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UniProtKB - P19540 (FA9_CANLF)
Protein
Coagulation factor IX
Gene
F9
Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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.
By similarity2 PublicationsCatalytic activityi
- Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.By similarity EC:3.4.21.22
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 40 | Calcium 1; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 41 | Calcium 2By similarity | 1 | |
Metal bindingi | 46 | Calcium 1; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 46 | Calcium 2; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 47 | Calcium 2; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 47 | Calcium 3; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 54 | Calcium 4; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 54 | Magnesium 1; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 56 | Calcium 1; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 56 | Calcium 2; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 56 | Calcium 3; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 59 | Calcium 4; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 59 | Magnesium 1; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 60 | Calcium 1; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 65 | Calcium 5; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 65 | Magnesium 2; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 66 | Calcium 2; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 66 | Calcium 3; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 69 | Calcium 3; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 69 | Calcium 5; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 69 | Magnesium 2; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 75 | Calcium 6; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 75 | Magnesium 3; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 79 | Calcium 6; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 79 | Magnesium 3; via 4-carboxyglutamateBy similarity | 1 | |
Metal bindingi | 86 | Calcium 7By similarity | 1 | |
Metal bindingi | 87 | Calcium 7; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 89 | Calcium 7By similarity | 1 | |
Metal bindingi | 103 | Calcium 7By similarity | 1 | |
Metal bindingi | 104 | Calcium 7; via carbonyl oxygenBy similarity | 1 | |
Active sitei | 258 | Charge relay systemBy similarity | 1 | |
Metal bindingi | 272 | Calcium 8By similarity | 1 | |
Metal bindingi | 274 | Calcium 8; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 279 | Calcium 8By similarity | 1 | |
Metal bindingi | 282 | Calcium 8By similarity | 1 | |
Active sitei | 306 | Charge relay systemBy similarity | 1 | |
Active sitei | 402 | Charge relay systemBy similarity | 1 |
GO - Molecular functioni
- calcium ion binding Source: UniProtKB
- endopeptidase activity 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 |
Protein family/group databases
MEROPSi | S01.214 |
Names & Taxonomyi
Protein namesi | Recommended name: Coagulation factor IX (EC:3.4.21.22By similarity)Alternative name(s): Christmas factor Cleaved into the following 2 chains: |
Gene namesi | Name:F9 |
Organismi | Canis lupus familiaris (Dog) (Canis familiaris) |
Taxonomic identifieri | 9615 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular space Source: UniProtKB
Keywords - Cellular componenti
SecretedPathology & Biotechi
Involvement in diseasei
Defects in F9 are the cause of hemophilia B (HEMB).1 Publication
Keywords - Diseasei
Disease variant, HemophiliaPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | Sequence analysisAdd BLAST | 21 | |
PropeptideiPRO_0000027745 | 22 – 39 | By similarityAdd BLAST | 18 | |
ChainiPRO_0000027746 | 40 – 452 | Coagulation factor IXAdd BLAST | 413 | |
ChainiPRO_0000027747 | 40 – 185 | Coagulation factor IXa light chainAdd BLAST | 146 | |
PropeptideiPRO_0000027748 | 186 – 217 | Activation peptideAdd BLAST | 32 | |
ChainiPRO_0000027749 | 218 – 452 | Coagulation factor IXa heavy chainAdd BLAST | 235 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 46 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 47 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 54 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 56 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Disulfide bondi | 57 ↔ 62 | By similarity | ||
Modified residuei | 59 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 60 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 65 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 66 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 69 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 72 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 75 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Glycosylationi | 78 | O-linked (GalNAc...) threonineBy similarity | 1 | |
Modified residuei | 79 | 4-carboxyglutamatePROSITE-ProRule annotationBy similarity | 1 | |
Disulfide bondi | 90 ↔ 101 | By similarity | ||
Glycosylationi | 92 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 95 ↔ 110 | By similarity | ||
Modified residuei | 103 | (3R)-3-hydroxyaspartateBy similarity | 1 | |
Modified residuei | 107 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 112 ↔ 121 | By similarity | ||
Disulfide bondi | 127 ↔ 138 | By similarity | ||
Disulfide bondi | 134 ↔ 148 | By similarity | ||
Disulfide bondi | 150 ↔ 163 | By similarity | ||
Disulfide bondi | 171 ↔ 326 | Interchain (between light and heavy chains)By similarity | ||
Modified residuei | 195 | SulfotyrosineBy similarity | 1 | |
Glycosylationi | 197 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 198 | PhosphoserineBy similarity | 1 | |
Modified residuei | 199 | Phosphothreonine; alternateBy similarity | 1 | |
Glycosylationi | 199 | O-linked (GalNAc...) threonine; alternateBy similarity | 1 | |
Glycosylationi | 207 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 209 | O-linked (GalNAc...) threonineBy similarity | 1 | |
Glycosylationi | 216 | O-linked (GalNAc...) threonineBy similarity | 1 | |
Disulfide bondi | 243 ↔ 259 | By similarity | ||
Glycosylationi | 297 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 373 ↔ 387 | By similarity | ||
Disulfide bondi | 398 ↔ 426 | 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.By similarity
Predominantly O-glucosylated at Ser-92 by POGLUT1 in vitro.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 185 – 186 | Cleavage; by factor XIaBy similarity | 2 | |
Sitei | 217 – 218 | Cleavage; by factor XIaBy similarity | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, ZymogenProteomic databases
PaxDbi | P19540 |
Expressioni
Tissue specificityi
Detected in the liver.1 Publication
Interactioni
Subunit structurei
Heterodimer of a light chain and a heavy chain; disulfide-linked.
Interacts with SERPINC1.
By similarityProtein-protein interaction databases
STRINGi | 9612.ENSCAFP00000028031 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 40 – 85 | GlaPROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 86 – 122 | EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 123 – 164 | EGF-like 2PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 218 – 450 | Peptidase S1PROSITE-ProRule annotationAdd BLAST | 233 |
Domaini
Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain. 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.By similarity
Sequence similaritiesi
Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Keywords - Domaini
EGF-like domain, Repeat, SignalPhylogenomic databases
eggNOGi | ENOG502QUEV, Eukaryota |
InParanoidi | P19540 |
OrthoDBi | 1314811at2759 |
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
P19540-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAEASGLVTV CLLGYLLSAE CAVFLDRENA TKILSRPKRY NSGKLEEFVR
60 70 80 90 100
GNLERECIEE KCSFEEAREV FENTEKTTEF WKQYVDGDQC ESNPCLNDGV
110 120 130 140 150
CKDDINSYEC WCRAGFEGKN CELDVTCNIK NGRCKQFCKL GPDNKVVCSC
160 170 180 190 200
TTGYQLAEDQ RSCEPAVPFP CGRVSVPHIS MTRTRAETLF SNMDYENSTE
210 220 230 240 250
VEKILDNVTQ PLNDFTRVVG GKDAKPGQFP WQVLLNGKVD AFCGGSIINE
260 270 280 290 300
KWVVTAAHCI EPDVKITIVA GEHNTEKREH TEQKRNVIRT ILHHSYNATI
310 320 330 340 350
NKYNHDIALL ELDEPLTLNS YVTPICIADR EYSNIFLKFG SGYVSGWGRV
360 370 380 390 400
FNKGRSASIL QYLKVPLVDR ATCLRSTKFT IYNNMFCAGF HEGGKDSCQG
410 420 430 440 450
DSGGPHVTEV EGISFLTGII SWGEECAMKG KYGIYTKVSR YVNWIKEKTK
LT
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 418 | G → E in HEMB. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M21757 mRNA Translation: AAA75006.1 M33826 mRNA Translation: AAA30844.1 |
PIRi | A30351 |
RefSeqi | NP_001003323.1, NM_001003323.2 |
Genome annotation databases
GeneIDi | 404015 |
KEGGi | cfa:404015 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M21757 mRNA Translation: AAA75006.1 M33826 mRNA Translation: AAA30844.1 |
PIRi | A30351 |
RefSeqi | NP_001003323.1, NM_001003323.2 |
3D structure databases
AlphaFoldDBi | P19540 |
SMRi | P19540 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9612.ENSCAFP00000028031 |
Protein family/group databases
MEROPSi | S01.214 |
Proteomic databases
PaxDbi | P19540 |
Genome annotation databases
GeneIDi | 404015 |
KEGGi | cfa:404015 |
Organism-specific databases
CTDi | 2158 |
Phylogenomic databases
eggNOGi | ENOG502QUEV, Eukaryota |
InParanoidi | P19540 |
OrthoDBi | 1314811at2759 |
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_CANLF | |
Accessioni | P19540Primary (citable) accession number: P19540 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1991 |
Last sequence update: | February 1, 1991 | |
Last modified: | May 25, 2022 | |
This is version 180 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families