F13A_MOUSE
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 03-AUG-2022, entry version 155.
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 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; Q8BH61; -.
DR PRIDE; Q8BH61; -.
DR ProteomicsDB; 271521; -.
DR Antibodypedia; 882; 1392 antibodies from 42 providers.
DR DNASU; 74145; -.
DR Ensembl; ENSMUST00000037491; ENSMUSP00000048667; ENSMUSG00000039109.
DR Ensembl; ENSMUST00000164727; ENSMUSP00000128316; ENSMUSG00000039109.
DR GeneID; 74145; -.
DR KEGG; mmu:74145; -.
DR UCSC; uc007qcn.2; mouse.
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; TRPMRKM; -.
DR OrthoDB; 297055at2759; -.
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 72 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 tissues.
DR Genevisible; Q8BH61; MM.
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; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.90.260.10; -; 1.
DR InterPro; IPR034810; Factor_XIII_A.
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; PTHR11590:SF42; 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; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
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
