[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Chorioallantoic membrane; DOI=10.1016/0014-5793(91)80608-6; PubMed=2044767 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki H., Harada A., Hayashi Y., Wada K., Asaka J., Gotoh B., Ogasawara T., Nagai Y.; "Primary structure of the virus activating protease from chick embryo. Its identity with the blood clotting factor Xa."; FEBS Lett. 283:281-285(1991).
[2]	PROTEIN SEQUENCE OF 41-55 AND 241-261. TISSUE=Allantoic fluid; PubMed=2174359 [NCBI, ExPASy, EBI, Israel, Japan] Gotoh B., Ogasawara T., Toyoda T., Inocencio N.M., Hamaguchi M., Nagai Y.; "An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo."; EMBO J. 9:4189-4195(1990).

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. VAP cleaves the fusion proteins of Sendai virus, NDV, and influenza virus a at a specific single arginine-containing site, and plays a key role in the viral spreading in the allantoic sac.
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.
TISSUE SPECIFICITY: Liver and chorioallantoic membrane.
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
PTM: The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
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

D00844; BAA00724.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S15838; EXCH.

NP_990353.1; -.

3D structure databases

HSSP

P00742; 1HCG. [HSSP ENTRY / PDB]

ModBase

P25155.

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).

ProtoNet

P25155.

Genome annotation databases

GeneID

395876; -.

KEGG

gga:395876; -.

Phylogenomic databases

HOVERGEN

P25155; -.

Other

UniRef

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

Keywords

Blood coagulation; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; 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`		`PRO_0000027810`
`CHAIN`	`41 475`	`435`	`Coagulation factor X.`	`PRO_0000027811`
`CHAIN`	`41 180`	`140`	`Factor X light chain.`	`PRO_0000027812`
`CHAIN`	`186 475`	`290`	`Factor X heavy chain.`	`PRO_0000027813`
`PROPEP`	`186 240`	`55`	`Activation peptide.`	`PRO_0000027814`
`CHAIN`	`241 475`	`235`	`Activated factor Xa heavy chain.`	`PRO_0000027815`
`DOMAIN`	`41 85`	`45`	`Gla.`
`DOMAIN`	`86 122`	`37`	`EGF-like 1; calcium-binding (Potential).`
`DOMAIN`	`125 168`	`44`	`EGF-like 2.`
`DOMAIN`	`241 473`	`233`	`Peptidase S1.`
`ACT_SITE`	`282 282`		`Charge relay system (By similarity).`
`ACT_SITE`	`328 328`		`Charge relay system (By similarity).`
`ACT_SITE`	`425 425`		`Charge relay system (By similarity).`
`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`	`79 79`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`103 103`		`3-hydroxyaspartate (By similarity).`
`CARBOHYD`	`196 196`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`207 207`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`228 228`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`285 285`		`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`	`136 152`		`By similarity.`
`DISULFID`	`154 167`		`By similarity.`
`DISULFID`	`175 348`		`Interchain (between light and heavy chains) (By similarity).`
`DISULFID`	`247 252`		`By similarity.`
`DISULFID`	`267 283`		`By similarity.`
`DISULFID`	`396 410`		`By similarity.`
`DISULFID`	`421 449`		`By similarity.`

Sequence information

Length: 475 AA [This is the length of the unprocessed precursor]

Molecular weight: 53142 Da [This is the MW of the unprocessed precursor]

CRC64: 570BF84956C5C74D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGRLLLLLL CAALPDELRA EGGVFIKKES ADKFLERTKR ANSFLEEMKQ GNIERECNEE 

        70         80         90        100        110        120 
RCSKEEAREA FEDNEKTEEF WNIYVDGDQC SSNPCHYGGQ CKDGLGSYTC SCLDGYQGKN 

       130        140        150        160        170        180 
CEFVIPKYCK INNGDCEQFC SIKKSVQKDV VCSCTSGYEL AEDGKQCVSK VKYPCGKVLM 

       190        200        210        220        230        240 
KRIKRSVILP TNSNTNATSD QDVPSTNGSI LEEVFTTTTE SPTPPPRNGS SITDPNVDTR 

       250        260        270        280        290        300 
IVGGDECRPG ECPWQAVLIN EKGEEFCGGT ILNEDFILTA AHCINQSKEI KVVVGEVDRE 

       310        320        330        340        350        360 
KEEHSETTHT AEKIFVHSKY IAETYDNDIA LIKLKEPIQF SEYVVPACLP QADFANEVLM 

       370        380        390        400        410        420 
NQKSGMVSGF GREFEAGRLS KRLKVLEVPY VDRSTCKQST NFAITENMFC AGYETEQKDA 

       430        440        450        460        470 
CQGDSGGPHV TRYKDTYFVT GIVSWGEGCA RKGKYGVYTK LSRFLRWVRT VMRQK

P25155 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