(data stored in ACNUC19913 zone)

HOGENOM: HS13_PE1081

ID   HS13_PE1081                          STANDARD;      PRT;   488 AA.
AC   HS13_PE1081; P00742; Q14340;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Coagulation factor X; EC=3.4.21 6;AltName: Full=Stuart
DE   factor;AltName: Full=Stuart-Prower factor;Contains: RecName: Full=Factor
DE   X light chain;Contains: RecName: Full=Factor X heavy chain;Contains:
DE   RecName: Full=Activated factor Xa heavy chain;Flags: Precursor;
DE   (HS13.PE1081).
GN   Name=F10;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS13.PE1081.
CC       Homo sapiens chromosome 13 GRCh37  sequence 1..115109878 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA10_HUMAN
CC   -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that
CC       converts prothrombin to thrombin in the presence of factor Va,
CC       calcium and phospholipid during blood clotting.
CC   -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Thr and then
CC       Arg-|-Ile bonds in prothrombin to form thrombin.
CC   -!- SUBUNIT: The two chains are formed from a single-chain precursor
CC       by the excision of two Arg residues and are held together by 1 or
CC       more disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium.
CC   -!- PTM: N- and O-glycosylated.
CC   -!- PTM: The activation peptide is cleaved by factor IXa (in the
CC       intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC   -!- DISEASE: Defects in F10 are the cause of factor X deficiency
CC       (FA10D) [MIM:227600]. A hemorrhagic disease with variable
CC       presentation. Affected individuals can manifest prolonged nasal
CC       and mucosal hemorrhage, menorrhagia, hematuria, and occasionally
CC       hemarthrosis. Some patients do not have clinical bleeding
CC       diathesis.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Factor X entry;
CC       URL="http://en.wikipedia.org/wiki/Factor_X";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/f10/";
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000126218;ENST00000375559;ENSP00000364709.
DR   EMBL; AF503510; - ;
DR   EMBL; AK313798; - ;
DR   EMBL; AL137002; - ;
DR   EMBL; BC046125; - ;
DR   EMBL; CH471085; - ;
DR   EMBL; EF445049; - ;
DR   EMBL; K01886; - ;
DR   EMBL; K03194; - ;
DR   EMBL; L00390; - ;
DR   EMBL; L00391; - ;
DR   EMBL; L00392; - ;
DR   EMBL; L00393; - ;
DR   EMBL; L00394; - ;
DR   EMBL; L00395; - ;
DR   EMBL; L00396; - ;
DR   EMBL; M22613; - ;
DR   EMBL; M33297; - ;
DR   EMBL; M57285; - ;
DR   EMBL; N00045; - ;
DR   UniProtKB/Swiss-Prot; P00742; Q14340; -.
DR   EMBL; K03194; AAA52490.1; -; mRNA.
DR   EMBL; M57285; AAA52421.1; -; mRNA.
DR   EMBL; AF503510; AAM19347.1; -; Genomic_DNA.
DR   EMBL; BC046125; AAH46125.1; -; mRNA.
DR   EMBL; N00045; AAA52764.1; -; Genomic_DNA.
DR   EMBL; L00390; AAA52764.1; JOINED; Genomic_DNA.
DR   EMBL; L00391; AAA52764.1; JOINED; Genomic_DNA.
DR   EMBL; L00392; AAA52764.1; JOINED; Genomic_DNA.
DR   EMBL; L00393; AAA52764.1; JOINED; Genomic_DNA.
DR   EMBL; L00394; AAA52764.1; JOINED; Genomic_DNA.
DR   EMBL; L00395; AAA52764.1; JOINED; Genomic_DNA.
DR   EMBL; L00396; AAA52764.1; JOINED; Genomic_DNA.
DR   EMBL; M22613; AAA51984.1; -; mRNA.
DR   EMBL; K01886; AAA52486.1; -; mRNA.
DR   EMBL; M33297; AAA52636.1; -; Genomic_DNA.
DR   IPI; IPI00019576; -.
DR   PIR; A24478; EXHU.
DR   RefSeq; NP_000495.1; NM_000504.3.
DR   UniGene; Hs.361463; -.
DR   PDB; 1C5M; X-ray; 1.95 A; D=235-481, F=84-179.
DR   PDB; 1EZQ; X-ray; 2.20 A; A=235-488, B=46-179.
DR   PDB; 1F0R; X-ray; 2.10 A; A=235-488, B=46-179.
DR   PDB; 1F0S; X-ray; 2.10 A; A=235-488, B=46-179.
DR   PDB; 1FAX; X-ray; 3.00 A; A=235-481, L=84-179.
DR   PDB; 1FJS; X-ray; 1.92 A; A=235-468, L=127-178.
DR   PDB; 1FXY; X-ray; 2.15 A; A=-.
DR   PDB; 1G2L; X-ray; 1.90 A; A=235-469, B=86-179.
DR   PDB; 1G2M; X-ray; 3.02 A; A=235-469, B=86-179.
DR   PDB; 1HCG; X-ray; 2.20 A; A=235-475, B=129-179.
DR   PDB; 1IOE; X-ray; 2.90 A; A=235-469, L=84-179.
DR   PDB; 1IQE; X-ray; 2.90 A; A=235-469, L=84-179.
DR   PDB; 1IQF; X-ray; 3.20 A; A=235-469, L=84-179.
DR   PDB; 1IQG; X-ray; 2.60 A; A=235-469, L=84-179.
DR   PDB; 1IQH; X-ray; 3.00 A; A=235-469, L=84-179.
DR   PDB; 1IQI; X-ray; 2.90 A; A=235-469, L=84-179.
DR   PDB; 1IQJ; X-ray; 3.00 A; A=235-469, L=84-179.
DR   PDB; 1IQK; X-ray; 3.20 A; A=235-469, L=84-179.
DR   PDB; 1IQL; X-ray; 2.70 A; A=235-469, L=84-179.
DR   PDB; 1IQM; X-ray; 2.60 A; A=235-469, L=84-179.
DR   PDB; 1IQN; X-ray; 2.60 A; A=235-469, L=84-179.
DR   PDB; 1KSN; X-ray; 2.10 A; A=235-488, B=46-179.
DR   PDB; 1LPG; X-ray; 2.00 A; A=46-179, B=235-488.
DR   PDB; 1LPK; X-ray; 2.20 A; A=46-179, B=235-488.
DR   PDB; 1LPZ; X-ray; 2.40 A; A=46-179, B=235-488.
DR   PDB; 1LQD; X-ray; 2.70 A; A=46-179, B=235-488.
DR   PDB; 1MQ5; X-ray; 2.10 A; A=235-467, L=127-177.
DR   PDB; 1MQ6; X-ray; 2.10 A; A=235-467, L=127-177.
DR   PDB; 1MSX; Model; -; A=235-469.
DR   PDB; 1NFU; X-ray; 2.05 A; A=235-488, B=46-240.
DR   PDB; 1NFW; X-ray; 2.10 A; A=235-488, B=46-179.
DR   PDB; 1NFX; X-ray; 2.15 A; A=235-488, B=46-179.
DR   PDB; 1NFY; X-ray; 2.10 A; A=235-488, B=46-179.
DR   PDB; 1NL8; Model; -; F=235-469, L=41-179.
DR   PDB; 1P0S; X-ray; 2.80 A; H=235-488, L=41-178.
DR   PDB; 1V3X; X-ray; 2.20 A; A=235-467, B=127-178.
DR   PDB; 1WU1; X-ray; 2.30 A; A=235-467, B=85-179.
DR   PDB; 1XKA; X-ray; 2.30 A; C=235-469, L=85-179.
DR   PDB; 1XKB; X-ray; 2.40 A; A/B=85-179, C/D=235-469.
DR   PDB; 1Z6E; X-ray; 1.80 A; A=235-468, L=127-178.
DR   PDB; 2BMG; X-ray; 2.70 A; A=126-178, B=235-468.
DR   PDB; 2BOH; X-ray; 2.20 A; A=46-179, B=235-488.
DR   PDB; 2BOK; X-ray; 1.64 A; A=235-475, L=126-180.
DR   PDB; 2BQ6; X-ray; 3.00 A; A=126-177, B=220-468.
DR   PDB; 2BQ7; X-ray; 2.20 A; A=126-177, B=220-468.
DR   PDB; 2BQW; X-ray; 2.95 A; A=126-177, B=220-468.
DR   PDB; 2CJI; X-ray; 2.10 A; A=235-488, B=46-179.
DR   PDB; 2D1J; X-ray; 2.20 A; A=235-467, B=125-178.
DR   PDB; 2EI6; X-ray; 2.30 A; A=235-467, B=125-178.
DR   PDB; 2EI7; X-ray; 2.30 A; A=235-467, B=125-178.
DR   PDB; 2EI8; X-ray; 2.10 A; A=235-467, B=125-178.
DR   PDB; 2FZZ; X-ray; 2.20 A; A=235-468, L=127-178.
DR   PDB; 2G00; X-ray; 2.10 A; A=235-468, L=127-178.
DR   PDB; 2GD4; X-ray; 3.30 A; A/L=126-182, B/H=235-475.
DR   PDB; 2H9E; X-ray; 2.20 A; H=235-467, L=86-234.
DR   PDB; 2J2U; X-ray; 1.90 A; A=235-488, B=46-179.
DR   PDB; 2J34; X-ray; 2.01 A; A=235-488, B=46-179.
DR   PDB; 2J38; X-ray; 2.10 A; A=235-488, B=46-179.
DR   PDB; 2J4I; X-ray; 1.80 A; A=235-488, B=46-179.
DR   PDB; 2J94; X-ray; 2.10 A; A=235-488, B=46-179.
DR   PDB; 2J95; X-ray; 2.01 A; A=235-488, B=46-179.
DR   PDB; 2JKH; X-ray; 1.25 A; A=235-475, L=126-180.
DR   PDB; 2P16; X-ray; 2.30 A; A=235-468, L=127-178.
DR   PDB; 2P3F; X-ray; 3.10 A; H=235-469, L=125-178.
DR   PDB; 2P3T; X-ray; 1.92 A; A=127-178, B=235-467.
DR   PDB; 2P3U; X-ray; 1.62 A; A=127-178, B=235-467.
DR   PDB; 2P93; X-ray; 1.90 A; A=235-468, L=127-178.
DR   PDB; 2P94; X-ray; 1.80 A; A=235-468, L=127-178.
DR   PDB; 2P95; X-ray; 2.20 A; A=235-468, L=127-178.
DR   PDB; 2PHB; X-ray; 2.30 A; A=235-468, B=128-178.
DR   PDB; 2PR3; X-ray; 1.50 A; A=235-468, B=128-178.
DR   PDB; 2Q1J; X-ray; 1.90 A; A=235-468, B=128-178.
DR   PDB; 2RA0; X-ray; 2.30 A; A=235-468, L=129-178.
DR   PDB; 2UWL; X-ray; 1.90 A; A=235-488, B=46-179.
DR   PDB; 2UWO; X-ray; 1.75 A; A=235-488, B=46-179.
DR   PDB; 2UWP; X-ray; 1.75 A; A=235-488, B=46-179.
DR   PDB; 2VH0; X-ray; 1.70 A; A=235-488, B=46-179.
DR   PDB; 2VH6; X-ray; 1.95 A; A=235-488, B=46-177.
DR   PDB; 2VVC; X-ray; 1.95 A; A/B=235-475, K/L=126-180.
DR   PDB; 2VVU; X-ray; 2.30 A; A=235-475, L=126-180.
DR   PDB; 2VVV; X-ray; 1.73 A; A=235-475, L=126-180.
DR   PDB; 2VWL; X-ray; 1.80 A; A=235-475, L=126-180.
DR   PDB; 2VWM; X-ray; 1.96 A; A/B=235-475, K/L=126-180.
DR   PDB; 2VWN; X-ray; 1.61 A; A=235-475, L=126-180.
DR   PDB; 2VWO; X-ray; 1.60 A; A=235-475, L=126-180.
DR   PDB; 2W26; X-ray; 2.08 A; A=235-468, B=129-177.
DR   PDB; 2W3I; X-ray; 1.90 A; A=235-468, B=128-178.
DR   PDB; 2W3K; X-ray; 2.05 A; A=235-468, B=128-178.
DR   PDB; 2WYG; X-ray; 1.88 A; A=235-487, B=46-179.
DR   PDB; 2WYJ; X-ray; 2.38 A; A=235-488, B=47-179.
DR   PDB; 2XBV; X-ray; 1.66 A; A=235-475, L=126-180.
DR   PDB; 2XBW; X-ray; 1.72 A; A=235-475, L=126-180.
DR   PDB; 2XBX; X-ray; 1.85 A; A=235-475, L=126-180.
DR   PDB; 2XBY; X-ray; 2.02 A; A=235-475, L=126-180.
DR   PDB; 2XC0; X-ray; 2.05 A; A=235-475, L=126-180.
DR   PDB; 2XC4; X-ray; 1.67 A; A=235-475, L=126-180.
DR   PDB; 2XC5; X-ray; 1.70 A; A=235-475, L=126-180.
DR   PDB; 2Y7X; X-ray; 1.90 A; A=235-488, B=46-179.
DR   PDB; 2Y7Z; X-ray; 1.84 A; A=235-488, B=46-179.
DR   PDB; 2Y80; X-ray; 1.90 A; A=235-488, B=46-179.
DR   PDB; 2Y81; X-ray; 1.70 A; A=235-488, B=46-179.
DR   PDB; 2Y82; X-ray; 2.20 A; A=235-488, B=46-179.
DR   PDB; 3CEN; X-ray; 1.60 A; A=235-468, L=127-178.
DR   PDB; 3CS7; X-ray; 2.20 A; A=235-468, L=127-178.
DR   PDB; 3ENS; X-ray; 2.30 A; A/C=85-178, B/D=235-472.
DR   PDB; 3FFG; X-ray; 1.54 A; A=235-468, L=127-178.
DR   PDB; 3HPT; X-ray; 2.19 A; A/C=85-178, B/D=235-472.
DR   PDB; 3IIT; X-ray; 1.80 A; A=235-467, B=125-178.
DR   PDB; 3K9X; X-ray; 1.90 A; A/C=85-178, B/D=235-472.
DR   PDB; 3KL6; X-ray; 1.45 A; A=235-475, B=126-179.
DR   PDB; 3KQB; X-ray; 2.25 A; A=235-468, L=127-178.
DR   PDB; 3KQC; X-ray; 2.20 A; A=235-468, L=127-178.
DR   PDB; 3KQD; X-ray; 2.75 A; A=235-468, L=127-178.
DR   PDB; 3KQE; X-ray; 2.35 A; A=235-468, L=127-178.
DR   PDB; 3LIW; X-ray; 2.22 A; A=235-468, B=128-178.
DR   PDB; 3M36; X-ray; 2.15 A; A=235-468, L=127-178.
DR   PDB; 3M37; X-ray; 1.90 A; A=235-468, L=127-178.
DR   PDBsum; 1C5M; -.
DR   PDBsum; 1EZQ; -.
DR   PDBsum; 1F0R; -.
DR   PDBsum; 1F0S; -.
DR   PDBsum; 1FAX; -.
DR   PDBsum; 1FJS; -.
DR   PDBsum; 1FXY; -.
DR   PDBsum; 1G2L; -.
DR   PDBsum; 1G2M; -.
DR   PDBsum; 1HCG; -.
DR   PDBsum; 1IOE; -.
DR   PDBsum; 1IQE; -.
DR   PDBsum; 1IQF; -.
DR   PDBsum; 1IQG; -.
DR   PDBsum; 1IQH; -.
DR   PDBsum; 1IQI; -.
DR   PDBsum; 1IQJ; -.
DR   PDBsum; 1IQK; -.
DR   PDBsum; 1IQL; -.
DR   PDBsum; 1IQM; -.
DR   PDBsum; 1IQN; -.
DR   PDBsum; 1KSN; -.
DR   PDBsum; 1LPG; -.
DR   PDBsum; 1LPK; -.
DR   PDBsum; 1LPZ; -.
DR   PDBsum; 1LQD; -.
DR   PDBsum; 1MQ5; -.
DR   PDBsum; 1MQ6; -.
DR   PDBsum; 1MSX; -.
DR   PDBsum; 1NFU; -.
DR   PDBsum; 1NFW; -.
DR   PDBsum; 1NFX; -.
DR   PDBsum; 1NFY; -.
DR   PDBsum; 1NL8; -.
DR   PDBsum; 1P0S; -.
DR   PDBsum; 1V3X; -.
DR   PDBsum; 1WU1; -.
DR   PDBsum; 1XKA; -.
DR   PDBsum; 1XKB; -.
DR   PDBsum; 1Z6E; -.
DR   PDBsum; 2BMG; -.
DR   PDBsum; 2BOH; -.
DR   PDBsum; 2BOK; -.
DR   PDBsum; 2BQ6; -.
DR   PDBsum; 2BQ7; -.
DR   PDBsum; 2BQW; -.
DR   PDBsum; 2CJI; -.
DR   PDBsum; 2D1J; -.
DR   PDBsum; 2EI6; -.
DR   PDBsum; 2EI7; -.
DR   PDBsum; 2EI8; -.
DR   PDBsum; 2FZZ; -.
DR   PDBsum; 2G00; -.
DR   PDBsum; 2GD4; -.
DR   PDBsum; 2H9E; -.
DR   PDBsum; 2J2U; -.
DR   PDBsum; 2J34; -.
DR   PDBsum; 2J38; -.
DR   PDBsum; 2J4I; -.
DR   PDBsum; 2J94; -.
DR   PDBsum; 2J95; -.
DR   PDBsum; 2JKH; -.
DR   PDBsum; 2P16; -.
DR   PDBsum; 2P3F; -.
DR   PDBsum; 2P3T; -.
DR   PDBsum; 2P3U; -.
DR   PDBsum; 2P93; -.
DR   PDBsum; 2P94; -.
DR   PDBsum; 2P95; -.
DR   PDBsum; 2PHB; -.
DR   PDBsum; 2PR3; -.
DR   PDBsum; 2Q1J; -.
DR   PDBsum; 2RA0; -.
DR   PDBsum; 2UWL; -.
DR   PDBsum; 2UWO; -.
DR   PDBsum; 2UWP; -.
DR   PDBsum; 2VH0; -.
DR   PDBsum; 2VH6; -.
DR   PDBsum; 2VVC; -.
DR   PDBsum; 2VVU; -.
DR   PDBsum; 2VVV; -.
DR   PDBsum; 2VWL; -.
DR   PDBsum; 2VWM; -.
DR   PDBsum; 2VWN; -.
DR   PDBsum; 2VWO; -.
DR   PDBsum; 2W26; -.
DR   PDBsum; 2W3I; -.
DR   PDBsum; 2W3K; -.
DR   PDBsum; 2WYG; -.
DR   PDBsum; 2WYJ; -.
DR   PDBsum; 2XBV; -.
DR   PDBsum; 2XBW; -.
DR   PDBsum; 2XBX; -.
DR   PDBsum; 2XBY; -.
DR   PDBsum; 2XC0; -.
DR   PDBsum; 2XC4; -.
DR   PDBsum; 2XC5; -.
DR   PDBsum; 2Y7X; -.
DR   PDBsum; 2Y7Z; -.
DR   PDBsum; 2Y80; -.
DR   PDBsum; 2Y81; -.
DR   PDBsum; 2Y82; -.
DR   PDBsum; 3CEN; -.
DR   PDBsum; 3CS7; -.
DR   PDBsum; 3ENS; -.
DR   PDBsum; 3FFG; -.
DR   PDBsum; 3HPT; -.
DR   PDBsum; 3IIT; -.
DR   PDBsum; 3K9X; -.
DR   PDBsum; 3KL6; -.
DR   PDBsum; 3KQB; -.
DR   PDBsum; 3KQC; -.
DR   PDBsum; 3KQD; -.
DR   PDBsum; 3KQE; -.
DR   PDBsum; 3LIW; -.
DR   PDBsum; 3M36; -.
DR   PDBsum; 3M37; -.
DR   ProteinModelPortal; P00742; -.
DR   SMR; P00742; 43-467.
DR   DIP; DIP-29896N; -.
DR   IntAct; P00742; 6.
DR   MINT; MINT-276128; -.
DR   STRING; P00742; -.
DR   MEROPS; S01.216; -.
DR   GlycoSuiteDB; P00742; -.
DR   PRIDE; P00742; -.
DR   Ensembl; ENST00000375559; ENSP00000364709; ENSG00000126218.
DR   GeneID; 2159; -.
DR   KEGG; hsa:2159; -.
DR   UCSC; uc001vsx.1; human.
DR   CTD; 2159; -.
DR   GeneCards; GC13P094215; -.
DR   H-InvDB; HIX0026566; -.
DR   HGNC; HGNC:3528; F10.
DR   MIM; 227600; phenotype.
DR   MIM; 613872; gene.
DR   neXtProt; NX_P00742; -.
DR   Orphanet; 328; Congenital factor X deficiency.
DR   PharmGKB; PA27940; -.
DR   eggNOG; prNOG09450; -.
DR   InParanoid; P00742; -.
DR   OMA; PACLPQK; -.
DR   OrthoDB; EOG447FTB; -.
DR   PhylomeDB; P00742; -.
DR   BioCyc; MetaCyc:HS05000-MON; -.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   Reactome; REACT_604; Hemostasis.
DR   DrugBank; DB00009; Alteplase.
DR   DrugBank; DB00029; Anistreplase.
DR   DrugBank; DB00025; Antihemophilic Factor.
DR   DrugBank; DB00100; Coagulation Factor IX.
DR   DrugBank; DB00036; Coagulation factor VIIa.
DR   DrugBank; DB01225; Enoxaparin.
DR   DrugBank; DB01109; Heparin.
DR   DrugBank; DB00170; Menadione.
DR   DrugBank; DB00015; Reteplase.
DR   DrugBank; DB00031; Tenecteplase.
DR   NextBio; 8723; -.
DR   PMAP-CutDB; P00742; -.
DR   ArrayExpress; P00742; -.
DR   Bgee; P00742; -.
DR   CleanEx; HS_F10; -.
DR   Genevestigator; P00742; -.
DR   GermOnline; ENSG00000126218; Homo sapiens.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0007598; P:blood coagulation, extrinsic pathway; EXP:Reactome.
DR   GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
DR   GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
DR   GO; GO:0030335; P:positive regulation of cell migration; TAS:BHF-UCL.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling cascade; IDA:BHF-UCL.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; TAS:Reactome.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Gene3D; G3DSA:4.10.740.10; Coagulation_factor_Gla; 1.
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; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   SUPFAM; SSF57630; VitK_dep_GLA; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
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.
DR   HOGENOMDNA; HS13.PE1081; -.
KW   ENSG000001262181755old_1320000031; ENSP000003647097901old_1320000031;
KW   Q5JVE7_HUMAN; AF503510; AK313798; AL137002; BC046125; CH471085; EF445049;
KW   K03194; L00390; L00391; L00392; L00393; L00394; L00395; L00396; M22613;
KW   M57285; N00045;
KW   3D-structure; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase;
KW   Hydroxylation; Polymorphism; Protease; Reference proteome; Repeat;
KW   Secreted; Serine protease; Signal; Zymogen.
SQ   SEQUENCE   488 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK GHLERECMEE
     TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK CKDGLGEYTC TCLEGFEGKN
     CELFTRKLCS LDNGDCDQFC HEEQNSVVCS CARGYTLADN GKACIPTGPY PCGKQTLERR
     KRSVAQATSS SGEAPDSITW KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE
     CKDGECPWQA LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKVRVGD RNTEQEEGGE
     AVHEVEVVIK HNRFTKETYD FDIAVLRLKT PITFRMNVAP ACLPERDWAE STLMTQKTGI
     VSGFGRTHEK GRQSTRLKML EVPYVDRNSC KLSSSFIITQ NMFCAGYDTK QEDACQGDSG
     GPHVTRFKDT YFVTGIVSWG EGCARKGKYG IYTKVTAFLK WIDRSMKTRG LPKAKSHAPE
     VITSSPLK
//

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