ID   F13A_MOUSE              Reviewed;         732 AA.
AC   Q8BH61; Q3TNF9; Q8BIP2;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 163.
DE   RecName: Full=Coagulation factor XIII A chain;
DE            Short=Coagulation factor XIIIa;
DE            EC=2.3.2.13 {ECO:0000250|UniProtKB:P00488};
DE   AltName: Full=Protein-glutamine gamma-glutamyltransferase A chain;
DE   AltName: Full=Transglutaminase A chain;
DE   Flags: Precursor;
GN   Name=F13a1; Synonyms=F13a;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone, Cerebellum, and Spleen;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Lung, Pancreas, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Factor XIII is activated by thrombin and calcium ion to a
CC       transglutaminase that catalyzes the formation of gamma-glutamyl-
CC       epsilon-lysine cross-links between fibrin chains, thus stabilizing the
CC       fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin,
CC       to the alpha chains of fibrin. {ECO:0000250|UniProtKB:P00488}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC         lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:138370; EC=2.3.2.13;
CC         Evidence={ECO:0000250|UniProtKB:P00488};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P00488};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00488};
CC   -!- SUBUNIT: Tetramer of two A chains (F13A1) and two B (F13B) chains.
CC       {ECO:0000250|UniProtKB:P00488}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00488}.
CC       Secreted {ECO:0000250|UniProtKB:P00488}. Note=Secreted into the blood
CC       plasma. Cytoplasmic in most tissues, but also secreted in the blood
CC       plasma. {ECO:0000250|UniProtKB:P00488}.
CC   -!- PTM: The activation peptide is released by thrombin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
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DR   EMBL; AK036403; BAC29414.1; -; mRNA.
DR   EMBL; AK049092; BAC33539.1; -; mRNA.
DR   EMBL; AK165311; BAE38130.1; -; mRNA.
DR   EMBL; BC040274; AAH40274.1; -; mRNA.
DR   CCDS; CCDS26456.1; -.
DR   RefSeq; NP_001159863.1; NM_001166391.1.
DR   RefSeq; NP_083060.2; NM_028784.3.
DR   AlphaFoldDB; Q8BH61; -.
DR   SMR; Q8BH61; -.
DR   BioGRID; 216524; 8.
DR   STRING; 10090.ENSMUSP00000048667; -.
DR   BindingDB; Q8BH61; -.
DR   GlyCosmos; Q8BH61; 1 site, No reported glycans.
DR   GlyGen; Q8BH61; 1 site.
DR   iPTMnet; Q8BH61; -.
DR   PhosphoSitePlus; Q8BH61; -.
DR   CPTAC; non-CPTAC-5604; -.
DR   EPD; Q8BH61; -.
DR   jPOST; Q8BH61; -.
DR   MaxQB; Q8BH61; -.
DR   PaxDb; 10090-ENSMUSP00000048667; -.
DR   ProteomicsDB; 271521; -.
DR   Pumba; Q8BH61; -.
DR   Antibodypedia; 882; 1561 antibodies from 42 providers.
DR   DNASU; 74145; -.
DR   Ensembl; ENSMUST00000037491.11; ENSMUSP00000048667.9; ENSMUSG00000039109.18.
DR   Ensembl; ENSMUST00000164727.8; ENSMUSP00000128316.2; ENSMUSG00000039109.18.
DR   GeneID; 74145; -.
DR   KEGG; mmu:74145; -.
DR   UCSC; uc007qcn.2; mouse.
DR   AGR; MGI:1921395; -.
DR   CTD; 2162; -.
DR   MGI; MGI:1921395; F13a1.
DR   VEuPathDB; HostDB:ENSMUSG00000039109; -.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   GeneTree; ENSGT01050000244939; -.
DR   HOGENOM; CLU_013435_0_2_1; -.
DR   InParanoid; Q8BH61; -.
DR   OMA; EEVCQPW; -.
DR   OrthoDB; 5344745at2759; -.
DR   PhylomeDB; Q8BH61; -.
DR   TreeFam; TF324278; -.
DR   BRENDA; 2.3.2.13; 3474.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR   BioGRID-ORCS; 74145; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; F13a1; mouse.
DR   PRO; PR:Q8BH61; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q8BH61; Protein.
DR   Bgee; ENSMUSG00000039109; Expressed in stroma of bone marrow and 172 other cell types or tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IMP:MGI.
DR   GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR   GO; GO:0072378; P:blood coagulation, fibrin clot formation; IMP:MGI.
DR   GO; GO:0018149; P:peptide cross-linking; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   InterPro; IPR023608; Transglutaminase_animal.
DR   InterPro; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590:SF42; COAGULATION FACTOR XIII A CHAIN; 1.
DR   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   PIRSF; PIRSF000459; TGM_EBP42; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
DR   Genevisible; Q8BH61; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Blood coagulation; Calcium; Cytoplasm;
KW   Glycoprotein; Hemostasis; Metal-binding; Reference proteome; Secreted;
KW   Transferase; Zymogen.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   PROPEP          2..38
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033648"
FT   CHAIN           39..732
FT                   /note="Coagulation factor XIII A chain"
FT                   /id="PRO_0000033649"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   ACT_SITE        397
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   BINDING         437
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   BINDING         439
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   BINDING         486
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   BINDING         491
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   SITE            38..39
FT                   /note="Cleavage; by thrombin; to produce active factor
FT                   XIII-A"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   CARBOHYD        614
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        5
FT                   /note="P -> Q (in Ref. 1; BAC29414)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   732 AA;  83207 MW;  47B338665D40C4D9 CRC64;
     MSDTPASTFG GRRAVPPNNS NAAEVDLPTE ELQGLVPRGV NLKDYLNVTA VHLFKERWDS
     NKIDHHTDKY DNNKLIVRRG QTFYIQIDFN RPYDPRKDLF RVEYVIGRYP QENKGTYIPV
     PVVKELQSGK WGAKVIMNED RSVRLSVQSS PECIVGKFRM YVAVWTPYGI LRTRRDPETD
     TYILFNPWCE EDAVYLDDEK EREEYVLNDI GVIFYGDFKD IKSRSWSYGQ FEDGILDTCL
     YVMDKAEMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNVYAYGIPP SAWTGSVDIL
     LEYRSSETPV RYGQCWVFAG VFNTFLRCLG IPARVITNYF SAHDNDANLQ MDIFLEEDGN
     VSSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAVKH
     GHVCFQFDAP FVFAEVNSDL VYITAKQDGT HVVEAVDATH IGKLIVTKQI GGDGMQDITD
     TYKFQEGQEE ERLALETALM YGAKKTLNTE GVVKSRSDVT MNFDVENAVL GKDFKVTITF
     QNNSSNLYTI LAYLSGNITF YTGVSKKEFK KESFEETLDP FSSKKKEVLV RAGEYMSHLL
     EQGFLHFFVT ARINESRDVL AKQKSIILTI PKITIKVRGA AMVGSDMVVT VEFTNPLKET
     LQNVWIHLDG PGVMRPKRKV FREIRPNTTV QWEEVCRPWV SGHRKLIASM TSDSLRHVYG
     ELDLQIQRRP TM
//