FA5_PIG
ID FA5_PIG Reviewed; 2258 AA.
AC Q9GLP1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Coagulation factor V;
DE AltName: Full=Activated protein C cofactor;
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING OF F5/8 TYPE A AND C
RP DOMAINS.
RC TISSUE=Liver;
RX PubMed=11229814; DOI=10.1007/pl00000775;
RA Grimm D.R., Colter M.B., Braunschweig M., Alexander L.J., Neame P.J.,
RA Kim H.K.W.;
RT "Porcine factor V: cDNA cloning, gene mapping, three-dimensional protein
RT modeling of membrane binding sites and comparative anatomy of domains.";
RL Cell. Mol. Life Sci. 58:148-159(2001).
CC -!- FUNCTION: Coagulation factor V is a cofactor that participates with
CC factor Xa to activate prothrombin to thrombin.
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC -!- SUBUNIT: Factor Va, the activated form of factor V, is composed of a
CC heavy chain and a light chain, non-covalently bound. The interaction
CC between the two chains is calcium-dependent. Forms heterodimer with
CC SERPINA5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: Domain B contains 41 X 9 AA tandem repeats. Domains C1 and C2
CC may be involved in membrane binding.
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 -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AF191308; AAG28381.1; -; mRNA.
DR RefSeq; NP_999285.1; NM_214120.1.
DR AlphaFoldDB; Q9GLP1; -.
DR SMR; Q9GLP1; -.
DR STRING; 9823.ENSSSCP00000006704; -.
DR PaxDb; Q9GLP1; -.
DR PeptideAtlas; Q9GLP1; -.
DR PRIDE; Q9GLP1; -.
DR GeneID; 397217; -.
DR KEGG; ssc:397217; -.
DR CTD; 2153; -.
DR eggNOG; ENOG502QSUG; Eukaryota.
DR InParanoid; Q9GLP1; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031091; C:platelet alpha granule; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008015; P:blood circulation; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR009271; Coagulation_factor_V_LSPD.
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; 2.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF06049; LSPR; 37.
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; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
PE 2: Evidence at transcript level;
KW Blood coagulation; Calcium; Copper; Disulfide bond; Glycoprotein;
KW Hemostasis; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal; Sulfation; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..2258
FT /note="Coagulation factor V"
FT /id="PRO_0000002982"
FT CHAIN 23..737
FT /note="Coagulation factor V heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002983"
FT PROPEP 738..1611
FT /note="Activation peptide (connecting region)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002984"
FT CHAIN 1612..2258
FT /note="Coagulation factor V light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002985"
FT DOMAIN 30..329
FT /note="F5/8 type A 1"
FT DOMAIN 30..193
FT /note="Plastocyanin-like 1"
FT DOMAIN 203..329
FT /note="Plastocyanin-like 2"
FT DOMAIN 348..683
FT /note="F5/8 type A 2"
FT DOMAIN 348..525
FT /note="Plastocyanin-like 3"
FT DOMAIN 535..683
FT /note="Plastocyanin-like 4"
FT REPEAT 1168..1176
FT /note="1"
FT REPEAT 1177..1185
FT /note="2"
FT REPEAT 1186..1194
FT /note="3"
FT REPEAT 1195..1203
FT /note="4"
FT REPEAT 1204..1212
FT /note="5"
FT REPEAT 1213..1221
FT /note="6"
FT REPEAT 1222..1230
FT /note="7"
FT REPEAT 1231..1239
FT /note="8"
FT REPEAT 1240..1248
FT /note="9"
FT REPEAT 1249..1257
FT /note="10"
FT REPEAT 1258..1266
FT /note="11"
FT REPEAT 1267..1275
FT /note="12"
FT REPEAT 1276..1284
FT /note="13"
FT REPEAT 1285..1293
FT /note="14"
FT REPEAT 1294..1302
FT /note="15"
FT REPEAT 1303..1311
FT /note="16"
FT REPEAT 1312..1320
FT /note="17"
FT REPEAT 1321..1329
FT /note="18"
FT REPEAT 1330..1338
FT /note="19"
FT REPEAT 1339..1347
FT /note="20"
FT REPEAT 1348..1356
FT /note="21"
FT REPEAT 1357..1365
FT /note="22"
FT REPEAT 1366..1374
FT /note="23"
FT REPEAT 1375..1383
FT /note="24"
FT REPEAT 1384..1392
FT /note="25"
FT REPEAT 1393..1401
FT /note="26"
FT REPEAT 1402..1410
FT /note="27"
FT REPEAT 1411..1419
FT /note="28"
FT REPEAT 1420..1428
FT /note="29"
FT REPEAT 1429..1437
FT /note="30"
FT REPEAT 1438..1446
FT /note="31"
FT REPEAT 1447..1455
FT /note="32"
FT REPEAT 1456..1464
FT /note="33"
FT REPEAT 1465..1473
FT /note="34"
FT REPEAT 1474..1482
FT /note="35"
FT REPEAT 1483..1491
FT /note="36"
FT REPEAT 1492..1500
FT /note="37"
FT REPEAT 1501..1509
FT /note="38"
FT REPEAT 1510..1518
FT /note="39"
FT REPEAT 1519..1527
FT /note="40"
FT REPEAT 1531..1539
FT /note="41"
FT DOMAIN 1616..1941
FT /note="F5/8 type A 3"
FT DOMAIN 1616..1785
FT /note="Plastocyanin-like 5"
FT DOMAIN 1795..1941
FT /note="Plastocyanin-like 6"
FT DOMAIN 1941..2095
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 2100..2255
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 691..1611
FT /note="B"
FT REGION 703..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1539
FT /note="41 X 9 AA approximate tandem repeats of T-L-S-P-D-L-
FT [GS]-[HQ]-T"
FT REGION 1252..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1877
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 1879
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 1919
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT SITE 737..738
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 1029..1030
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 1611..1612
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT MOD_RES 639
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12259"
FT MOD_RES 692
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 696
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 724
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 726
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 745
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1560
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1576
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1581
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1584
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1588
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1631
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1073
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1089
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2044
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 248..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 499..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 602..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 1759..1785
FT /evidence="ECO:0000305"
FT DISULFID 1941..2095
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 2100..2255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
SQ SEQUENCE 2258 AA; 256080 MW; 9159B9E0076A2ACC CRC64;
MFPALPCPWV LVVLGTSWAA WGNLGTEAAR VRQFYVAAQS ISWNYHPEPT HPSSSPFATS
FKKIVYREYE AYFQKEKPPS RMSGLLGPTL YADVGDIMKV HFRNKADKPL SIHPQGIKYS
KFAEGASYPD HTFLVEKMDD AVAPGQEYTY EWNISEDSGP THNDPPCLTH IYYSYENLIQ
DFNSGLIGPL LICKKGTLTE DGIQKMFDKQ YVLMFAVFDE SKSWNQSSSL MYTVNGYVNG
TMPDITVCAY DHISWHLIGM SSGPELFSIH FSGQVLEQNH HKVSAITLVS ATSTTANMTV
SPEGKWPISS LIPKHFQAGM QAYIDIKNCA KKTRKPKKLT RDQRRHIKRW EYFIAAEEVI
WDYAPIIPAN MDKKYRSLHL DNFSNQIGKH YKKVVYKQYQ DESFTKRLEN PNNKEDGILG
PVIRAQVRDT LKIVFKNMAS RSYSIYPHGV TFSPYEDDVN SSSTSDNNTM IRAVQPGETY
TYKWNILESD EPTENDAQCL TRPYYSNVDI TRDIASGLIG LLLICKSRSL DKRGIQRTAD
IEQKAVFAVF DENKSWYIED NIYKFCENPE KVKRDDPKFY ESNIMSTING YVPESIPTLG
FCFDDTVQWH FCSVRTHDNI LTIHFTGHSF IYGKRHEDTL TLFPMRGESV TVTMDNVGTW
MLTTMNSNPR NKKLQLKFRD VKCIRDDDED SYEIIYEPSS STTLTTRKMH DSSENKEEEN
DDEYDYQDLL ASVLGIRSFR NSSLYQEDDE FNLTALALEN NSEFIPPSTD RAVDSNSSSP
GNISRAPANT FTEPRKILPH PEATKAGSPR RHTGLVKNLV LNRRRTQHSD PYSEDPIENP
LQSVITGISL LPFGTEGFRN REHPKHKRFK AGRDQAAKHR FSQMEFPAHK TGRHISQDNS
SSSSMGPLED LSSDLLLLER KDPSTINGKW HLVSEKGSYE IVQDADEDMA VNKLPNNPQN
ASRSWGENIP FTNKHGKQRG HPIFVTRHKL LQERQDEGNS ILKKGRFFIR TRRKKKERKP
VHHVPLSPRS FNPLRGEANT PFSDRRQNHS LLLHESNETF PPTDLNQTFP SMNLSLIASH
PDHNQNLPND THQTSSPLDL YQTVTPDEPY QTAPIQDLDP THSTAVPSHQ SSLPEPIQMH
DYDLRNKASP TDVSEMFFSL KLKAGHRTTS PDLNQTSLSP ELSQTTLSPD PGHVTLSPDL
SQTTLSPDLS HTTLSPDLGH TTLSPDLSHT TLSPDLSQTT LSPDLSHTTL SPDLGHTTLS
PDLSHTTLSP DLGHATLSPD LSHTTLSPDL GHTTLSPDLG HTTLSPDFSQ TTLSPDLGHT
TLSSDVSHTT LSPDLSHTTL SPDLSHTTLS PDLGHTTLSP DLSQTTLSPD LGHMTLSPDL
SHTTLSPDLG HTTLSPDLSH TTLSPDLGHM TLSPDLGQTT LSLDFGQTTL SPDLSHMTLS
SELSHETLSP DLSQVTLSPD LSEIPFSPDL WQTTLSSDLN ETTLSPDLRQ TSPHPDPDKT
SYISESSQSV TLPEFGQTSP FPDLGQRPSP PSHSTLNNTF IPREFNPMVV VGLSRDDGDY
VEIIPRQQEE NSEEDYVKID YVEYDDPYQT DVRTDINSSR NPDNIAAWYL RSNNGNRRNY
YIAAEELSWD YSKFTQREDI DDVPEHTIYK KVVFRKYLDS TFTKLDPRGE YEEHLGILGP
IIRAEVDDVI QVRFKNLASR PYSLHAHGLS YEKSSEGKTY EDDSPEWFKE DNAVQPNSSY
TYVWHATERS GPESPGSACR AWAYYSAVNP EKDIHSGLIG PLLICRKGTL HKENNMPVDM
REFVLLFMVF DEKKSWYYEK KFTRSWRLTS SEVKNSHKFH AINGMIYNLP GLRMYEQEWV
RLHLLNLGGS RDIHVVHFHG QTLLENGTQQ HQLGVWPLLP GSFKTLEMKT SKAGWWLLDT
EVGENQRAGM QTPFLIIDRE CKMPMGLSTG LIADSQIKAS EFWGHWQPKL ARLNNGGSYN
AWITDKFSGE SNSKPWIQVD MQREVVFTGI QTQGAKYYLK SYYTTEFNVA YSSDQRNWRI
FKGNSTKNVM YFNGNSDAST ITENQFDPPV VARYIRISPT ESYNKPALRL ELQGCEVNGC
STPLGMESGN IKNEQITASS FKKSWWGDYW EPFRARLNAQ GRVNAWQAKA NNNNQWLQID
LLKIKKITAI TTQGCKSLSS EMYVKRYTIQ YSDRGVEWKS YREKSSMVDK IFEGNNNIKG
HVKNFFNPPI ISRFIRIIPK MWNQSIALRL ELFGCDIY
