FA11_BOVIN
ID FA11_BOVIN Reviewed; 625 AA.
AC Q5NTB3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Coagulation factor XI;
DE Short=FXI;
DE EC=3.4.21.27;
DE AltName: Full=Plasma thromboplastin antecedent;
DE Short=PTA;
DE Contains:
DE RecName: Full=Coagulation factor XIa heavy chain;
DE Contains:
DE RecName: Full=Coagulation factor XIa light chain;
DE Flags: Precursor;
GN Name=F11;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT FACTOR XI DEFICIENCY
RP 290-LEU-TYR-VAL-GLN-ASN-ILE INS DEL.
RX PubMed=16104386; DOI=10.1007/s00335-004-2462-5;
RA Kunieda M., Tsuji T., Abbasi A.R., Khalaj M., Ikeda M., Miyadera K.,
RA Ogawa H., Kunieda T.;
RT "An insertion mutation of the bovine F11 gene is responsible for factor XI
RT deficiency in Japanese black cattle.";
RL Mamm. Genome 16:383-389(2005).
CC -!- FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway
CC of blood coagulation by activating factor IX. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor
CC IX to form factor IXa.; EC=3.4.21.27;
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms a heterodimer with
CC SERPINA5. After activation the heavy and light chains are also linked
CC by a disulfide bond (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Activated by factor XIIa (or XII), which cleaves each polypeptide
CC after Arg-387 into the light chain, which contains the active site, and
CC the heavy chain, which associates with high molecular weight (HMW)
CC kininogen. {ECO:0000250}.
CC -!- PTM: N-glycosylated on both chains. N-glycosylated sites mainly consist
CC of nonfucosylated sialylated biantennary (in high abundance) and/or
CC triantennary (in low abundance) complex structures.
CC {ECO:0000250|UniProtKB:P03951}.
CC -!- DISEASE: Note=Defects in F11 are the cause of factor XI deficiency in
CC Japanese black cattle. It is a hereditary mild bleeding disorder with
CC an autosomal recessive mode of inheritance.
CC {ECO:0000269|PubMed:16104386}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AB196307; BAD77921.1; -; mRNA.
DR EMBL; AB196308; BAD77922.1; -; Genomic_DNA.
DR RefSeq; NP_001008665.1; NM_001008665.1.
DR AlphaFoldDB; Q5NTB3; -.
DR SMR; Q5NTB3; -.
DR STRING; 9913.ENSBTAP00000004648; -.
DR MEROPS; S01.213; -.
DR PaxDb; Q5NTB3; -.
DR PRIDE; Q5NTB3; -.
DR GeneID; 407998; -.
DR KEGG; bta:407998; -.
DR CTD; 2160; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q5NTB3; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01100; APPLE_Factor_XI_like; 4.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR000177; Apple.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00024; PAN_1; 4.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00005; APPLEDOMAIN.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00223; APPLE; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS00495; APPLE; 2.
DR PROSITE; PS50948; PAN; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Disease variant; Disulfide bond; Glycoprotein;
KW Hemostasis; Heparin-binding; Hydrolase; Protease; Reference proteome;
KW Repeat; Secreted; Serine protease; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..387
FT /note="Coagulation factor XIa heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000244565"
FT CHAIN 388..625
FT /note="Coagulation factor XIa light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000244566"
FT DOMAIN 20..103
FT /note="Apple 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 110..193
FT /note="Apple 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 200..283
FT /note="Apple 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 291..374
FT /note="Apple 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 388..623
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 431
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 480
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 575
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 547..550
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P03951"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P03951"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P03951"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P03951"
FT DISULFID 20..103
FT /evidence="ECO:0000255"
FT DISULFID 29
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 46..76
FT /evidence="ECO:0000250"
FT DISULFID 50..56
FT /evidence="ECO:0000250"
FT DISULFID 110..193
FT /evidence="ECO:0000250"
FT DISULFID 136..165
FT /evidence="ECO:0000250"
FT DISULFID 140..146
FT /evidence="ECO:0000250"
FT DISULFID 200..283
FT /evidence="ECO:0000250"
FT DISULFID 226..255
FT /evidence="ECO:0000250"
FT DISULFID 230..236
FT /evidence="ECO:0000250"
FT DISULFID 291..374
FT /evidence="ECO:0000250"
FT DISULFID 317..346
FT /evidence="ECO:0000250"
FT DISULFID 321..327
FT /evidence="ECO:0000250"
FT DISULFID 339
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 380..500
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 416..432
FT /evidence="ECO:0000250"
FT DISULFID 514..581
FT /evidence="ECO:0000250"
FT DISULFID 545..560
FT /evidence="ECO:0000250"
FT DISULFID 571..599
FT /evidence="ECO:0000250"
FT VARIANT 290
FT /note="F -> LYVQNI (in factor XI deficiency)"
SQ SEQUENCE 625 AA; 69872 MW; B4F10BCC7CA7B972 CRC64;
MTLLYQMVHF ALFASVAGEC VTTLFQDACF KGGDITVAFA PNAKHCQIIC THHPRCLLFT
FMTESSSEDP TKWYTCILKD SVTETLPMVN MTGAISGYSS KQCLHHISAC SKDMYVDLNM
KGMNYNSSLA QSARECQQRC TDDTHCHFFT FATRHFPSIK DRNTCLLKNT QTGTPTSITK
LHEVVSGFSL KSCGLSNLAC IRDIFPRTAF VDITIDTVMA PDPFVCRSIC THHPSCLFFT
FLSEEWPTAS ERNLCLLKTS SSGLPSARFR KNRAFSGFSL QHCQHSVPVF CHSSFYRNTD
FLGEELDIVD ADSHEACQKT CTNSIRCQFF TYSPSQESCN GGKGKCYLKL SANGSPTKIL
HGTGSISGYT LRLCKMDNVC TTKIKTRIVG GTQSVHGEWP WQITLHVTSP TQRHLCGGAI
IGNQWILTAA HCFNEVKSPN VLRVYSGILN QSEIKEDTSF FGVQEIIIHD QYEKAESGYD
IALLKLETAM NYTDSQWPIC LPSKGDRNVM YTECWVTGWG YRKLRDKIQN TLQKAKVPLM
TNEECQAGYR EHRITSKMVC AGYREGGKDA CKGDSGGPLS CKHNEVWHLV GITSWGEGCG
QRERPGVYSN VVEYVDWILE KTQGP
