FA10_TROCA
ID FA10_TROCA Reviewed; 483 AA.
AC Q4QXT9; A5X459;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Coagulation factor X;
DE EC=3.4.21.6;
DE Contains:
DE RecName: Full=Factor X light chain;
DE Contains:
DE RecName: Full=Factor X heavy chain;
DE Contains:
DE RecName: Full=Activated factor Xa heavy chain;
DE Flags: Precursor;
GN Name=F10; Synonyms=TrFX;
OS Tropidechis carinatus (Australian rough-scaled snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Notechinae; Tropidechis.
OX NCBI_TaxID=100989;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=15630489; DOI=10.1160/th04-07-0435;
RA Reza M.A., Swarup S., Kini R.M.;
RT "Two parallel prothrombin activator systems in Australian rough-scaled
RT snake, Tropidechis carinatus. Structural comparison of venom prothrombin
RT activator with blood coagulation factor X.";
RL Thromb. Haemost. 93:40-47(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver;
RX PubMed=17239167; DOI=10.1111/j.1538-7836.2006.02266.x;
RA Reza M.A., Swarup S., Kini R.M.;
RT "Structure of two genes encoding parallel prothrombin activators in
RT Tropidechis carinatus snake: gene duplication and recruitment of factor X
RT gene to the venom gland.";
RL J. Thromb. Haemost. 5:117-126(2007).
CC -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts
CC prothrombin to thrombin in the presence of factor Va, calcium and
CC phospholipid during blood clotting. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in
CC prothrombin to form thrombin.; EC=3.4.21.6;
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC -!- SUBUNIT: The two chains are formed from a single-chain precursor by the
CC excision of two Arg residues and are held together by 1 or more
CC disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
CC carboxylation. These residues are essential for the binding of calcium.
CC -!- PTM: The activation peptide is cleaved by factor IXa (in the intrinsic
CC pathway), or by factor VIIa (in the extrinsic pathway). {ECO:0000250}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Factor X entry;
CC URL="https://en.wikipedia.org/wiki/Factor_X";
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DR EMBL; AY651849; AAV65959.1; -; mRNA.
DR EMBL; DQ533831; ABG02403.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4QXT9; -.
DR SMR; Q4QXT9; -.
DR MEROPS; S01.396; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR GO; GO:0044469; P:envenomation resulting in positive regulation of blood coagulation in another organism; IEA:UniProt.
DR GO; GO:0035807; P:positive regulation of blood coagulation in another organism; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cleavage on pair of basic residues; Disulfide bond;
KW EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
KW Hydrolase; Hydroxylation; Protease; Prothrombin activator; Repeat;
KW Secreted; Serine protease; Signal; Toxin; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..40
FT /evidence="ECO:0000250"
FT /id="PRO_0000043201"
FT CHAIN 41..483
FT /note="Coagulation factor X"
FT /id="PRO_0000043202"
FT CHAIN 41..180
FT /note="Factor X light chain"
FT /id="PRO_0000043203"
FT CHAIN 183..483
FT /note="Factor X heavy chain"
FT /id="PRO_0000043204"
FT PROPEP 183..238
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043205"
FT CHAIN 239..483
FT /note="Activated factor Xa heavy chain"
FT /id="PRO_0000043206"
FT DOMAIN 41..86
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 86..122
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 125..165
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 239..470
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 422
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 54
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 56
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 75
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 103
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="O-linked (Hex...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..62
FT /evidence="ECO:0000250"
FT DISULFID 90..101
FT /evidence="ECO:0000250"
FT DISULFID 95..110
FT /evidence="ECO:0000250"
FT DISULFID 112..121
FT /evidence="ECO:0000250"
FT DISULFID 129..140
FT /evidence="ECO:0000250"
FT DISULFID 136..149
FT /evidence="ECO:0000250"
FT DISULFID 151..164
FT /evidence="ECO:0000250"
FT DISULFID 172..345
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00463"
FT DISULFID 245..250
FT /evidence="ECO:0000250"
FT DISULFID 265..281
FT /evidence="ECO:0000250"
FT DISULFID 393..407
FT /evidence="ECO:0000250"
FT DISULFID 418..446
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 53901 MW; F040EAC534BC960F CRC64;
MAPQLLLCLI LTFLWSLSEA ESNVFLKSKV ANRFLQRTKR ANSLFEEFKA GNIERECIEE
RCSKEEAREA FEDNEKTETF WNVYVDGDQC SSNPCHYGGT CKDGIGSYTC TCLAGYEGKN
CQYVLYQSCR VDNGNCWHFC KPVQNEIQCS CAESYLLGDD GYSCVAGGDF SCGRNIKARN
KREASLPDFQ TDFSDDYDAI DENNFVETPT NFSGLVPTVQ SQNATLLKKS DNPSPDIRVV
NGTDCKLGEC PWQALLINDQ GDGFCGGTIL SPIYVLTAAH CINQTKYIRV VVGEIDISRK
KTGRLLSVDK IYVHQKFVPS TYDYDIALIQ MKTPIQFSEN VVPACLPTAD FANQVLMKQD
FGIVSGFGRT RERGQTSNTL KVVTLPYVDR HTCMLSSNFP ITQNMFCAGY NTLPQDACQG
DSGGPHITAY RDTHFITGII SWGEGCAQTG KYGAYTKVSR FILWIKRIMR LKLPSTESST
GRL
