GenomeNet

Database: UniProt/SWISS-PROT
Entry: F13A_MOUSE
LinkDB: F13A_MOUSE
Original site: 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   28-FEB-2018, entry version 130.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Factor XIII is activated by thrombin and calcium ion to
CC       a transglutaminase that catalyzes the formation of gamma-glutamyl-
CC       epsilon-lysine cross-links between fibrin chains, thus stabilizing
CC       the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or
CC       fibronectin, to the alpha chains of fibrin.
CC       {ECO:0000250|UniProtKB:P00488}.
CC   -!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
CC       protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
CC       {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.
CC       {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
CC       blood plasma. Cytoplasmic in most tissues, but also secreted in
CC       the blood plasma. {ECO:0000250|UniProtKB:P00488}.
CC   -!- PTM: The activation peptide is released by thrombin.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
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   UniGene; Mm.235105; -.
DR   ProteinModelPortal; Q8BH61; -.
DR   SMR; Q8BH61; -.
DR   STRING; 10090.ENSMUSP00000048667; -.
DR   iPTMnet; Q8BH61; -.
DR   PhosphoSitePlus; Q8BH61; -.
DR   EPD; Q8BH61; -.
DR   MaxQB; Q8BH61; -.
DR   PaxDb; Q8BH61; -.
DR   PRIDE; Q8BH61; -.
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   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   GeneTree; ENSGT00760000119108; -.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; Q8BH61; -.
DR   KO; K03917; -.
DR   OMA; CEEDAVY; -.
DR   OrthoDB; EOG091G030K; -.
DR   PhylomeDB; Q8BH61; -.
DR   TreeFam; TF324278; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR   ChiTaRS; F13a1; mouse.
DR   PRO; PR:Q8BH61; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   Bgee; ENSMUSG00000039109; -.
DR   CleanEx; MM_F13A1; -.
DR   Genevisible; Q8BH61; MM.
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; ISS:UniProtKB.
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; 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; SSF81296; SSF81296; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Blood coagulation; Calcium;
KW   Complete proteome; Cytoplasm; Glycoprotein; Hemostasis; Metal-binding;
KW   Reference proteome; Secreted; Transferase; Zymogen.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P00488}.
FT   PROPEP        2     38       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000033648.
FT   CHAIN        39    732       Coagulation factor XIII A chain.
FT                                /FTId=PRO_0000033649.
FT   ACT_SITE    315    315       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    374    374       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    397    397       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       437    437       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   METAL       439    439       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   METAL       486    486       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   METAL       491    491       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   SITE         38     39       Cleavage; by thrombin; to produce active
FT                                factor XIII-A. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000250|UniProtKB:P00488}.
FT   CARBOHYD    614    614       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT      5      5       P -> Q (in Ref. 1; BAC29414).
FT                                {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
//
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