F13B_MOUSE
ID F13B_MOUSE Reviewed; 669 AA.
AC Q07968; B1AY02;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Coagulation factor XIII B chain;
DE AltName: Full=Protein-glutamine gamma-glutamyltransferase B chain;
DE AltName: Full=Transglutaminase B chain;
DE Flags: Precursor;
GN Name=F13b; Synonyms=Cf13b;
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], AND TISSUE SPECIFICITY.
RC STRAIN=B10.D2/OSN; TISSUE=Liver;
RX PubMed=8468048; DOI=10.1006/geno.1993.1106;
RA Nonaka M., Matsuda Y., Shiroishi T., Moriwaki K., Nonaka M.,
RA Natsuume-Sakai S.;
RT "Molecular cloning of the b subunit of mouse coagulation factor XIII and
RT assignment of the gene to chromosome 1: close evolutionary relationship to
RT complement factor H.";
RL Genomics 15:535-542(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
CC -!- FUNCTION: The B chain of factor XIII is not catalytically active, but
CC is thought to stabilize the A subunits and regulate the rate of
CC transglutaminase formation by thrombin. {ECO:0000250|UniProtKB:P05160}.
CC -!- SUBUNIT: Tetramer of two A chains (F13A1) and two B (F13B) chains.
CC {ECO:0000250|UniProtKB:P05160}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05160}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver and kidney.
CC {ECO:0000269|PubMed:8468048}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA00963.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D10071; BAA00963.1; ALT_INIT; mRNA.
DR EMBL; AC158946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL837518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466520; EDL39526.1; -; Genomic_DNA.
DR CCDS; CCDS48386.1; -.
DR PIR; A46013; A46013.
DR RefSeq; NP_112441.2; NM_031164.2.
DR AlphaFoldDB; Q07968; -.
DR SMR; Q07968; -.
DR BioGRID; 199567; 4.
DR IntAct; Q07968; 1.
DR STRING; 10090.ENSMUSP00000027615; -.
DR GlyGen; Q07968; 2 sites.
DR iPTMnet; Q07968; -.
DR PhosphoSitePlus; Q07968; -.
DR CPTAC; non-CPTAC-3398; -.
DR CPTAC; non-CPTAC-3537; -.
DR MaxQB; Q07968; -.
DR PaxDb; Q07968; -.
DR PeptideAtlas; Q07968; -.
DR PRIDE; Q07968; -.
DR ProteomicsDB; 275497; -.
DR Antibodypedia; 868; 241 antibodies from 25 providers.
DR DNASU; 14060; -.
DR Ensembl; ENSMUST00000027615; ENSMUSP00000027615; ENSMUSG00000026368.
DR GeneID; 14060; -.
DR KEGG; mmu:14060; -.
DR UCSC; uc007cwk.2; mouse.
DR CTD; 2165; -.
DR MGI; MGI:88379; F13b.
DR VEuPathDB; HostDB:ENSMUSG00000026368; -.
DR eggNOG; ENOG502RDCS; Eukaryota.
DR GeneTree; ENSGT00940000154967; -.
DR HOGENOM; CLU_020107_6_0_1; -.
DR InParanoid; Q07968; -.
DR OMA; PLCVRKE; -.
DR OrthoDB; 296899at2759; -.
DR PhylomeDB; Q07968; -.
DR TreeFam; TF326157; -.
DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR BioGRID-ORCS; 14060; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q07968; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q07968; protein.
DR Bgee; ENSMUSG00000026368; Expressed in left lobe of liver and 31 other tissues.
DR Genevisible; Q07968; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:MGI.
DR GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR CDD; cd00033; CCP; 7.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 8.
DR SMART; SM00032; CCP; 8.
DR SUPFAM; SSF57535; SSF57535; 10.
DR PROSITE; PS50923; SUSHI; 7.
PE 1: Evidence at protein level;
KW Blood coagulation; Disulfide bond; Glycoprotein; Hemostasis;
KW Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..669
FT /note="Coagulation factor XIII B chain"
FT /id="PRO_0000021223"
FT DOMAIN 25..89
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 90..149
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 152..211
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 212..270
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 273..330
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 335..392
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 395..453
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 454..517
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 523..581
FT /note="Sushi 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 582..648
FT /note="Sushi 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT DISULFID 26..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 60..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 92..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 119..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 154..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 181..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 214..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 242..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 275..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 303..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 337..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 365..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 397..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 426..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 455..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 487..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 525..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 554..579
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 583..637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 617..647
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CONFLICT 237
FT /note="V -> L (in Ref. 1; BAA00963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 76195 MW; 1ADB8DCCDE1050E0 CRC64;
MMTLRHLPFI LLLILSGELY AEEKQCDFPT VENGRIAQYY YTFKSFYFPM SVDKKLSFFC
LAGYATESGK QEEQIRCTAE GWSPNPRCYK KCLKPDLRNG YVSNDKVLYK LQERMSYGCS
SGYKTTGGKD EEVVHCLSAG WSSQPSCRKE QETCLAPELE HGNYSTTQRT FKVKDIVAYT
CTAGYYTTTG KQTGEAECQA NGWSLTPQCN KLMCSSLRLI ENGYFHPVKQ TYEEGDVVQF
FCHENYYLSG SDLIQCYNFG WYPESPICEG RRNRCPPPPV PLNSKIQPHS TTYRHGERVH
IECELNFVIQ GSEELLCENG KWTEPPKCIE EKEKVACEQP PSVENGVAHP HSEIYYSGDK
VTYRCGGGYS LRGSSTITCN RGRWTLPPEC VENIENCKPP PDIANGVVVD GLLASYTTGS
SVEYRCNEYY LLKGSETSRC EQGAWSSPPV CLEPCTIDVD HMNRNNIQLK WKYEGKILHG
DLIDFVCKQG YNLSPSIPLS EISAQCNRGD VRYPMCIRKE SKGMCASPPV IRNGDIVSSA
ARTYENGSSV EYRCFDNHFL QGSQNVYCVD GVWTTPPSCL EPCTLSFVEM DKNYLQLKWN
FDNRPLILHG EYIEFMCKRD AYISETSIAG SVLRVQCDRG RLKYPKCTPR DRRLSFQEAL
RTRRQMEKR
