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O88783 (FA5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Coagulation factor V
Alternative name(s):
Activated protein C cofactor

Cleaved into the following 2 chains:

  1. Coagulation factor V heavy chain
  2. Coagulation factor V light chain
Gene names
Name:F5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length2183 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 regulation

Inhibited by SERPINA5 By similarity.

Subunit structure

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.

Subcellular location

Secreted By similarity.

Domain

Domain B contains 32 X 9 AA tandem repeats, and 1 X 17 AA repeats.

Post-translational modification

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) By similarity.

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.

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.

Sequence caution

The sequence BAE23393.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 21832164Coagulation factor V
PRO_0000358718
Chain20 – 736717Coagulation factor V heavy chain By similarity
PRO_0000358719
Propeptide737 – 1533797Activation peptide (connecting region) By similarity
PRO_0000358720
Chain1534 – 2183650Coagulation factor V light chain By similarity
PRO_0000358721

Regions

Domain30 – 328299F5/8 type A 1
Domain30 – 192163Plastocyanin-like 1
Domain202 – 328127Plastocyanin-like 2
Domain347 – 682336F5/8 type A 2
Domain347 – 524178Plastocyanin-like 3
Domain534 – 682149Plastocyanin-like 4
Repeat892 – 911201-1
Repeat1175 – 118392-1
Repeat1184 – 119292-2
Repeat1193 – 120192-3
Repeat1202 – 121092-4
Repeat1211 – 121992-5
Repeat1220 – 122892-6
Repeat1229 – 123792-7
Repeat1238 – 124692-8
Repeat1247 – 125592-9
Repeat1256 – 126492-10
Repeat1265 – 127392-11
Repeat1274 – 128292-12
Repeat1283 – 129192-13
Repeat1292 – 129982-14
Repeat1300 – 130892-15
Repeat1309 – 131682-16
Repeat1317 – 132592-17
Repeat1326 – 133492-18
Repeat1335 – 134172-19
Repeat1342 – 135092-20
Repeat1351 – 135992-21
Repeat1360 – 136892-22
Repeat1369 – 137792-23
Repeat1378 – 138692-24
Repeat1387 – 139592-25
Repeat1396 – 140492-26
Repeat1405 – 141392-27
Repeat1414 – 142292-28
Repeat1423 – 143192-29
Repeat1432 – 144092-30
Repeat1441 – 144992-31
Repeat1452 – 1461102-32
Domain1538 – 1866329F5/8 type A 3
Domain1538 – 1711174Plastocyanin-like 5
Domain1721 – 1866146Plastocyanin-like 6
Domain1866 – 2020155F5/8 type C 1
Domain2025 – 2180156F5/8 type C 2
Region691 – 1533843B By similarity
Region892 – 908171 X 17 AA tandem repeats
Region1175 – 146128732 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-T

Sites

Metal binding1381Calcium By similarity
Metal binding1391Calcium By similarity
Metal binding18021Copper By similarity
Metal binding18041Copper By similarity
Site333 – 3342Cleavage; by activated protein C By similarity
Site532 – 5332Cleavage; by activated protein C By similarity
Site706 – 7072Cleavage; by activated protein C By similarity
Site736 – 7372Cleavage; by thrombin By similarity
Site1004 – 10052Cleavage; by activated protein C By similarity
Site1029 – 10302Cleavage; by thrombin By similarity
Site1533 – 15342Cleavage; by thrombin By similarity

Amino acid modifications

Modified residue6381Phosphothreonine By similarity
Modified residue6921Sulfotyrosine Potential
Modified residue7251Sulfotyrosine Potential
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation8411N-linked (GlcNAc...) Ref.3
Glycosylation9591N-linked (GlcNAc...) Potential
Glycosylation9721N-linked (GlcNAc...) Potential
Glycosylation14381N-linked (GlcNAc...) Potential
Glycosylation18111N-linked (GlcNAc...) Potential
Disulfide bond1866 ↔ 2020 By similarity
Disulfide bond2025 ↔ 2180 By similarity

Experimental info

Mutagenesis3331R → Q: Does not affect pro-coagulant function. Partially resistant to inactivation by activated protein C. Ref.1
Mutagenesis5321R → Q: Does not affect pro-coagulant function. Partially resistant to inactivation by activated protein C. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O88783 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: BF0A8AA723F60317

FASTA2,183247,230
        10         20         30         40         50         60 
MLLVCPCFFL LVVLGTRWAG WGSHQAEAAQ LRQFYVAAQG ILWNYHPEPT DPSLNSIPSF 

        70         80         90        100        110        120 
KKIVYREYEQ YFKKEKPRSS NSGLLGPTLY AEVGDVIKVH FRNKADKPLS IHPQGIKYSK 

       130        140        150        160        170        180 
FSEGASYADH TFPAERKDDA VAPGEEYTYE WIVSEDSGPT PDDPPCLTHI YYSYENLTQD 

       190        200        210        220        230        240 
FNSGLIGPLL ICKKGTLTED GTQKMFDKQH VLLFAVFDES KSRSQSPSLM YTINGFVNKT 

       250        260        270        280        290        300 
MPDITVCAHD HVSWHLIGMS SGPELFSIHF NGQVLEQNQH KVSTVTLVSA TSTTANMTMS 

       310        320        330        340        350        360 
PEGRWIVSSL IPKHYQAGMQ AYIDIKNCPK KTRSPKTLTR EQRRYMKRWE YFIAAEEVIW 

       370        380        390        400        410        420 
NYAPVIPANM DKIYRSQHLD NFSNQIGKHY KKVIYRQYEE ETFTKRTDNP SIKQSGILGP 

       430        440        450        460        470        480 
VIRAQVRDTL KIVFKNMASR PYSIYPHGVT FSPYEDGINS SSTSGSHTTI RPVQPGETFT 

       490        500        510        520        530        540 
YKWNILEFDE PTENDAQCLT RPYYSDVDVT RDIASGLIGL LLICKSRSLD QRGVQRVADI 

       550        560        570        580        590        600 
EQQAVFAVFD ENKSWYIEDN INKFCENPDE VKRDDPKFYE SNIMSTINGY VPESISTLGF 

       610        620        630        640        650        660 
CFDDTVQWHF CSVGTHDDIL TIHFTGHSFI YGRRHEDTLT LFPMRGESVT VTMDNVGTWM 

       670        680        690        700        710        720 
LTTMNSNPKR RNLRLRFRDV KCNRDYDNED SYEIYEPPAP TSMTTRRIHD SLENEFGIDN 

       730        740        750        760        770        780 
EDDDYQYLLA SSLGIRSFKN SSLNPEENEF NLTALALENS SEFISPSTDR VVDSNSSRIL 

       790        800        810        820        830        840 
SKIINNNLKD FQRTLPGSGA TVAGTLLRNL IGLDENFVLN SSTEHRSSSY HENDMENPQS 

       850        860        870        880        890        900 
NITMVYLLPL GPKGSGNREQ DKPKTIKTGR PHMMKHRFSW MKAPAGKTGR HSNPKNSYSG 

       910        920        930        940        950        960 
MKSEEDIPSE LIPLKQKITS KFLNRRWRVA SEKGSYEIIA ANGEDTDVDK LTNSPQNQNI 

       970        980        990       1000       1010       1020 
TVPRGESTSH TNTTRKPSDL PTFSGVGHKS PHVRQEEENS GFQKRQLFIR TRKKKKNKKL 

      1030       1040       1050       1060       1070       1080 
ALHSPLSPRG FDPLRGHNHS PFPDRRLLNH SLLLHKSNET ALSPDLNQTS PSMSTDRSLP 

      1090       1100       1110       1120       1130       1140 
DYNQYSKNDT EQMSSSLDLY QSVPAEEHSP TFPAQDPDQT HSTTDPSYRS SPPELSQGLD 

      1150       1160       1170       1180       1190       1200 
YDLSHDFYPD DIGLTSFFPD QSQKSSFSSD DDQAIPSSDL SLFTISPELD QTIIYPDLDQ 

      1210       1220       1230       1240       1250       1260 
LLLSPEDNQK TSSPDLGQVP LSPDDNQKTS SPDLGQVSLS PDDNQKTSSP DLGQVPLSLD 

      1270       1280       1290       1300       1310       1320 
DNQKTTSPDL GQVPLSPDDN QMITSPDLGQ VPLSSDNQKT SSPDLGQVPL FPEDNQNYFL 

      1330       1340       1350       1360       1370       1380 
DLSQVPLSSD QNQETSSTDL LTLSPDFGQT VLSPDLDQLP LPSDNSQVTV SPDLSLLTLS 

      1390       1400       1410       1420       1430       1440 
PDFNEIILAP DLGQVTLSPD LIQTNPALNH GHKASSADPD QASYPPDSGQ ASSLPELNRT 

      1450       1460       1470       1480       1490       1500 
LPHPDLTHIP PPSPSPTLNN TSLSRKFNPL VVVGLSRVDG DDVEIVPSEE PERIDEDYAE 

      1510       1520       1530       1540       1550       1560 
DDFVTYNDPY RTDTRTDVNS SRNPDTIAAW YLRGHGGHKK FYYIAAEEIT WNYAEFAQSE 

      1570       1580       1590       1600       1610       1620 
MDHEDTGHTP KDTTYKKVVF RKYLDSTFTS RDPRAEYEEH LGILGPVIRA EVDDVIQVRF 

      1630       1640       1650       1660       1670       1680 
KNLASRPYSL HAHGLSYEKS SEGKTYEDES PEWFQEDDAV QPNSSYTYVW HATKRSGPEN 

      1690       1700       1710       1720       1730       1740 
PGSACRAWAY YSAVNVERDI HSGLIGPLLI CRKGTLHMER NLPMDMREFV LLFMVFDEKK 

      1750       1760       1770       1780       1790       1800 
SWYYEKSKGS RRIESPEEKN AHKFYAINGM IYNLPGLRMY EQEWVRLHLL NMGGSRDIHV 

      1810       1820       1830       1840       1850       1860 
VHFHGQTLLD NRTKQHQLGV WPLLPGSFKT LEMKASKPGW WLLDTEVGEN QVAGMQTPFL 

      1870       1880       1890       1900       1910       1920 
IIDKECKMPM GLSTGVISDS QIKASEYLTY WEPRLARLNN AGSYNAWSIE KTALDFPIKP 

      1930       1940       1950       1960       1970       1980 
WIQVDMQKEV VVTGIQTQGA KHYLKSCFTT EFQVAYSSDQ TNWQIFRGKS GKSVMYFTGN 

      1990       2000       2010       2020       2030       2040 
SDGSTIKENR LDPPIVARYI RIHPTKSYNR PTLRLELQGC EVNGCSTPLG LEDGRIQDKQ 

      2050       2060       2070       2080       2090       2100 
ITASSFKKSW WGDYWEPSLA RLNAQGRVNA WQAKANNNKQ WLQVDLLKIK KVTAIVTQGC 

      2110       2120       2130       2140       2150       2160 
KSLSSEMYVK SYSIQYSDQG VAWKPYRQKS SMVDKIFEGN SNTKGHMKNF FNPPIISRFI 

      2170       2180 
RIIPKTWNQS IALRLELFGC DIY

« Hide

References

« Hide 'large scale' references
[1]"The structure and function of murine factor V and its inactivation by protein C."
Yang T.L., Cui J., Rehumtulla A., Yang A., Moussalli M., Kaufman R.J., Ginsburg D.
Blood 91:4593-4599(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CLEAVAGE BY ACTIVATED PROTEIN C, MUTAGENESIS OF ARG-333 AND ARG-532.
Strain: C57BL/6J.
Tissue: Bone marrow.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1012.
Strain: C57BL/6J.
Tissue: Bone, Cerebellum and Olfactory bulb.
[3]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-841, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U52925 mRNA. Translation: AAC99553.1.
AK137521 mRNA. Translation: BAE23393.1. Different initiation.
AK139240 mRNA. Translation: BAE23928.1.
IPIIPI00406603.
PIRT42764.
RefSeqNP_032002.1. NM_007976.2.
UniGeneMm.12900.

3D structure databases

HSSPHSSP built from PDB template 1SDD based on UniProtKB Q28107.
ProteinModelPortalO88783.
SMRO88783. Positions 32-684, 1537-2183.
ModBaseSearch...

PTM databases

PhosphoSiteO88783.

Proteomic databases

PaxDbO88783.
PRIDEO88783.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086040; ENSMUSP00000083204; ENSMUSG00000026579.
GeneID14067.
KEGGmmu:14067.
UCSCuc007dic.1. mouse.

Organism-specific databases

CTD2153.
MGIMGI:88382. F5.

Phylogenomic databases

eggNOGNOG240444.
GeneTreeENSGT00550000074552.
HOGENOMHOG000082542.
HOVERGENHBG005631.
InParanoidQ3UV80.
KOK03902.
OMAPDLSHTT.
OrthoDBEOG41RPT3.

Gene expression databases

ArrayExpressO88783.
BgeeO88783.
GenevestigatorO88783.

Family and domain databases

Gene3D2.60.40.420. 6 hits.
InterProIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR009271. Coagulation_factor_V_LSPD.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamPF07732. Cu-oxidase_3. 3 hits.
PF00754. F5_F8_type_C. 2 hits.
PF06049. LSPR. 22 hits.
[Graphical view]
SMARTSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMSSF49503. Cupredoxin. 6 hits.
SSF49785. Gal_bind_like. 2 hits.
PROSITEPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSF5. mouse.
NextBio285052.
SOURCESearch...

Entry information

Entry nameFA5_MOUSE
AccessionPrimary (citable) accession number: O88783
Secondary accession number(s): Q3UTQ2, Q3UV80
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents