[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0888-7543(90)90458-7; PubMed=2303254 [NCBI, ExPASy, EBI, Israel, Japan] Sarkar G., Koeberl D.D., Sommer S.S.; "Direct sequencing of the activation peptide and the catalytic domain of the factor IX gene in six species."; Genomics 6:133-143(1990).

Comments

FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide-linked.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Synthesized primarily in the liver and secreted in plasma.
DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain.
PTM: Activated by factor XIa, which excises the activation peptide.
SIMILARITY: Belongs to the peptidase S1 family [view classification].
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

M26247; AAA41162.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I84621; I84621.

UniGene

Rn.214249

3D structure databases

HSSP

P00740; 1RFN. [HSSP ENTRY / PDB]

SMR

P16296; 56-282.

ModBase

P16296.

Protein family/group databases

MEROPS

S01.214; -.

Organism-specific databases

RGD

2589; F9.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
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 UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000294; VitK_dep_GLA.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

P16296; -.

Phylogenomic databases

HOVERGEN

P16296; -.

Other

ProtoNet

P16296.

UniRef

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

Keywords

Blood coagulation; Calcium; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >282`	`>282`	`Coagulation factor IX.`	`PRO_0000088685`
`DOMAIN`	`56 >282`	`>227`	`Peptidase S1.`
`ACT_SITE`	`96 96`		`Charge relay system.`
`ACT_SITE`	`144 144`		`Charge relay system.`
`ACT_SITE`	`240 240`		`Charge relay system.`
`CARBOHYD`	`25 25`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`36 36`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`42 42`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`135 135`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`81 97`		`By similarity.`
`DISULFID`	`211 225`		`By similarity.`
`DISULFID`	`236 264`		`By similarity.`
`NON_TER`	`1 1`
`NON_TER`	`282 282`

Sequence information

Length: 282 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 31447 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 88B37B0A4673BEC9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
RVSVAYNSKK ITRAETVFSN TDYGNSTELI LDDITNSTIL DNLTENSEPI NDFTRVVGGE 

        70         80         90        100        110        120 
NAKPGQIPWQ VILNGEIEAF CGGAIINEKW IVTAAHCLKP GDKIEVVAGE HNIDEKEDTE 

       130        140        150        160        170        180 
QRRNVIRTIP HHQYNATINK YSHDIALLEL DKPLILNSYV TPICVANKEY TNIFLKFGSG 

       190        200        210        220        230        240 
YVSGWGKVFN KGRQASILQY LRVPLVDRAT CLRSTKFSIY NNMFCAGYRE GGKDSCEGDS 

       250        260        270        280 
GGPHVTEVEG TSFLTGIISW GEECAMKGKY GIYTKVSRYV NW

P16296 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