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Q5NTB3

- FA11_BOVIN

UniProt

Q5NTB3 - FA11_BOVIN

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Protein

Coagulation factor XI

Gene

F11

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.By similarity

Catalytic activityi

Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei431 – 4311Charge relay systemBy similarity
Active sitei480 – 4801Charge relay systemBy similarity
Active sitei575 – 5751Charge relay systemBy similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. blood coagulation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Heparin-binding

Protein family/group databases

MEROPSiS01.213.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor XI (EC:3.4.21.27)
Short name:
FXI
Alternative name(s):
Plasma thromboplastin antecedent
Short name:
PTA
Cleaved into the following 2 chains:
Gene namesi
Name:F11
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in F11 are the cause of factor XI deficiency in Japanese black cattle. It is a hereditary mild bleeding disorder with an autosomal recessive mode of inheritance.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 387369Coagulation factor XIa heavy chainBy similarityPRO_0000244565Add
BLAST
Chaini388 – 625238Coagulation factor XIa light chainBy similarityPRO_0000244566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 103Sequence Analysis
Disulfide bondi29 – 29InterchainBy similarity
Disulfide bondi46 ↔ 76By similarity
Disulfide bondi50 ↔ 56By similarity
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi110 ↔ 193By similarity
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi136 ↔ 165By similarity
Disulfide bondi140 ↔ 146By similarity
Disulfide bondi200 ↔ 283By similarity
Disulfide bondi226 ↔ 255By similarity
Disulfide bondi230 ↔ 236By similarity
Disulfide bondi291 ↔ 374By similarity
Disulfide bondi317 ↔ 346By similarity
Disulfide bondi321 ↔ 327By similarity
Disulfide bondi339 – 339InterchainSequence Analysis
Disulfide bondi380 ↔ 500Interchain (between heavy and light chains)PROSITE-ProRule annotation
Disulfide bondi416 ↔ 432By similarity
Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi514 ↔ 581By similarity
Disulfide bondi545 ↔ 560By similarity
Disulfide bondi571 ↔ 599By similarity

Post-translational modificationi

Activated by factor XIIa (or XII), which cleaves each polypeptide after Arg-387 into the light chain, which contains the active site, and the heavy chain, which associates with high molecular weight (HMW) kininogen.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ5NTB3.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Forms a heterodimer with SERPINA5. After activation the heavy and light chains are also linked by a disulfide bond (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5NTB3.
SMRiQ5NTB3. Positions 20-622.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 10384Apple 1PROSITE-ProRule annotationAdd
BLAST
Domaini110 – 19384Apple 2PROSITE-ProRule annotationAdd
BLAST
Domaini200 – 28384Apple 3PROSITE-ProRule annotationAdd
BLAST
Domaini291 – 37484Apple 4PROSITE-ProRule annotationAdd
BLAST
Domaini388 – 623236Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni547 – 5504Heparin-bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase S1 family. Plasma kallikrein subfamily.PROSITE-ProRule annotation
Contains 4 apple domains.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000112467.
HOVERGENiHBG000399.
InParanoidiQ5NTB3.
KOiK01323.

Family and domain databases

InterProiIPR000177. Apple.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00024. PAN_1. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00005. APPLEDOMAIN.
PR00722. CHYMOTRYPSIN.
SMARTiSM00223. APPLE. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS00495. APPLE. 2 hits.
PS50948. PAN. 4 hits.
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.

Q5NTB3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLLYQMVHF ALFASVAGEC VTTLFQDACF KGGDITVAFA PNAKHCQIIC
60 70 80 90 100
THHPRCLLFT FMTESSSEDP TKWYTCILKD SVTETLPMVN MTGAISGYSS
110 120 130 140 150
KQCLHHISAC SKDMYVDLNM KGMNYNSSLA QSARECQQRC TDDTHCHFFT
160 170 180 190 200
FATRHFPSIK DRNTCLLKNT QTGTPTSITK LHEVVSGFSL KSCGLSNLAC
210 220 230 240 250
IRDIFPRTAF VDITIDTVMA PDPFVCRSIC THHPSCLFFT FLSEEWPTAS
260 270 280 290 300
ERNLCLLKTS SSGLPSARFR KNRAFSGFSL QHCQHSVPVF CHSSFYRNTD
310 320 330 340 350
FLGEELDIVD ADSHEACQKT CTNSIRCQFF TYSPSQESCN GGKGKCYLKL
360 370 380 390 400
SANGSPTKIL HGTGSISGYT LRLCKMDNVC TTKIKTRIVG GTQSVHGEWP
410 420 430 440 450
WQITLHVTSP TQRHLCGGAI IGNQWILTAA HCFNEVKSPN VLRVYSGILN
460 470 480 490 500
QSEIKEDTSF FGVQEIIIHD QYEKAESGYD IALLKLETAM NYTDSQWPIC
510 520 530 540 550
LPSKGDRNVM YTECWVTGWG YRKLRDKIQN TLQKAKVPLM TNEECQAGYR
560 570 580 590 600
EHRITSKMVC AGYREGGKDA CKGDSGGPLS CKHNEVWHLV GITSWGEGCG
610 620
QRERPGVYSN VVEYVDWILE KTQGP
Length:625
Mass (Da):69,872
Last modified:February 1, 2005 - v1
Checksum:iB4F10BCC7CA7B972
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti290 – 2901F → LYVQNI in factor XI deficiency.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB196307 mRNA. Translation: BAD77921.1.
AB196308 Genomic DNA. Translation: BAD77922.1.
RefSeqiNP_001008665.1. NM_001008665.1.
UniGeneiBt.29971.

Genome annotation databases

GeneIDi407998.
KEGGibta:407998.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB196307 mRNA. Translation: BAD77921.1 .
AB196308 Genomic DNA. Translation: BAD77922.1 .
RefSeqi NP_001008665.1. NM_001008665.1.
UniGenei Bt.29971.

3D structure databases

ProteinModelPortali Q5NTB3.
SMRi Q5NTB3. Positions 20-622.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S01.213.

Proteomic databases

PRIDEi Q5NTB3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 407998.
KEGGi bta:407998.

Organism-specific databases

CTDi 2160.

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000112467.
HOVERGENi HBG000399.
InParanoidi Q5NTB3.
KOi K01323.

Miscellaneous databases

NextBioi 20818619.

Family and domain databases

InterProi IPR000177. Apple.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00024. PAN_1. 4 hits.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00005. APPLEDOMAIN.
PR00722. CHYMOTRYPSIN.
SMARTi SM00223. APPLE. 4 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS00495. APPLE. 2 hits.
PS50948. PAN. 4 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "An insertion mutation of the bovine F11 gene is responsible for factor XI deficiency in Japanese black cattle."
    Kunieda M., Tsuji T., Abbasi A.R., Khalaj M., Ikeda M., Miyadera K., Ogawa H., Kunieda T.
    Mamm. Genome 16:383-389(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT FACTOR XI DEFICIENCY 290-LEU-TYR-VAL-GLN-ASN-ILE INS DEL.

Entry informationi

Entry nameiFA11_BOVIN
AccessioniPrimary (citable) accession number: Q5NTB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 1, 2005
Last modified: October 29, 2014
This is version 69 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

External Data

Dasty 3