[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/S0049-3848(97)00039-X; PubMed=9101642 [NCBI, ExPASy, EBI, Israel, Japan] Pendurthi U.R., Anderson K.D., James H.L.; "Characterization of a full-length cDNA for rabbit factor X."; Thromb. Res. 85:503-514(1997).

Comments

FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
SUBUNIT: The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds.
SUBCELLULAR LOCATION: Secreted (By similarity).
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium (By similarity).
PTM: N- and O-glycosylated (By similarity).
PTM: The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity).
MISCELLANEOUS: Calcium also binds, with stronger affinity to another site, beyond the GLA domain.
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 2 EGF-like domains.
SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF003200; AAB62542.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001075485.1; -.

UniGene

Ocu.2157

3D structure databases

HSSP

P00742; 1HCG. [HSSP ENTRY / PDB]

SMR

O19045; 233-473.

ModBase

O19045.

Protein family/group databases

MEROPS

S01.216; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002383; Coagulation_factor_Gla.
IPR006210; EGF.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR001438; EGF_2.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR012224; Pept_S1A_FX.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000294; VitK_dep_GLA.
Graphical view of domain structure.

Pfam

PF00008; EGF; 2.
PF00594; Gla; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001143; Factor_X; 1.

PRINTS

PR00722; CHYMOTRYPSIN.
PR00010; EGFBLOOD.
PR00001; GLABLOOD.

SMART

SM00181; EGF; 1.
SM00179; EGF_CA; 1.
SM00069; GLA; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00010; ASX_HYDROXYL; 1.
PS00022; EGF_1; 1.
PS01186; EGF_2; 2.
PS50026; EGF_3; 1.
PS01187; EGF_CA; 1.
PS00011; GLA_1; 1.
PS50998; GLA_2; 1.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

100008647; -.

Phylogenomic databases

HOVERGEN

O19045; -.

Other

ProtoNet

O19045.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Blood coagulation; Calcium; Cleavage on pair of basic residues; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`PROPEP`	`21 40`	`20`	`By similarity.`	`PRO_0000027798`
`CHAIN`	`41 490`	`450`	`Coagulation factor X.`	`PRO_0000027799`
`CHAIN`	`41 180`	`140`	`Factor X light chain.`	`PRO_0000027800`
`CHAIN`	`184 490`	`307`	`Factor X heavy chain.`	`PRO_0000027801`
`PROPEP`	`184 232`	`49`	`Activation peptide.`	`PRO_0000027802`
`CHAIN`	`233 490`	`258`	`Activated factor Xa heavy chain.`	`PRO_0000027803`
`DOMAIN`	`41 85`	`45`	`Gla.`
`DOMAIN`	`86 122`	`37`	`EGF-like 1; calcium-binding (Potential).`
`DOMAIN`	`125 165`	`41`	`EGF-like 2.`
`DOMAIN`	`233 465`	`233`	`Peptidase S1.`
`ACT_SITE`	`274 274`		`Charge relay system.`
`ACT_SITE`	`320 320`		`Charge relay system.`
`ACT_SITE`	`417 417`		`Charge relay system.`
`MOD_RES`	`46 46`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`47 47`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`54 54`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`56 56`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`59 59`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`60 60`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`65 65`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`66 66`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`69 69`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`72 72`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`75 75`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`79 79`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`103 103`		`3-hydroxyaspartate (By similarity).`
`CARBOHYD`	`61 61`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`187 187`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`205 205`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`57 62`		`By similarity.`
`DISULFID`	`90 101`		`By similarity.`
`DISULFID`	`95 110`		`By similarity.`
`DISULFID`	`112 121`		`By similarity.`
`DISULFID`	`129 140`		`By similarity.`
`DISULFID`	`136 149`		`By similarity.`
`DISULFID`	`151 164`		`By similarity.`
`DISULFID`	`172 340`		`Interchain (between light and heavy chains) (By similarity).`
`DISULFID`	`239 244`		`By similarity.`
`DISULFID`	`259 275`		`By similarity.`
`DISULFID`	`388 402`		`By similarity.`
`DISULFID`	`413 441`		`By similarity.`

Sequence information

Length: 490 AA [This is the length of the unprocessed precursor]

Molecular weight: 53965 Da [This is the MW of the unprocessed precursor]

CRC64: 3A39FA85AF2A6D11 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MANPLHLVLL GAALAGLLLS GSSVFISRRA ANDVLARTRR ANSFLEELKK GNLERECMEE 

        70         80         90        100        110        120 
NCSYEEALEV FEDREKTNEF WNKYVDGDQC ESNPCQNQGT CKDGLGMYTC SCVEGYEGQD 

       130        140        150        160        170        180 
CEPVTRKLCS LDNGGCDQFC KEEENSVLCS CASGYTLGDN GKSCISTELF PCGKVTLGRW 

       190        200        210        220        230        240 
RRSPATNSSE GPPEAPGPEQ QDDGNLTATE NPFNLLDSPE PPPEDDSSSL VRIVGGQDCR 

       250        260        270        280        290        300 
DGECPWQALL VNEENEGFCG GTILSEYHVL TAAHCLHQAK RFKVRVGDRD TEHEEGNEET 

       310        320        330        340        350        360 
HEVEVVVKHN RFVKETYDFD IAVLRLKTPI TFRRNVAPAC LPQKDWAEST LMAQKTGIVS 

       370        380        390        400        410        420 
GFGRTHEMGR LSTTLKMLEV PYVDRNSCKR SSSFTITQNM FCAGYDARPE DACQGDSGGP 

       430        440        450        460        470        480 
HVTRFRDTYF VTGIVSWGEG CARKGKFGVY TKVSNFLKWI EKSMRARAVP VAEAAGTPGP 

       490 
TQPTIKGSPS

O19045 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools