Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Coagulation factor IX

Gene

F9

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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 similarity

Catalytic activityi

Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi48 – 481Calcium 2By similarity
Metal bindingi53 – 531Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi53 – 531Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi54 – 541Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi54 – 541Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi61 – 611Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity
Metal bindingi63 – 631Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi63 – 631Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi63 – 631Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi66 – 661Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity
Metal bindingi67 – 671Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi72 – 721Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity
Metal bindingi73 – 731Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi73 – 731Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi76 – 761Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi76 – 761Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity
Metal bindingi82 – 821Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity
Metal bindingi86 – 861Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity
Metal bindingi93 – 931Calcium 7By similarity
Metal bindingi94 – 941Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi96 – 961Calcium 7By similarity
Metal bindingi110 – 1101Calcium 7By similarity
Metal bindingi111 – 1111Calcium 7; via carbonyl oxygenBy similarity
Active sitei272 – 2721Charge relay systemBy similarity
Metal bindingi286 – 2861Calcium 8By similarity
Metal bindingi288 – 2881Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi291 – 2911Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi293 – 2931Calcium 8By similarity
Metal bindingi296 – 2961Calcium 8By similarity
Active sitei320 – 3201Charge relay systemBy similarity
Active sitei416 – 4161Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Protein family/group databases

MEROPSiS01.214.

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
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
Proteomesi
  • UP000011712 Componenti: Chromosome X

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Propeptidei26 – 4621By similarityPRO_0000027750Add
BLAST
Chaini47 – 466420Coagulation factor IXPRO_0000027751Add
BLAST
Chaini47 – 192146Coagulation factor IXa light chainPRO_0000027752Add
BLAST
Propeptidei193 – 23139Activation peptideBy similarityPRO_0000027753Add
BLAST
Chaini232 – 466235Coagulation factor IXa heavy chainPRO_0000027754Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 5314-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei61 – 6114-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei63 – 6314-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi64 ↔ 69By similarity
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei67 – 6714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei73 – 7314-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei76 – 7614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei82 – 8214-carboxyglutamatePROSITE-ProRule annotationBy similarity
Glycosylationi85 – 851O-linked (GalNAc...)By similarity
Modified residuei86 – 8614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi97 ↔ 108By similarity
Glycosylationi99 – 991O-linked (Glc...); alternateBy similarity
Glycosylationi99 – 991O-linked (Xyl...); alternateBy similarity
Disulfide bondi102 ↔ 117By similarity
Modified residuei110 – 1101(3R)-3-hydroxyaspartateBy similarity
Modified residuei114 – 1141PhosphoserineBy similarity
Disulfide bondi119 ↔ 128By similarity
Disulfide bondi134 ↔ 145By similarity
Disulfide bondi141 ↔ 155By similarity
Disulfide bondi157 ↔ 170By similarity
Disulfide bondi178 ↔ 340Interchain (between light and heavy chains)By similarity
Modified residuei202 – 2021SulfotyrosineBy similarity
Modified residuei205 – 2051PhosphoserineBy similarity
Modified residuei206 – 2061Phosphothreonine; alternateBy similarity
Glycosylationi206 – 2061O-linked (GalNAc...); alternateBy similarity
Glycosylationi221 – 2211N-linked (GlcNAc...)Sequence analysis
Glycosylationi223 – 2231O-linked (GalNAc...)By similarity
Glycosylationi230 – 2301O-linked (GalNAc...)By similarity
Disulfide bondi257 ↔ 273By similarity
Disulfide bondi387 ↔ 401By similarity
Disulfide bondi412 ↔ 440By similarity

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity
Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease.By similarity
Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei192 – 1932Cleavage; by factor XIaBy similarity
Sitei231 – 2322Cleavage; by factor XIaBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, Zymogen

Interactioni

Subunit structurei

Heterodimer of a light chain and a heavy chain; disulfide-linked. Interacts with SERPINC1.By similarity

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000006767.

Structurei

3D structure databases

ProteinModelPortaliQ6SA95.
SMRiQ6SA95. Positions 47-192, 232-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 9246GlaPROSITE-ProRule annotationAdd
BLAST
Domaini93 – 12937EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini130 – 17142EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini232 – 464233Peptidase S1PROSITE-ProRule annotationAdd
BLAST

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
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG013304.
InParanoidiQ6SA95.
KOiK01321.
OMAiMKGKYGI.
OrthoDBiEOG091G0AH5.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6SA95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCLNMIMAE PPGLITICLL GYLLGADCTV FLDHEDATKV LSRPKRYNSG
60 70 80 90 100
KLEEFVQGNL ERECMEEKCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN
110 120 130 140 150
PCLNGGICKD DINSYECWCQ TGFEGKNCEL DVTCNIKNGR CKQFCKLDAD
160 170 180 190 200
NKVVCSCTTG YQLAEDQKSC EPAVPFPCGR VSVPHISTTH TRAETLFLNM
210 220 230 240 250
DYENSTTDYE NSAEAEKNVD NVTQPLNDLT RIVGGKTAKP GQFPWQVLLK
260 270 280 290 300
GKIDAFCGGS IINEKWVVTA AHCINPDVEI TVVAGEHNTE ETEHTEQKRN
310 320 330 340 350
VIRTILHHSY NASVNKYSHD IALLELDEPL TLNSYVTPIC VADREYTNTF
360 370 380 390 400
LKFGYGYVSG WGKVFNKGRP ATILQYLKVP LVDRATCLRS TKFTIYNNMF
410 420 430 440 450
CAGFHEGGKD SCQGDSGGPH VTEVEGINFL TGIISWGEEC AMKGKYGIYT
460
KVSRYVNWIK EKTKLT
Length:466
Mass (Da):52,320
Last modified:July 5, 2004 - v1
Checksum:iD4F788D4CC1A4DCC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY461386
, AY461381, AY461382, AY461383, AY461384, AY461385 Genomic DNA. Translation: AAR26346.1.
RefSeqiNP_001009377.1. NM_001009377.3.

Genome annotation databases

EnsembliENSFCAT00000007300; ENSFCAP00000006767; ENSFCAG00000007298.
GeneIDi493973.
KEGGifca:493973.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY461386
, AY461381, AY461382, AY461383, AY461384, AY461385 Genomic DNA. Translation: AAR26346.1.
RefSeqiNP_001009377.1. NM_001009377.3.

3D structure databases

ProteinModelPortaliQ6SA95.
SMRiQ6SA95. Positions 47-192, 232-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000006767.

Protein family/group databases

MEROPSiS01.214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSFCAT00000007300; ENSFCAP00000006767; ENSFCAG00000007298.
GeneIDi493973.
KEGGifca:493973.

Organism-specific databases

CTDi2158.

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG013304.
InParanoidiQ6SA95.
KOiK01321.
OMAiMKGKYGI.
OrthoDBiEOG091G0AH5.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFA9_FELCA
AccessioniPrimary (citable) accession number: Q6SA95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.