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UniProtKB - P00741 (FA9_BOVIN)
Protein
Coagulation factor IX
Gene
F9
Organism
Bos taurus (Bovine)
Status
Functioni
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 Ca2+ ions, phospholipids, and factor VIIIa.
1 PublicationCatalytic activityi
- Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.1 Publication EC:3.4.21.22
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 47 | Calcium 1; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 48 | Calcium 2Combined sources1 Publication | 1 | |
Metal bindingi | 53 | Calcium 1; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 53 | Calcium 2; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 54 | Calcium 2; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 54 | Calcium 3; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 61 | Calcium 4; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 61 | Magnesium 1; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 63 | Calcium 1; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 63 | Calcium 2; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 63 | Calcium 3; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 66 | Calcium 4; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 66 | Magnesium 1; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 67 | Calcium 1; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 72 | Calcium 5; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 72 | Magnesium 2; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 73 | Calcium 2; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 73 | Calcium 3; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 76 | Calcium 3; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 76 | Calcium 5; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 76 | Magnesium 2; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 82 | Calcium 6; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 82 | Magnesium 3; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 86 | Calcium 6; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 86 | Magnesium 3; via 4-carboxyglutamateCombined sources1 Publication | 1 | |
Metal bindingi | 93 | Calcium 7By similarity | 1 | |
Metal bindingi | 94 | Calcium 7; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 96 | Calcium 7By similarity | 1 | |
Metal bindingi | 110 | Calcium 7By similarity | 1 | |
Metal bindingi | 111 | Calcium 7; via carbonyl oxygenBy similarity | 1 | |
Active sitei | 268 | Charge relay systemBy similarity | 1 | |
Metal bindingi | 282 | Calcium 8By similarity | 1 | |
Metal bindingi | 284 | Calcium 8; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 289 | Calcium 8By similarity | 1 | |
Metal bindingi | 292 | Calcium 8By similarity | 1 | |
Active sitei | 316 | Charge relay systemBy similarity | 1 | |
Active sitei | 412 | Charge relay systemBy similarity | 1 |
GO - Molecular functioni
- calcium ion binding Source: UniProtKB
- endopeptidase activity Source: UniProtKB
- magnesium ion binding Source: UniProtKB
- serine-type endopeptidase activity Source: UniProtKB-EC
GO - Biological processi
- blood coagulation Source: UniProtKB
- proteolysis Source: UniProtKB
- zymogen activation Source: UniProtKB
Keywordsi
Molecular function | Hydrolase, Protease, Serine protease |
Biological process | Blood coagulation, Hemostasis |
Ligand | Calcium, Magnesium, Metal-binding |
Enzyme and pathway databases
SABIO-RKi | P00741 |
Protein family/group databases
MEROPSi | S01.214 |
Names & Taxonomyi
Protein namesi | Recommended name: Coagulation factor IX (EC:3.4.21.22)Alternative name(s): Christmas factor Cleaved into the following 2 chains: |
Gene namesi | Name:F9 |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular space Source: UniProtKB
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 25 | Sequence analysisAdd BLAST | 25 | |
ChainiPRO_0000027741 | 26 – 462 | Coagulation factor IXAdd BLAST | 437 | |
PropeptideiPRO_0000433084 | 29 – 46 | By similarityAdd BLAST | 18 | |
ChainiPRO_0000027742 | 47 – 192 | Coagulation factor IXa light chainAdd BLAST | 146 | |
PropeptideiPRO_0000027743 | 193 – 227 | Activation peptideAdd BLAST | 35 | |
ChainiPRO_0000027744 | 228 – 462 | Coagulation factor IXa heavy chainAdd BLAST | 235 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 53 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Modified residuei | 54 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Modified residuei | 61 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Modified residuei | 63 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Disulfide bondi | 64 ↔ 69 | Combined sources1 Publication | ||
Modified residuei | 66 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Modified residuei | 67 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Modified residuei | 72 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Modified residuei | 73 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Modified residuei | 76 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Modified residuei | 79 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Modified residuei | 82 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Glycosylationi | 85 | O-linked (GalNAc...) threonineBy similarity | 1 | |
Modified residuei | 86 | 4-carboxyglutamatePROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Disulfide bondi | 97 ↔ 108 | By similarity | ||
GlycosylationiCAR_000008 | 99 | O-linked (Glc...) serine3 Publications | 1 | |
Disulfide bondi | 102 ↔ 117 | By similarity | ||
Modified residuei | 110 | (3R)-3-hydroxyaspartate1 Publication | 1 | |
Modified residuei | 114 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 119 ↔ 128 | By similarity | ||
Disulfide bondi | 134 ↔ 145 | By similarity | ||
Disulfide bondi | 141 ↔ 155 | By similarity | ||
Disulfide bondi | 157 ↔ 170 | By similarity | ||
Disulfide bondi | 178 ↔ 336 | Interchain (between light and heavy chains)By similarity | ||
Modified residuei | 202 | SulfotyrosineBy similarity | 1 | |
Glycosylationi | 204 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Modified residuei | 205 | PhosphoserineBy similarity | 1 | |
Glycosylationi | 214 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 219 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 253 ↔ 269 | By similarity | ||
Glycosylationi | 307 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 383 ↔ 397 | By similarity | ||
Disulfide bondi | 408 ↔ 436 | By similarity |
Post-translational modificationi
Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease.By similarity
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication
Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 192 – 193 | Cleavage; by factor XIa | 2 | |
Sitei | 227 – 228 | Cleavage; by factor XIa | 2 |
Keywords - PTMi
Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, ZymogenProteomic databases
PaxDbi | P00741 |
PTM databases
GlyConnecti | 97, 5 N-Linked glycans, 1 O-Linked glycan (1 site) |
iPTMneti | P00741 |
Expressioni
Tissue specificityi
Detected in blood plasma (at protein level) (PubMed:12695512).1 Publication
Gene expression databases
Bgeei | ENSBTAG00000004003, Expressed in liver and 17 other tissues |
Interactioni
Subunit structurei
Heterodimer of a light chain and a heavy chain; disulfide-linked,
Interacts with SERPINC1 (By similarity).
Interacts with the heterodimeric snake venom coagulation factor IX-binding protein (PubMed:12695512).
By similarity1 PublicationProtein-protein interaction databases
STRINGi | 9913.ENSBTAP00000005227 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P00741 |
SMRi | P00741 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P00741 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 47 – 92 | GlaPROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 93 – 129 | EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 130 – 171 | EGF-like 2PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 228 – 460 | Peptidase S1PROSITE-ProRule annotationAdd BLAST | 233 |
Domaini
Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain (PubMed:12695512). Calcium can also bind, with stronger affinity, to another site beyond the Gla domain (By similarity). Under physiological ion concentrations, Ca2+ is displaced by Mg2+ from some of the gammaglutamate residues in the N-terminal Gla domain. This leads to a subtle conformation change that may affect the interaction with its binding protein (PubMed:12695512).By similarity1 Publication
Sequence similaritiesi
Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Keywords - Domaini
EGF-like domain, SignalPhylogenomic databases
eggNOGi | ENOG502QUEV, Eukaryota |
InParanoidi | P00741 |
OrthoDBi | 1314811at2759 |
TreeFami | TF327329 |
Family and domain databases
CDDi | cd00190, Tryp_SPc, 1 hit |
Gene3Di | 2.40.10.10, 2 hits 4.10.740.10, 1 hit |
InterProi | View protein in InterPro IPR017857, Coagulation_fac-like_Gla_dom IPR035694, Coagulation_factor_IX IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR035972, GLA-like_dom_SF IPR000294, GLA_domain IPR012224, Pept_S1A_FX IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001314, Peptidase_S1A IPR001254, Trypsin_dom IPR018114, TRYPSIN_HIS IPR033116, TRYPSIN_SER |
PANTHERi | PTHR24278:SF31, PTHR24278:SF31, 1 hit |
Pfami | View protein in Pfam PF00008, EGF, 1 hit PF00594, Gla, 1 hit PF00089, Trypsin, 1 hit |
PIRSFi | PIRSF001143, Factor_X, 1 hit |
PRINTSi | PR00722, CHYMOTRYPSIN PR00001, GLABLOOD |
SMARTi | View protein in SMART SM00181, EGF, 2 hits SM00179, EGF_CA, 1 hit SM00069, GLA, 1 hit SM00020, Tryp_SPc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF57630, SSF57630, 1 hit |
PROSITEi | View protein in PROSITE PS00010, ASX_HYDROXYL, 1 hit PS00022, EGF_1, 1 hit PS01186, EGF_2, 2 hits PS50026, EGF_3, 1 hit PS01187, EGF_CA, 1 hit PS00011, GLA_1, 1 hit PS50998, GLA_2, 1 hit PS50240, TRYPSIN_DOM, 1 hit PS00134, TRYPSIN_HIS, 1 hit PS00135, TRYPSIN_SER, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P00741-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MWCLNMIMAE SPGLVTICLL GYLLSAECTV FLDRENATKI LHRPKRYNSG
60 70 80 90 100
KLEEFVRGNL ERECKEEKCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN
110 120 130 140 150
PCLNGGMCKD DINSYECWCQ AGFEGTNCEL DATCSIKNGR CKQFCKRDTD
160 170 180 190 200
NKVVCSCTDG YRLAEDQKSC EPAVPFPCGR VSVSHISKKL TRAETIFSNT
210 220 230 240 250
NYENSSEAEI IWDNVTQSNQ SFDEFSRVVG GEDAERGQFP WQVLLHGEIA
260 270 280 290 300
AFCGGSIVNE KWVVTAAHCI KPGVKITVVA GEHNTEKPEP TEQKRNVIRA
310 320 330 340 350
IPYHSYNASI NKYSHDIALL ELDEPLELNS YVTPICIADR DYTNIFLKFG
360 370 380 390 400
YGYVSGWGKV FNRGRSASIL QYLKVPLVDR ATCLRSTKFS IYSHMFCAGY
410 420 430 440 450
HEGGKDSCQG DSGGPHVTEV EGTSFLTGII SWGEECAMKG KYGIYTKVSR
460
YVNWIKEKTK LT
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 110 | D → T AA sequence (PubMed:291916).Curated | 1 | |
Sequence conflicti | 347 | L → S AA sequence (PubMed:291916).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DAAA02067809 Genomic DNA No translation available. DAAA02067810 Genomic DNA No translation available. J00007 mRNA Translation: AAA30520.1 |
PIRi | A14757, KFBO |
RefSeqi | XP_005227591.1, XM_005227534.3 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DAAA02067809 Genomic DNA No translation available. DAAA02067810 Genomic DNA No translation available. J00007 mRNA Translation: AAA30520.1 |
PIRi | A14757, KFBO |
RefSeqi | XP_005227591.1, XM_005227534.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1J34 | X-ray | 1.55 | C | 47-92 | [»] | |
1J35 | X-ray | 1.80 | C | 47-92 | [»] | |
AlphaFoldDBi | P00741 | |||||
SMRi | P00741 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 9913.ENSBTAP00000005227 |
Protein family/group databases
MEROPSi | S01.214 |
PTM databases
GlyConnecti | 97, 5 N-Linked glycans, 1 O-Linked glycan (1 site) |
iPTMneti | P00741 |
Proteomic databases
PaxDbi | P00741 |
Phylogenomic databases
eggNOGi | ENOG502QUEV, Eukaryota |
InParanoidi | P00741 |
OrthoDBi | 1314811at2759 |
TreeFami | TF327329 |
Enzyme and pathway databases
SABIO-RKi | P00741 |
Miscellaneous databases
EvolutionaryTracei | P00741 |
Gene expression databases
Bgeei | ENSBTAG00000004003, Expressed in liver and 17 other tissues |
Family and domain databases
CDDi | cd00190, Tryp_SPc, 1 hit |
Gene3Di | 2.40.10.10, 2 hits 4.10.740.10, 1 hit |
InterProi | View protein in InterPro IPR017857, Coagulation_fac-like_Gla_dom IPR035694, Coagulation_factor_IX IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR035972, GLA-like_dom_SF IPR000294, GLA_domain IPR012224, Pept_S1A_FX IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001314, Peptidase_S1A IPR001254, Trypsin_dom IPR018114, TRYPSIN_HIS IPR033116, TRYPSIN_SER |
PANTHERi | PTHR24278:SF31, PTHR24278:SF31, 1 hit |
Pfami | View protein in Pfam PF00008, EGF, 1 hit PF00594, Gla, 1 hit PF00089, Trypsin, 1 hit |
PIRSFi | PIRSF001143, Factor_X, 1 hit |
PRINTSi | PR00722, CHYMOTRYPSIN PR00001, GLABLOOD |
SMARTi | View protein in SMART SM00181, EGF, 2 hits SM00179, EGF_CA, 1 hit SM00069, GLA, 1 hit SM00020, Tryp_SPc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF57630, SSF57630, 1 hit |
PROSITEi | View protein in PROSITE PS00010, ASX_HYDROXYL, 1 hit PS00022, EGF_1, 1 hit PS01186, EGF_2, 2 hits PS50026, EGF_3, 1 hit PS01187, EGF_CA, 1 hit PS00011, GLA_1, 1 hit PS50998, GLA_2, 1 hit PS50240, TRYPSIN_DOM, 1 hit PS00134, TRYPSIN_HIS, 1 hit PS00135, TRYPSIN_SER, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | FA9_BOVIN | |
Accessioni | P00741Primary (citable) accession number: P00741 Secondary accession number(s): F1MFL4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | May 27, 2015 | |
Last modified: | May 25, 2022 | |
This is version 207 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families