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Protein

Coagulation factor X

Gene

F10

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei275 – 2751Charge relay system1 Publication
Active sitei321 – 3211Charge relay system1 Publication
Active sitei418 – 4181Charge relay system1 Publication

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

Enzyme and pathway databases

ReactomeiR-BTA-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-140875. Common Pathway of Fibrin Clot Formation.
R-BTA-159740. Gamma-carboxylation of protein precursors.
R-BTA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-BTA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00743.

Protein family/group databases

MEROPSiS01.216.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor X (EC:3.4.21.6)
Alternative name(s):
Stuart factor
Cleaved into the following 3 chains:
Gene namesi
Name:F10
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 12

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3656.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Propeptidei24 – 40171 PublicationPRO_0000027779Add
BLAST
Chaini41 – 492452Coagulation factor XPRO_0000027780Add
BLAST
Chaini41 – 180140Factor X light chainPRO_0000027781Add
BLAST
Chaini183 – 492310Factor X heavy chainPRO_0000027782Add
BLAST
Propeptidei183 – 23351Activation peptidePRO_0000027783Add
BLAST
Chaini234 – 492259Activated factor Xa heavy chainPRO_0000027784Add
BLAST
Propeptidei476 – 49217May be removed but is not necessary for activationPRO_0000027785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi57 ↔ 62By similarity
Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi90 ↔ 1011 Publication
Disulfide bondi95 ↔ 1101 Publication
Modified residuei103 – 1031(3R)-3-hydroxyaspartate1 Publication
Disulfide bondi112 ↔ 1211 Publication
Disulfide bondi129 ↔ 140By similarity
Disulfide bondi136 ↔ 149By similarity
Disulfide bondi151 ↔ 164By similarity
Disulfide bondi172 ↔ 341Interchain (between light and heavy chains)PROSITE-ProRule annotation1 Publication
Modified residuei200 – 2001Sulfotyrosine1 Publication
Glycosylationi208 – 2081O-linked (GalNAc...)1 Publication
Glycosylationi218 – 2181N-linked (GlcNAc...)1 PublicationCAR_000011
Disulfide bondi240 ↔ 2451 Publication
Disulfide bondi260 ↔ 2761 Publication
Disulfide bondi389 ↔ 4031 Publication
Disulfide bondi414 ↔ 4421 Publication
Glycosylationi485 – 4851O-linked (GalNAc...)1 Publication

Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
N- and O-glycosylated.2 Publications
The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).1 Publication
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei233 – 2342Cleavage; by coagulation factor IXa and coagulation factor VIIa

Keywords - PTMi

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

Proteomic databases

PaxDbiP00743.
PRIDEiP00743.

PTM databases

UniCarbKBiP00743.

Miscellaneous databases

PMAP-CutDBP00743.

Interactioni

Subunit structurei

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. Forms a heterodimer with SERPINA5 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021789.

Chemistry

BindingDBiP00743.

Structurei

Secondary structure

1
492
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 483Combined sources
Helixi53 – 575Combined sources
Beta strandi58 – 614Combined sources
Helixi64 – 718Combined sources
Helixi74 – 829Combined sources
Turni86 – 905Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi121 – 1233Combined sources
Turni131 – 1344Combined sources
Beta strandi135 – 1384Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi235 – 2373Combined sources
Turni242 – 2443Combined sources
Beta strandi248 – 2525Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi258 – 2647Combined sources
Beta strandi266 – 2727Combined sources
Beta strandi304 – 3096Combined sources
Turni315 – 3173Combined sources
Beta strandi323 – 3297Combined sources
Helixi345 – 3506Combined sources
Turni351 – 3544Combined sources
Beta strandi355 – 3639Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi370 – 3723Combined sources
Beta strandi377 – 3837Combined sources
Helixi386 – 3927Combined sources
Beta strandi401 – 4077Combined sources
Beta strandi421 – 4266Combined sources
Beta strandi429 – 44315Combined sources
Beta strandi447 – 4548Combined sources
Helixi455 – 4573Combined sources
Helixi458 – 4647Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APONMR-A85-126[»]
1CCFNMR-A85-126[»]
1IODX-ray2.30G41-84[»]
1KIGX-ray3.00H234-474[»]
L129-179[»]
1WHENMR-A41-126[»]
1WHFNMR-A41-126[»]
ProteinModelPortaliP00743.
SMRiP00743. Positions 42-126, 129-179, 234-474.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00743.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8545GlaPROSITE-ProRule annotationAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini125 – 16541EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini234 – 466233Peptidase S1PROSITE-ProRule annotationAdd
BLAST

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.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00743.
KOiK01314.
OMAiEMAHEVE.
OrthoDBiEOG75B84T.
TreeFamiTF327329.

Family and domain databases

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. 1 hit.
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.

P00743-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLLHLVLL STALGGLLRP AGSVFLPRDQ AHRVLQRARR ANSFLEEVKQ
60 70 80 90 100
GNLERECLEE ACSLEEAREV FEDAEQTDEF WSKYKDGDQC EGHPCLNQGH
110 120 130 140 150
CKDGIGDYTC TCAEGFEGKN CEFSTREICS LDNGGCDQFC REERSEVRCS
160 170 180 190 200
CAHGYVLGDD SKSCVSTERF PCGKFTQGRS RRWAIHTSED ALDASELEHY
210 220 230 240 250
DPADLSPTES SLDLLGLNRT EPSAGEDGSQ VVRIVGGRDC AEGECPWQAL
260 270 280 290 300
LVNEENEGFC GGTILNEFYV LTAAHCLHQA KRFTVRVGDR NTEQEEGNEM
310 320 330 340 350
AHEVEMTVKH SRFVKETYDF DIAVLRLKTP IRFRRNVAPA CLPEKDWAEA
360 370 380 390 400
TLMTQKTGIV SGFGRTHEKG RLSSTLKMLE VPYVDRSTCK LSSSFTITPN
410 420 430 440 450
MFCAGYDTQP EDACQGDSGG PHVTRFKDTY FVTGIVSWGE GCARKGKFGV
460 470 480 490
YTKVSNFLKW IDKIMKARAG AAGSRGHSEA PATWTVPPPL PL
Length:492
Mass (Da):54,510
Last modified:August 13, 1987 - v1
Checksum:iD5BD911FB72F1D30
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031D → N AA sequence (PubMed:6766735).Curated
Sequence conflicti293 – 2931Missing AA sequence (PubMed:1059093).Curated
Sequence conflicti296 – 2983EGN → GDE AA sequence (PubMed:1059093).Curated
Sequence conflicti335 – 3351Missing AA sequence (PubMed:1059093).Curated
Sequence conflicti349 – 3502EA → AE AA sequence (PubMed:1059093).Curated
Sequence conflicti355 – 3551Missing AA sequence (PubMed:1059093).Curated
Sequence conflicti442 – 4454CARK → GKFG AA sequence (PubMed:1059093).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00673 mRNA. Translation: CAA25286.1.
PIRiA22867. EXBO.
RefSeqiNP_001073682.1. NM_001080213.1.
UniGeneiBt.13151.

Genome annotation databases

EnsembliENSBTAT00000021789; ENSBTAP00000021789; ENSBTAG00000016385.
GeneIDi280787.
KEGGibta:280787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00673 mRNA. Translation: CAA25286.1.
PIRiA22867. EXBO.
RefSeqiNP_001073682.1. NM_001080213.1.
UniGeneiBt.13151.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APONMR-A85-126[»]
1CCFNMR-A85-126[»]
1IODX-ray2.30G41-84[»]
1KIGX-ray3.00H234-474[»]
L129-179[»]
1WHENMR-A41-126[»]
1WHFNMR-A41-126[»]
ProteinModelPortaliP00743.
SMRiP00743. Positions 42-126, 129-179, 234-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021789.

Chemistry

BindingDBiP00743.
ChEMBLiCHEMBL3656.

Protein family/group databases

MEROPSiS01.216.

PTM databases

UniCarbKBiP00743.

Proteomic databases

PaxDbiP00743.
PRIDEiP00743.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000021789; ENSBTAP00000021789; ENSBTAG00000016385.
GeneIDi280787.
KEGGibta:280787.

Organism-specific databases

CTDi2159.

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00743.
KOiK01314.
OMAiEMAHEVE.
OrthoDBiEOG75B84T.
TreeFamiTF327329.

Enzyme and pathway databases

ReactomeiR-BTA-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-140875. Common Pathway of Fibrin Clot Formation.
R-BTA-159740. Gamma-carboxylation of protein precursors.
R-BTA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-BTA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00743.

Miscellaneous databases

EvolutionaryTraceiP00743.
NextBioi20804947.
PMAP-CutDBP00743.

Family and domain databases

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. 1 hit.
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...

Publicationsi

  1. "Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequence."
    Fung M.R., Campbell R.M., McGillivray R.T.A.
    Nucleic Acids Res. 12:4481-4492(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-487.
  2. "Amino acid sequence of the light chain of bovine factor X1 (Stuart factor)."
    Enfield D.L., Ericsson L.H., Fujikawa K., Walsh K.A., Neurath H., Titani K.
    Biochemistry 19:659-667(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 41-180, GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-72; GLU-75 AND GLU-79.
  3. "The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens."
    McMullen B.A., Fujikawa K., Kisiel W.
    Biochem. Biophys. Res. Commun. 115:8-14(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION AT ASP-103.
  4. Cited for: PROTEIN SEQUENCE OF 183-492, GLYCOSYLATION AT ASN-218 AND THR-485, DISULFIDE BONDS.
  5. "Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X."
    Inoue K., Morita T.
    Eur. J. Biochem. 218:153-163(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 183-233, GLYCOSYLATION AT THR-208.
  6. "Bovine factor X 1a (activated Stuart factor). Evidence of homology with mammalian serine proteases."
    Titani K., Hermodson M.A., Fujikawa K., Ericsson L.H., Walsh K.A., Neurath H., Davie E.W.
    Biochemistry 11:4899-4903(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  7. "Activation of bovine factor X (Stuart factor): conversion of factor Xa-alpha to factor Xa-beta."
    Fujikawa K., Titani K., Davie E.W.
    Proc. Natl. Acad. Sci. U.S.A. 72:3359-3363(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  8. "Calcium-binding properties of bovine factor X lacking the gamma-carboxyglutamic acid-containing region."
    Sugo T., Bjoerk I., Holmgren A., Stenflo J.
    J. Biol. Chem. 259:5705-5710(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING.
  9. "Localization of the structural difference between bovine blood coagulation factors X1 and X2 to tyrosine 18 in the activation peptide."
    Morita T., Jackson C.M.
    J. Biol. Chem. 261:4008-4014(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION AT TYR-200.
  10. "1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X."
    Selander M., Persson E., Stenflo J., Drakenberg T.
    Biochemistry 29:8111-8118(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 85-126.
  11. "Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding."
    Ullner M., Selander M., Persson E., Stenflo J., Drakenberg T., Teleman O.
    Biochemistry 31:5974-5983(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 85-126.
  12. "How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X."
    Selander-Sunnerhagen M., Ullner M., Persson E., Teleman O., Stenflo J., Drakenberg T.
    J. Biol. Chem. 267:19642-19649(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 85-126.
  13. "The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study."
    Sunnerhagen M., Olah G.A., Stenflo J., Forsen S., Drakenberg T., Trewhella J.
    Biochemistry 35:11547-11559(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 41-126.

Entry informationi

Entry nameiFA10_BOVIN
AccessioniPrimary (citable) accession number: P00743
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: May 11, 2016
This is version 191 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Calcium also binds, with stronger affinity to another site, beyond the GLA domain.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.