FA11_MOUSE
ID FA11_MOUSE Reviewed; 624 AA.
AC Q91Y47; Q9DAT3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 153.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B10.WR; TISSUE=Liver;
RX PubMed=9242536;
RA Gailani D., Sun M.F., Sun Y.;
RT "A comparison of murine and human factor XI.";
RL Blood 90:1055-1064(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.
CC -!- PTM: Activated by factor XIIa (or XII), which cleaves each polypeptide
CC after Arg-389 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 -!- SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; AF356627; AAK40233.1; -; mRNA.
DR EMBL; AK005546; BAB24114.1; -; mRNA.
DR EMBL; CH466554; EDL35542.1; -; Genomic_DNA.
DR EMBL; BC019485; AAH19485.1; -; mRNA.
DR CCDS; CCDS22274.1; -.
DR RefSeq; NP_082342.1; NM_028066.2.
DR AlphaFoldDB; Q91Y47; -.
DR SMR; Q91Y47; -.
DR STRING; 10090.ENSMUSP00000034064; -.
DR MEROPS; S01.213; -.
DR GlyGen; Q91Y47; 5 sites.
DR iPTMnet; Q91Y47; -.
DR PhosphoSitePlus; Q91Y47; -.
DR SwissPalm; Q91Y47; -.
DR CPTAC; non-CPTAC-3420; -.
DR MaxQB; Q91Y47; -.
DR PaxDb; Q91Y47; -.
DR PeptideAtlas; Q91Y47; -.
DR PRIDE; Q91Y47; -.
DR ProteomicsDB; 267694; -.
DR Antibodypedia; 17547; 461 antibodies from 32 providers.
DR DNASU; 109821; -.
DR Ensembl; ENSMUST00000034064; ENSMUSP00000034064; ENSMUSG00000031645.
DR GeneID; 109821; -.
DR KEGG; mmu:109821; -.
DR UCSC; uc009los.2; mouse.
DR CTD; 2160; -.
DR MGI; MGI:99481; F11.
DR VEuPathDB; HostDB:ENSMUSG00000031645; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158569; -.
DR HOGENOM; CLU_031604_0_0_1; -.
DR InParanoid; Q91Y47; -.
DR OMA; QNCRHSV; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q91Y47; -.
DR TreeFam; TF343687; -.
DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR BioGRID-ORCS; 109821; 5 hits in 57 CRISPR screens.
DR ChiTaRS; F11; mouse.
DR PRO; PR:Q91Y47; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91Y47; protein.
DR Bgee; ENSMUSG00000031645; Expressed in left lobe of liver and 20 other tissues.
DR Genevisible; Q91Y47; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; ISO:MGI.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:MGI.
DR GO; GO:0031639; P:plasminogen activation; ISO:MGI.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; ISO:MGI.
DR GO; GO:0030193; P:regulation of blood coagulation; IMP:MGI.
DR CDD; cd01100; APPLE_Factor_XI_like; 4.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
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; 3.
DR PROSITE; PS50948; PAN; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Blood coagulation; Disulfide bond; Glycoprotein; Hemostasis;
KW Heparin-binding; Hydrolase; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..389
FT /note="Coagulation factor XIa heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027827"
FT CHAIN 390..624
FT /note="Coagulation factor XIa light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027828"
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..376
FT /note="Apple 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 390..622
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 430
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 479
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 574
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 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P03951"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P03951"
FT DISULFID 20..103
FT /evidence="ECO:0000255"
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..376
FT /evidence="ECO:0000250"
FT DISULFID 317..348
FT /evidence="ECO:0000250"
FT DISULFID 321..327
FT /evidence="ECO:0000250"
FT DISULFID 339
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 382..499
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000255|PROSITE-ProRule:PRU00315"
FT DISULFID 415..431
FT /evidence="ECO:0000250"
FT DISULFID 513..580
FT /evidence="ECO:0000250"
FT DISULFID 544..559
FT /evidence="ECO:0000250"
FT DISULFID 570..598
FT /evidence="ECO:0000250"
FT CONFLICT 114
FT /note="V -> E (in Ref. 1; AAK40233)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="S -> I (in Ref. 1; AAK40233)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="I -> L (in Ref. 1; AAK40233)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="V -> E (in Ref. 1; AAK40233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 69789 MW; 0EEDDEBC56009E97 CRC64;
MTSLHQVLYF IFFASVSSEC VTKVFKDISF QGGDLSTVFT PSATYCRLVC THHPRCLLFT
FMAESSSDDP TKWFACILKD SVTEILPMVN MTGAISGYSF KQCPQQLSTC SKDVYVNLDM
KGMNYNSSVV KNARECQERC TDDAHCQFFT YATGYFPSVD HRKMCLLKYT RTGTPTTITK
LNGVVSGFSL KSCGLSNLAC IRDIFPNTVL ADLNIDSVVA PDAFVCRRIC THHPTCLFFT
FFSQAWPKES QRHLCLLKTS ESGLPSTRIT KSHALSGFSL QHCRHSVPVF CHPSFYNDTD
FLGEELDIVD VKGQETCQKT CTNNARCQFF TYYPSHRLCN ERNRRGRCYL KLSSNGSPTR
ILHGRGGISG YSLRLCKMDN VCTTKINPRV VGGAASVHGE WPWQVTLHIS QGHLCGGSII
GNQWILTAAH CFSGIETPKK LRVYGGIVNQ SEINEGTAFF RVQEMIIHDQ YTTAESGYDI
ALLKLESAMN YTDFQRPICL PSKGDRNAVH TECWVTGWGY TALRGEVQST LQKAKVPLVS
NEECQTRYRR HKITNKMICA GYKEGGKDTC KGDSGGPLSC KYNGVWHLVG ITSWGEGCGQ
KERPGVYTNV AKYVDWILEK TQTV
