhosphothreonineBy similarity
Modified residuei692 – 6921SulfotyrosineSequence analysis
Modified residuei696 – 6961SulfotyrosineSequence analysis
Modified residuei724 – 7241SulfotyrosineSequence analysis
Modified residuei726 – 7261SulfotyrosineSequence analysis
Glycosylationi741 – 7411N-linked (GlcNAc...)Sequence analysis
Modified residuei745 – 7451SulfotyrosineSequence analysis
Glycosylationi752 – 7521N-linked (GlcNAc...)Sequence analysis
Glycosylationi760 – 7601N-linked (GlcNAc...)Sequence analysis
Glycosylationi776 – 7761N-linked (GlcNAc...)Sequence analysis
Glycosylationi782 – 7821N-linked (GlcNAc...)Sequence analysis
Glycosylationi899 – 8991N-linked (GlcNAc...)Sequence analysis
Glycosylationi960 – 9601N-linked (GlcNAc...)Sequence analysis
Glycosylationi1048 – 10481N-linked (GlcNAc...)Sequence analysis
Glycosylationi1057 – 10571N-linked (GlcNAc...)Sequence analysis
Glycosylationi1066 – 10661N-linked (GlcNAc...)Sequence analysis
Glycosylationi1073 – 10731N-linked (GlcNAc...)Sequence analysis
Glycosylationi1089 – 10891N-linked (GlcNAc...)Sequence analysis
Glycosylationi1174 – 11741N-linked (GlcNAc...)Sequence analysis
Glycosylationi1480 – 14801N-linked (GlcNAc...)Sequence analysis
Glycosylationi1537 – 15371N-linked (GlcNAc...)Sequence analysis
Modified residuei1560 – 15601SulfotyrosineSequence analysis
Modified residuei1576 – 15761SulfotyrosineSequence analysis
Modified residuei1581 – 15811SulfotyrosineSequence analysis
Modified residuei1584 – 15841SulfotyrosineSequence analysis
Modified residuei1588 – 15881SulfotyrosineSequence analysis
Glycosylationi1597 – 15971N-linked (GlcNAc...)Sequence analysis
Modified residuei1631 – 16311SulfotyrosineSequence analysis
Glycosylationi1737 – 17371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1759 ↔ 1785Curated
Glycosylationi1886 – 18861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1941 ↔ 2095PROSITE-ProRule annotation
Glycosylationi2044 – 20441N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2100 ↔ 2255PROSITE-ProRule annotation
Glycosylationi2243 – 22431N-linked (GlcNAc...)Sequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei737 – 7382Cleavage; by thrombinBy similarity
Sitei1029 – 10302Cleavage; by thrombinBy similarity
Sitei1611 – 16122Cleavage; by thrombinBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

PaxDbiQ9GLP1.
PeptideAtlasiQ9GLP1.

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.
SMRiQ9GLP1. Positions 1613-2257.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 329300F5/8 type A 1Add
BLAST
Domaini30 – 193164Plastocyanin-like 1Add
BLAST
Domaini203 – 329127Plastocyanin-like 2Add
BLAST
Domaini348 – 683336F5/8 type A 2Add
BLAST
Domaini348 – 525178Plastocyanin-like 3Add
BLAST
Domaini535 – 683149Plastocyanin-like 4Add
BLAST
Repeati1168 – 117691
Repeati1177 – 118592
Repeati1186 – 119493
Repeati1195 – 120394
Repeati1204 – 121295
Repeati1213 – 122196
Repeati1222 – 123097
Repeati1231 – 123998
Repeati1240 – 124899
Repeati1249 – 1257910
Repeati1258 – 1266911
Repeati1267 – 1275912
Repeati1276 – 1284913
Repeati1285 – 1293914
Repeati1294 – 1302915
Repeati1303 – 1311916
Repeati1312 – 1320917
Repeati1321 – 1329918
Repeati1330 – 1338919
Repeati1339 – 1347920
Repeati1348 – 1356921
Repeati1357 – 1365922
Repeati1366 – 1374923
Repeati1375 – 1383924
Repeati1384 – 1392925
Repeati1393 – 1401926
Repeati1402 – 1410927
Repeati1411 – 1419928
Repeati1420 – 1428929
Repeati1429 – 1437930
Repeati1438 – 1446931
Repeati1447 – 1455932
Repeati1456 – 1464933
Repeati1465 – 1473934
Repeati1474 – 1482935
Repeati1483 – 1491936
Repeati1492 – 1500937
Repeati1501 – 1509938
Repeati1510 – 1518939
Repeati1519 – 1527940
Repeati1531 – 1539941
Domaini1616 – 1941326F5/8 type A 3Add
BLAST
Domaini1616 – 1785170Plastocyanin-like 5Add
BLAST
Domaini1795 – 1941147Plastocyanin-like 6Add
BLAST
Domaini1941 – 2095155F5/8 type C 1PROSITE-ProRule annotationAdd
BLAST
Domaini2100 – 2255156F5/8 type C 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni691 – 1611921BAdd
BLAST
Regioni1168 – 153937241 X 9 AA approximate tandem repeats of T-L-S-P-D-L-[GS]-[HQ]-TAdd
BLAST

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.
SMRiQ9GLP1. Positions 1613-2257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000006704.

Proteomic databases

PaxDbiQ9GLP1.
PeptideAtlasiQ9GLP1.

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...

Publicationsi

  1. "Porcine factor V: cDNA cloning, gene mapping, three-dimensional protein modeling of membrane binding sites and comparative anatomy of domains."
    Grimm D.R., Colter M.B., Braunschweig M., Alexander L.J., Neame P.J., Kim H.K.W.
    Cell. Mol. Life Sci. 58:148-159(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING OF F5/8 TYPE A AND C DOMAINS.
    Tissue: Liver.

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: July 6, 2016
This is version 102 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.