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Protein

Coagulation factor V

Gene

F5

Organism
Bos taurus (Bovine)
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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Calcium
Metal bindingi140 – 1401Calcium
Metal bindingi1830 – 18301Copper
Metal bindingi1832 – 18321Copper
Metal bindingi1872 – 18721Copper

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 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 – 2828Sequence analysisAdd
BLAST
Chaini29 – 22112183Coagulation factor VPRO_0000002974Add
BLAST
Chaini29 – 741713Coagulation factor V heavy chainBy similarityPRO_0000002975Add
BLAST
Propeptidei742 – 1564823Activation peptide (connecting region)By similarityPRO_0000002976Add
BLAST
Chaini1565 – 2211647Coagulation factor V light chainBy similarityPRO_0000002977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi167 ↔ 193
Glycosylationi225 – 2251N-linked (GlcNAc...)1 Publication
Glycosylationi239 – 2391N-linked (GlcNAc...)1 Publication
Disulfide bondi248 ↔ 329
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence analysis
Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence analysis
Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi499 ↔ 525
Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence analysis
Glycosylationi587 – 5871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi607 ↔ 688
Modified residuei644 – 6441PhosphothreonineBy similarity
Modified residuei697 – 6971SulfotyrosineSequence analysis
Modified residuei701 – 7011SulfotyrosineSequence analysis
Modified residuei730 – 7301SulfotyrosineSequence analysis
Glycosylationi745 – 7451N-linked (GlcNAc...)Sequence analysis
Glycosylationi756 – 7561N-linked (GlcNAc...)Sequence analysis
Glycosylationi774 – 7741N-linked (GlcNAc...)Sequence analysis
Glycosylationi780 – 7801N-linked (GlcNAc...)Sequence analysis
Glycosylationi902 – 9021N-linked (GlcNAc...)Sequence analysis
Glycosylationi952 – 9521N-linked (GlcNAc...)Sequence analysis
Glycosylationi964 – 9641N-linked (GlcNAc...)Sequence analysis
Glycosylationi1044 – 10441N-linked (GlcNAc...)Sequence analysis
Glycosylationi1053 – 10531N-linked (GlcNAc...)Sequence analysis
Glycosylationi1062 – 10621N-linked (GlcNAc...)Sequence analysis
Glycosylationi1071 – 10711N-linked (GlcNAc...)Sequence analysis
Glycosylationi1078 – 10781N-linked (GlcNAc...)Sequence analysis
Glycosylationi1094 – 10941N-linked (GlcNAc...)Sequence analysis
Glycosylationi1451 – 14511N-linked (GlcNAc...)Sequence analysis
Glycosylationi1490 – 14901N-linked (GlcNAc...)Sequence analysis
Modified residuei1513 – 15131SulfotyrosineSequence analysis
Modified residuei1529 – 15291SulfotyrosineSequence analysis
Modified residuei1537 – 15371SulfotyrosineSequence analysis
Modified residuei1541 – 15411SulfotyrosineSequence analysis
Glycosylationi1550 – 15501N-linked (GlcNAc...)Sequence analysis
Glycosylationi1690 – 16901N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1712 ↔ 1738Curated
Glycosylationi1839 – 18391N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1894 ↔ 2048
Glycosylationi1997 – 19971N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2053 ↔ 2208
Glycosylationi2196 – 21961N-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).
Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity.By similarity
Activated protein C inactivates factor V and factor Va by proteolytic degradation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei334 – 3352Cleavage; by activated protein CBy similarity
Sitei533 – 5342Cleavage; by activated protein CBy similarity
Sitei741 – 7422Cleavage; by thrombinBy similarity
Sitei1034 – 10352Cleavage; by thrombinBy similarity
Sitei1564 – 15652Cleavage; by thrombin

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

PRIDEiQ28107.

Miscellaneous databases

PMAP-CutDBQ28107.

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

Structurei

Secondary structure

1
2211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 437Combined sources
Beta strandi61 – 677Combined sources
Turni71 – 733Combined sources
Beta strandi90 – 934Combined sources
Beta strandi97 – 1048Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi113 – 1175Combined sources
Turni121 – 1233Combined sources
Helixi134 – 1374Combined sources
Beta strandi147 – 1537Combined sources
Helixi156 – 1583Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 1738Combined sources
Beta strandi176 – 1783Combined sources
Helixi179 – 1835Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi202 – 2076Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi262 – 2643Combined sources
Turni313 – 3153Combined sources
Helixi316 – 3183Combined sources
Beta strandi1570 – 158314Combined sources
Turni1584 – 15874Combined sources
Beta strandi1601 – 161212Combined sources
Helixi1626 – 16283Combined sources
Beta strandi1635 – 16384Combined sources
Beta strandi1642 – 16476Combined sources
Beta strandi1651 – 16533Combined sources
Beta strandi1658 – 16603Combined sources
Turni1701 – 17033Combined sources
Beta strandi1707 – 17093Combined sources
Beta strandi1711 – 17188Combined sources
Helixi1723 – 17275Combined sources
Turni1728 – 17303Combined sources
Beta strandi1732 – 17387Combined sources
Beta strandi1755 – 176410Combined sources
Helixi1765 – 17673Combined sources
Beta strandi1791 – 17955Combined sources
Beta strandi1798 – 18003Combined sources
Beta strandi1806 – 18083Combined sources
Beta strandi1812 – 18198Combined sources
Beta strandi1827 – 18315Combined sources
Beta strandi1836 – 18383Combined sources
Beta strandi1840 – 18423Combined sources
Beta strandi1844 – 18518Combined sources
Beta strandi1855 – 18628Combined sources
Beta strandi1865 – 18728Combined sources
Helixi1876 – 18794Combined sources
Turni1880 – 18823Combined sources
Beta strandi1884 – 18907Combined sources
Turni1900 – 19023Combined sources
Helixi1907 – 19093Combined sources
Beta strandi1910 – 19134Combined sources
Helixi1921 – 19233Combined sources
Beta strandi1930 – 19323Combined sources
Beta strandi1934 – 19363Combined sources
Beta strandi1950 – 196617Combined sources
Beta strandi1968 – 199023Combined sources
Beta strandi1999 – 20024Combined sources
Beta strandi2009 – 20135Combined sources
Beta strandi2015 – 203824Combined sources
Beta strandi2040 – 20489Combined sources
Turni2059 – 20613Combined sources
Beta strandi2062 – 20643Combined sources
Beta strandi2069 – 20724Combined sources
Turni2078 – 20803Combined sources
Helixi2085 – 20873Combined sources
Beta strandi2089 – 20913Combined sources
Beta strandi2094 – 20963Combined sources
Beta strandi2098 – 21003Combined sources
Beta strandi2110 – 212617Combined sources
Beta strandi2128 – 21303Combined sources
Beta strandi2133 – 21408Combined sources
Beta strandi2142 – 21498Combined sources
Beta strandi2169 – 21724Combined sources
Beta strandi2175 – 219016Combined sources
Beta strandi2194 – 21985Combined sources
Beta strandi2200 – 22089Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SDDX-ray2.80A29-334[»]
B1565-2211[»]
ProteinModelPortaliQ28107.
SMRiQ28107. Positions 1566-2210.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ28107.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 327298F5/8 type A 1Add
BLAST
Domaini30 – 193164Plastocyanin-like 1Add
BLAST
Domaini203 – 327125Plastocyanin-like 2Add
BLAST
Domaini348 – 686339F5/8 type A 2Add
BLAST
Domaini348 – 525178Plastocyanin-like 3Add
BLAST
Domaini535 – 686152Plastocyanin-like 4Add
BLAST
Repeati1124 – 1137141-1Add
BLAST
Repeati1138 – 1151141-2Add
BLAST
Repeati1188 – 119692-1
Repeati1197 – 120592-2
Repeati1206 – 121492-3
Repeati1215 – 122392-4
Repeati1224 – 123292-5
Repeati1233 – 124192-6
Repeati1242 – 125092-7
Repeati1251 – 125992-8
Repeati1260 – 126892-9
Repeati1269 – 127792-10
Repeati1278 – 128692-11
Repeati1287 – 129592-12
Repeati1296 – 130492-13
Repeati1305 – 131392-14
Repeati1314 – 132292-15
Repeati1323 – 133192-16
Repeati1332 – 134092-17
Repeati1341 – 134992-18
Repeati1350 – 135892-19
Repeati1359 – 136792-20
Repeati1368 – 137692-21
Repeati1377 – 138592-22
Repeati1386 – 139492-23
Repeati1395 – 140392-24
Repeati1404 – 141292-25
Repeati1413 – 142192-26
Repeati1422 – 143092-27
Repeati1431 – 143992-28
Repeati1440 – 144452-29; truncated
Repeati1445 – 145392-30
Domaini1569 – 1890322F5/8 type A 3Add
BLAST
Domaini1569 – 1738170Plastocyanin-like 5Add
BLAST
Domaini1748 – 1890143Plastocyanin-like 6Add
BLAST
Domaini1894 – 2048155F5/8 type C 1PROSITE-ProRule annotationAdd
BLAST
Domaini2053 – 2208156F5/8 type C 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni696 – 1564869BAdd
BLAST
Regioni1124 – 1151282 X 14 AA tandem repeatsAdd
BLAST
Regioni1188 – 145326630 X 9 AA approximate tandem repeats of [AS]-L-S-P-D-[LP]-[GS]-Q-[TE]Add
BLAST

Domaini

Domain B contains 29.5 X 9 AA tandem repeats, and 2 X 14 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

HOGENOMiHOG000082542.
HOVERGENiHBG005631.
InParanoidiQ28107.
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.
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.
PF06049. LSPR. 28 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.

Q28107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLACPGFWV LVVLGSSWAG WGNLGAEAAK LRQFYVAAQS IRWNYRPEST
60 70 80 90 100
HLSSKPFETS FKKIVYREYE AYFQKEKPQS RTSGLLGPTL YAEVGDIMKV
110 120 130 140 150
HFKNKAHKPL SIHAQGIKYS KFSEGASYSD HTLPMEKMDD AVAPGQEYTY
160 170 180 190 200
EWIISEHSGP THDDPPCLTH IYYSYVNLVE DFNSGLIGPL LICKKGTLTE
210 220 230 240 250
DGTQKMFEKQ HVLMFAVFDE SKSWNQTSSL MYTVNGYVNG TMPDITVCAH
260 270 280 290 300
DHISWHLIGM SSGPELFSIH FNGQVLEQNH HKISAITLVS ATSTTANMTV
310 320 330 340 350
SPEGRWTIAS LIPRHFQAGM QAYIDIKNCA KKTRNPKKLT RDQRRHIKRW
360 370 380 390 400
EYFIAAEEVI WDYAPIIPAN MDKKYRSLHL DNFSNRIGKH YKKVVYKQYQ
410 420 430 440 450
DDSFTKRLED PSSEGDGILG PIIRAQVRDT LKIVFKNMAS RSYSIYPHGV
460 470 480 490 500
TFSPYDNEVN SSSTSGSNTM IRAVRPGETY TYKWNILESD EPTENDAQCL
510 520 530 540 550
TRPYYSNVDI TRDLASGLIG LLLICKSRSL DRRGIQRAAD IEQQAVFAVF
560 570 580 590 600
DENKSWYIED NIYKFCENPE KVKRDDPKFY ESNIMSNFTL PAINGYVPES
610 620 630 640 650
IPILGFCFDD TVQWHFCSVG TQNDILTIHF TGHSFIYGKR HEDTLTLFPM
660 670 680 690 700
QGESVTVTMD NVGTWMLTTM NSNPRSKKLR LRFRDAKCIR NDDDDSYEII
710 720 730 740 750
YEPSGSTAMT TKKIHDSSEI EDENDADSDY QDELALILGL RSFRNSSLNQ
760 770 780 790 800
EKDELNLTAL ALEKDSEFIP PSANRSLDSN SSSRSHVSRL IAKNFAESLK
810 820 830 840 850
TLLHLEAPAA GSPLEHAGLD KNSALNPPMA EHSSPYSEDP REDHPLSDVT
860 870 880 890 900
GVSLLPFGTG FKNRKPAKHQ RFQVGRGQAA KHKFSQTRFP AHKTRTRLSQ
910 920 930 940 950
DNSSSSRMGP WEDIPSDLLL LQQKDPYKIL NGEWHLVSEK GSYEIIQDAN
960 970 980 990 1000
ENKTVNKLPN SPQNDSRTWG ENIPFKNSHG KQSGHPTFLV TRRKPLQDRQ
1010 1020 1030 1040 1050
DRRNSRLKEG LPLIRTRRKK KEEKPAYHVP LSPRSFHPLR GEVNASFSDR
1060 1070 1080 1090 1100
RHNHSLLLHA SNETSLSIDL NQTFPSMNLS LAASLPDHDQ TSPNDTTSQT
1110 1120 1130 1140 1150
SSPPDLYPTV SPEEHYQIFP IQDSDPTHST TAPSNRSPDP THSTTAPSNR
1160 1170 1180 1190 1200
SPPTQPSQIP NYDLRNRAIP TDVSQIFPSL ELEVWQTATS LDLSQPSISP
1210 1220 1230 1240 1250
DLGQMALSPD PGQESLSPDL GQTSLSPDLS QESLSPDLGQ TALSPDPSQE
1260 1270 1280 1290 1300
SLSPDLGQTA LSPDPSQESL SPDLGQTALS PDPGQESLSP DLGQTSLSPD
1310 1320 1330 1340 1350
LSQESLSPDL GQTALSPDPS QESLSPDLGQ TALSPDPSQE SLSPDLGQTS
1360 1370 1380 1390 1400
LSPDLGQESL SPDLGQTALS PDPSQESLSP DLGQTSLSPD LGQESLSPDL
1410 1420 1430 1440 1450
GQTALSPDLS QESLSPDLGQ TPLSPDLSLE SLSPDLSQLD LKQTSPPLDL
1460 1470 1480 1490 1500
NQTSHTSESS QSLPLPEFGQ TFPNADIGQM PSPPPDSTLN NTFIPEEFNP
1510 1520 1530 1540 1550
LVVVGLSRDD GDYIEIIPRQ KEESSEEDYG EFEFVAYNDP YQTDLRTDIN
1560 1570 1580 1590 1600
SSRNPDNIAA WYLRSNTGNR KYYYIAAEEI SWDYSKFVQS DDVDYVPEDT
1610 1620 1630 1640 1650
VYKKVVFRKY LDSTFTKLDP QGEYEEHLGI LGPVIRAEVD DVIQVRFKNL
1660 1670 1680 1690 1700
ASRPYSLHAH GLSYEKSSEG KTYEDDSPEW FKEDNAIQPN KTYTYVWHAT
1710 1720 1730 1740 1750
TRSGPENPGS ACRAWAYYSA VNPEKDIHSG LIGPLLICRK GTLDKETNMP
1760 1770 1780 1790 1800
VDMREFVLLF MVFDEKKSWY YDKKPTRSWR RASSEVKNSH EFHAINGMIY
1810 1820 1830 1840 1850
NLPGLRMYEQ EWVRLHLLNL GGSRDIHVVH FHGQTLLENG TQQHQLGVWP
1860 1870 1880 1890 1900
LLPGSFKTLE MKASKPGWWL LDTEVGEIQR AGMQTPFLIV DRECKMPMGL
1910 1920 1930 1940 1950
STGLIADSQI QASEFWGYWE PKLARLNNGG SYNAWIAEKL STEFNPEPWI
1960 1970 1980 1990 2000
QVDMQKEVLL TGIQTQGAKH YLKPYYTTEF CVAYSLDRKN WRIFKGNSTR
2010 2020 2030 2040 2050
NVMYFGGNSD ASTIKENQID PPVVARYIRI SPTGSYNKPA LRLELQGCEV
2060 2070 2080 2090 2100
NGCSTPLGME SGKIENKQIT ASSFKKSWWG NYWEPFLARL NAQGRVNAWQ
2110 2120 2130 2140 2150
AKANNNNQWL QIDLLKIKKI TAIVTQGCKS LSSEMYVKSY TIHYSDQGTD
2160 2170 2180 2190 2200
WKPYREKSSM VDKIFEGNNN VRGHVKNFFN PPIISRFIRI IPKTWNQSIA
2210
LRLELFGCDM Y
Length:2,211
Mass (Da):248,983
Last modified:November 1, 1996 - v1
Checksum:iCBBF90B738667C45
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti587 – 5926NFTLPA → T in variant 2.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81440 mRNA. Translation: AAA30512.1.
M81441 mRNA. Translation: AAA30513.1.
PIRiA42580. KFBO5.
RefSeqiNP_776304.1. NM_173879.2.
UniGeneiBt.23666.

Genome annotation databases

GeneIDi280687.
KEGGibta:280687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81440 mRNA. Translation: AAA30512.1.
M81441 mRNA. Translation: AAA30513.1.
PIRiA42580. KFBO5.
RefSeqiNP_776304.1. NM_173879.2.
UniGeneiBt.23666.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SDDX-ray2.80A29-334[»]
B1565-2211[»]
ProteinModelPortaliQ28107.
SMRiQ28107. Positions 1566-2210.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ28107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280687.
KEGGibta:280687.

Organism-specific databases

CTDi2153.

Phylogenomic databases

HOGENOMiHOG000082542.
HOVERGENiHBG005631.
InParanoidiQ28107.
KOiK03902.

Miscellaneous databases

EvolutionaryTraceiQ28107.
PMAP-CutDBQ28107.

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.
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.
PF06049. LSPR. 28 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...

Publicationsi

  1. "The complete cDNA sequence of bovine coagulation factor V."
    Guinto E.R., Esmon C.T., Mann K.G., Macgillivray R.T.
    J. Biol. Chem. 267:2971-2978(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Determination of the disulfide bridges in factor Va heavy chain."
    Xue J., Kalafatis M., Silveira J.R., Kung C., Mann K.G.
    Biochemistry 33:13109-13116(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  3. "The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function."
    Adams T.E., Hockin M.F., Mann K.G., Everse S.J.
    Proc. Natl. Acad. Sci. U.S.A. 101:8918-8923(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 29-2211, GLYCOSYLATION AT ASN-225 AND ASN-239, DISULFIDE BONDS, METAL-BINDING SITES.

Entry informationi

Entry nameiFA5_BOVIN
AccessioniPrimary (citable) accession number: Q28107
Secondary accession number(s): Q28108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 120 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

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.