FA5_PSETE
ID FA5_PSETE Reviewed; 1459 AA.
AC Q593B6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Coagulation factor V;
DE Contains:
DE RecName: Full=Coagulation factor V heavy chain;
DE Contains:
DE RecName: Full=Coagulation factor V light chain;
DE Flags: Precursor;
GN Name=F5;
OS Pseudonaja textilis (Eastern brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX NCBI_TaxID=8673;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=15735790; DOI=10.1160/th04-11-0707;
RA Minh Le T.N., Reza M.A., Swarup S., Kini R.M.;
RT "Gene duplication of coagulation factor V and origin of venom prothrombin
RT activator in Pseudonaja textilis snake.";
RL Thromb. Haemost. 93:420-429(2005).
CC -!- FUNCTION: Central regulator of hemostasis. It serves as a critical
CC cofactor for the prothrombinase activity of factor Xa that results in
CC the activation of prothrombin to thrombin (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of a light and a heavy chains; non-disulfide-
CC linked. The interaction between the two chains is calcium-dependent (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC {ECO:0000269|PubMed:15735790}.
CC -!- PTM: Thrombin activates factor V proteolytically to the active
CC cofactor, factor Va (formation of a heavy chain at the N-terminus and a
CC light chain at the C-terminus).
CC -!- PTM: Activated protein C inactivates factor V and factor Va by
CC proteolytic degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AY576416; AAT78356.1; -; mRNA.
DR PDB; 4BXW; X-ray; 2.71 A; F=693-710.
DR PDBsum; 4BXW; -.
DR AlphaFoldDB; Q593B6; -.
DR SMR; Q593B6; -.
DR Proteomes; UP000472273; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR024715; Factor_5/8-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 1.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; SSF49503; 6.
DR SUPFAM; SSF49785; SSF49785; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Calcium; Copper; Disulfide bond;
KW Glycoprotein; Hemostasis; Metal-binding; Phosphoprotein;
KW Prothrombin activator; Reference proteome; Repeat; Secreted; Signal; Toxin;
KW Zymogen.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..1459
FT /note="Coagulation factor V"
FT /id="PRO_0000409910"
FT CHAIN 31..771
FT /note="Coagulation factor V heavy chain"
FT /id="PRO_0000409911"
FT PROPEP 772..817
FT /note="Activation peptide (connecting region)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000409912"
FT CHAIN 818..1459
FT /note="Coagulation factor V light chain"
FT /id="PRO_0000409913"
FT DOMAIN 32..330
FT /note="F5/8 type A 1"
FT DOMAIN 32..196
FT /note="Plastocyanin-like 1"
FT DOMAIN 206..330
FT /note="Plastocyanin-like 2"
FT DOMAIN 351..685
FT /note="F5/8 type A 2"
FT DOMAIN 351..529
FT /note="Plastocyanin-like 3"
FT DOMAIN 539..685
FT /note="Plastocyanin-like 4"
FT DOMAIN 823..1142
FT /note="F5/8 type A 3"
FT DOMAIN 823..991
FT /note="Plastocyanin-like 5"
FT DOMAIN 1000..1142
FT /note="Plastocyanin-like 6"
FT DOMAIN 1146..1297
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 1302..1456
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 693..817
FT /note="B"
FT REGION 739..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 348..349
FT /note="Cleavage; by activated protein C"
FT /evidence="ECO:0000250"
FT SITE 377..378
FT /note="Cleavage; by FXa"
FT /evidence="ECO:0000250"
FT SITE 379..380
FT /note="Cleavage; by FXa"
FT /evidence="ECO:0000250"
FT SITE 537..538
FT /note="Cleavage; by activated protein C"
FT /evidence="ECO:0000250"
FT SITE 771..772
FT /note="Cleavage; by thrombin and FXa"
FT /evidence="ECO:0000250"
FT SITE 817..818
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 1034..1035
FT /note="Cleavage; by FXa"
FT /evidence="ECO:0000250"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 943
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 170..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 251..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 503..529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 965..991
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 1146..1297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 1302..1456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT STRAND 706..710
FT /evidence="ECO:0007829|PDB:4BXW"
SQ SEQUENCE 1459 AA; 166218 MW; 1EBA3AEF3C69CB3E CRC64;
MGRYSVSPVP KCLLLMFLGW SGLKYYEVNA AQLREYHIAA QLEDWDYNPQ PEELSRLSES
DLTFKKIVYR EYELDFKQEK PRDELSGLLG PTLRGEVGDI LIIYFKNFAT QPVSIHPQSA
VYNKWSEGSS YSDGTSDVER LDDAVPPGQS FKYVWNITAE IGPKKADPPC LTYAYYSHVN
MVRDFNSGLI GALLICKEGS LNANGSQKFF NREYVLMFSV FDESKNWYRK PSLQYTINGF
ANGTLPDVQA CAYDHISWHL IGMSSSPEIF SVHFNGQTLE QNHYKVSTIN LVGGASVTAN
MSVSRTGKWL ISSLVAKHLQ AGMYGYLNIK DCGNPDTLTR KLSFRELRRI MNWEYFIAAE
EITWDYAPEI PSSVDRRYKA QYLDNFSNFI GKKYKKAVFR QYKDSNFTKP TYAIWPKERG
ILGPVIRAKV RDTISIVFKN LASRPYSIYV HGVSVSKDAE GAIYPSDPKE NITHGKAVEP
GQVYTYKWTV LDTDEPTVKD SECITKLYHS AVDMTRDIAS GLIGPLLVCK HKALSVKGVQ
NKADVEQHAV FAVFDENKSW YLEDNIKKYC SNPSTVKKDD PKFYKSNVMY TLNGYASDRT
EVLGFHQSEV VEWHLTSVGT VDEIVPVHLS GHTFLSKGKH QDILNLFPMS GESATVTMDN
LGTWLLSSWG SCEMSNGMRL RFLDANYDDE DEGNEEEEED DGDIFADIFI PPEVVKKKEK
DPVNFVSDPE SDKIAKELGL LDDEDNQEES HNVQTEDDEE QLMIATMLGF RSFKGSVAEE
ELNLTALALE EDAHASDPRI DSNSARNPDD IAGRYLRTIN RGNKRRYYIA AEEVLWDYSP
IGKSQVRSRA AKTTFKKAIF RSYLDDTFQT PSTGGEYEKH LGILGPIIRA EVDDVIEVQF
RNLASRPYSL HAHGLLYEKS SEGRSYDDKS PELFKKDDAI MPNGTYTYVW QVPPRSGPTD
NTEKCKSWAY YSGVNPEKDI HSGLIGPILI CQKGMIDKYN RTIDIREFVL FFMVFDEEKS
WYFPKSDKST RAEKLIGVQS RHTFPAINGI PYQLQGLTMY KDENVHWHLL NMGGPKDIHV
VNFHGQTFTE EGREDNQLGV LPLLPGTFAS IKMKPSKIGT WLLETEVGEN QERGMQALFT
VIDKDCKLPM GLASGIIQDS QISASGHVGY WEPKLARLNN TGKYNAWSII KKEHEHPWIQ
IDLQRQVVIT GIQTQGAMQL LKHLYTVEYF FTYSKDGQNW ITFKGRHSET QMHFEGNSDG
TTVKENHIDP PIIARYIRLH PTKFHNRPTF RIELLGCEVE GCSVPLGMES GAIKNSEITA
SSYKKTWWSS WEPSLARLNL KGRTNAWQPK VNNKDQWLQI DLQHLTKITS IITQGATSMT
TSMYVKTFSI HYTDDNSTWK PYLDVRTSME KVFTGNINSD GHVKHFFKPP ILSRFIRIIP
KTWNQYIALR IELFGCEVF
