Search by BoMiProt ID - Bomi4748


Primary Information

BoMiProt ID Bomi4748
Protein Name Coagulation factor V/Activated protein C cofactor
Organism Bos taurus
Uniprot IDQ28107
Milk FractionWhey
Ref Sequence ID NP_776304.1
Aminoacid Length 2211
Molecular Weight 248983
FASTA Sequence Download
Gene Name F5
Gene ID 280687
Protein Existence Status reviewed

Secondary Information

Protein Function Coagulation Factor V (FV) takes part in this process as a component of the prothrombinase complex. Besides its role as procoagulant factor, it is also involved in the physiologic anticoagulant pathway, by participating in the inactivation of activated factor VIII (FVIIIa).
Biochemical Properties FV and FVIII share about 40% sequence identity in their A and C domains: moreover, the three A domains are homologous to the copper binding protein ceruloplasmin, while the two C domains belong to the lipid-binding discoidin-like protein family.
Significance in milk essential component in the blood coagulation cascade
PTMs N linked glycosylation at Asn
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q28107|FA5_BOVIN Coagulation factor V OS=Bos taurus OX=9913 GN=F5 PE=1 SV=1 MFLACPGFWVLVVLGSSWAGWGNLGAEAAKLRQFYVAAQSIRWNYRPESTHLSSKPFETS FKKIVYREYEAYFQKEKPQSRTSGLLGPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIKYS KFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEHSGPTHDDPPCLTHIYYSYVNLVE DFNSGLIGPLLICKKGTLTEDGTQKMFEKQHVLMFAVFDESKSWN*225QTSSLMYTVNGYVN*239G TMPDITVCAHDHISWHLIGMSSGPELFSIHFNGQVLEQNHHKISAITLVSATSTTAN*297MTV SPEGRWTIASLIPRHFQAGMQAYIDIKNCAKKTRNPKKLTRDQRRHIKRWEYFIAAEEVI WDYAPIIPANMDKKYRSLHLDN*382FSNRIGKHYKKVVYKQYQDDSFTKRLEDPSSEGDGILG PIIRAQVRDTLKIVFKNMASRSYSIYPHGVTFSPYDNEVN*460SSSTSGSNTMIRAVRPGETY TYKWNILESDEPTENDAQCLTRPYYSNVDITRDLASGLIGLLLICKSRSLDRRGIQRAAD IEQQAVFAVFDEN*553KSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSN*587FTLPAINGYVPES IPILGFCFDDTVQWHFCSVGTQNDILTIHFTGHSFIYGKRHEDT*644LTLFPMQGESVTVTMD NVGTWMLTTMNSNPRSKKLRLRFRDAKCIRNDDDDSYEIIYEPSGSTAMTTKKIHDSSEI EDENDADSDYQDELALILGLRSFRN*745SSLNQEKDELN*756LTALALEKDSEFIPPSAN*774RSLDSN*780SSSRSHVSRLIAKNFAESLKTLLHLEAPAAGSPLEHAGLDKNSALNPPMAEHSSPYSEDP REDHPLSDVTGVSLLPFGTGFKNRKPAKHQRFQVGRGQAAKHKFSQTRFPAHKTRTRLSQ DN*902SSSSRMGPWEDIPSDLLLLQQKDPYKILNGEWHLVSEKGSYEIIQDANEN*952KTVNKLPN SPQN*964DSRTWGENIPFKNSHGKQSGHPTFLVTRRKPLQDRQDRRNSRLKEGLPLIRTRRKK KEEKPAYHVPLSPRSFHPLRGEVN*1044ASFSDRRHN*1053HSLLLHASN*1062ETSLSIDLN*1071QTFPSMN*1078LSLAASLPDHDQTSPN*1094DTTSQTSSPPDLYPTVSPEEHYQIFPIQDSDPTHSTTAPSNRSPDP THSTTAPSNRSPPTQPSQIPNYDLRNRAIPTDVSQIFPSLELEVWQTATSLDLSQPSISP DLGQMALSPDPGQESLSPDLGQTSLSPDLSQESLSPDLGQTALSPDPSQESLSPDLGQTA LSPDPSQESLSPDLGQTALSPDPGQESLSPDLGQTSLSPDLSQESLSPDLGQTALSPDPS QESLSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQESLSPDLGQTALSPDPSQESLSP DLGQTSLSPDLGQESLSPDLGQTALSPDLSQESLSPDLGQTPLSPDLSLESLSPDLSQLD LKQTSPPLDLN*1451QTSHTSESSQSLPLPEFGQTFPNADIGQMPSPPPDSTLN*1490NTFIPEEFNP LVVVGLSRDDGDYIEIIPRQKEESSEEDYGEFEFVAYNDPYQTDLRTDIN*1550SSRNPDNIAA WYLRSNTGNRKYYYIAAEEISWDYSKFVQSDDVDYVPEDTVYKKVVFRKYLDSTFTKLDP QGEYEEHLGILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEW FKEDNAIQPN*1690KTYTYVWHATTRSGPENPGSACRAWAYYSAVNPEKDIHSGLIGPLLICRK GTLDKETNMPVDMREFVLLFMVFDEKKSWYYDKKPTRSWRRASSEVKNSHEFHAINGMIY NLPGLRMYEQEWVRLHLLNLGGSRDIHVVHFHGQTLLEN*1839GTQQHQLGVWPLLPGSFKTLE MKASKPGWWLLDTEVGEIQRAGMQTPFLIVDRECKMPMGLSTGLIADSQIQASEFWGYWE PKLARLNNGGSYNAWIAEKLSTEFNPEPWIQVDMQKEVLLTGIQTQGAKHYLKPYYTTEF CVAYSLDRKNWRIFKGN*1997STRNVMYFGGNSDASTIKENQIDPPVVARYIRISPTGSYNKPA LRLELQGCEVNGCSTPLGMESGKIENKQITASSFKKSWWGNYWEPFLARLNAQGRVNAWQ AKANNNNQWLQIDLLKIKKITAIVTQGCKSLSSEMYVKSYTIHYSDQGTDWKPYREKSSM VDKIFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWN*2196QSIALRLELFGCDMY
SCOP Class : All beta proteins
Fold : Cupredoxin-like
Superfamily : Cupredoxins
Family : Multidomain cupredoxins
Domain Name : 1SDD A:1-180

Class : All beta proteins
Fold : Galactose-binding domain-like
Superfamily : galactose-binding domain-like
Family : Discoidin domain (fa58c, coagulation factor 5/8 c-terminal domain)
Domain Name : 1SDD B:1863-2024

CATH Matched CATH superfamily
2.60.120.260
2.60.40.420
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction no TM helices
Significance of PTMs  FV1-FV2 heterogeneity is caused by differential glycosylation of Asn(2181) related to the presence of a Ser rather than a Thr at the third position in the consensus sequence of glycosylation.
PDB ID 1SDD,
Bibliography 1.Duga S, Asselta R, Tenchini ML. Coagulation factor V. Int J Biochem Cell Biol. 2004 Aug;36(8):1393-9. doi: 10.1016/j.biocel.2003.08.002. PMID: 15147718. 2.Nicolaes GA, Villoutreix BO, Dahlbäck B. Partial glycosylation of Asn2181 in human factor V as a cause of molecular and functional heterogeneity. Modulation of glycosylation efficiency by mutagenesis of the consensus sequence for N-linked glycosylation. Biochemistry. 1999 Oct 12;38(41):13584-91. doi: 10.1021/bi991165r. PMID: 10521265.