|
|
|
Primary Information | |
|---|---|
| BoMiProt ID | Bomi4748 |
| Protein Name | Coagulation factor V/Activated protein C cofactor |
| Organism | Bos taurus |
| Uniprot ID | Q28107 |
| Milk Fraction | Whey |
| 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. |