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Database: UniProt
Entry: M3XN90_MUSPF
LinkDB: M3XN90_MUSPF
Original site: M3XN90_MUSPF 
ID   M3XN90_MUSPF            Unreviewed;       732 AA.
AC   M3XN90;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Coagulation factor XIII A chain {ECO:0000313|Ensembl:ENSMPUP00000000540.1, ECO:0000313|RefSeq:XP_004753720.1};
GN   Name=F13A1 {ECO:0000313|Ensembl:ENSMPUP00000000540.1,
GN   ECO:0000313|RefSeq:XP_004753720.1, ECO:0000313|RefSeq:XP_004753721.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000000540.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000000540.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_004753720.1, ECO:0000313|RefSeq:XP_004753721.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_004753720.1,
RC   ECO:0000313|RefSeq:XP_004753721.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000459-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000459-2};
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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DR   EMBL; AEYP01034734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01034735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01034736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01034737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01034738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004753720.1; XM_004753663.2.
DR   RefSeq; XP_004753721.1; XM_004753664.2.
DR   STRING; 9669.ENSMPUP00000000540; -.
DR   Ensembl; ENSMPUT00000000552.1; ENSMPUP00000000540.1; ENSMPUG00000000546.1.
DR   GeneID; 101671512; -.
DR   KEGG; mpuf:101671512; -.
DR   CTD; 2162; -.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   GeneTree; ENSGT01050000244939; -.
DR   HOGENOM; CLU_013435_0_2_1; -.
DR   OMA; EEVCQPW; -.
DR   OrthoDB; 5344745at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:Ensembl.
DR   GO; GO:0072378; P:blood coagulation, fibrin clot formation; IEA:Ensembl.
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.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715}.
FT   DOMAIN          307..400
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        397
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         437
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         439
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         486
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         491
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   732 AA;  83304 MW;  6BCD84608743F866 CRC64;
     MSETSEPAFG GRRALPRNAS NAAEDDLPTV ELQGLVPRGV NLQDYLHVTS VHLFKERWDT
     NKVDHHTDKY ENNKLIVRRG QSFFIQIDFN RPYDPRRDLF RVEYVIGRYP QENKGTYIPV
     PIVPELQKGK WGAKVVMRED RSVRLSIQSS PECIVGKFRM YVAVWTPYGI LRTSRNPETD
     TYILFNPWCE EDAVYLGDEK EKEEYVLNDI GVIFYGDFND IKSRSWSYGQ FEDGILDACL
     YVMDKAEMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNVYAYGVPP SAWTGSVDIL
     LEYQSTKNPV RYGQCWVFAG VFNTFLRCLG IPARVVTNYF SAHDNDANLQ MDIFLEEDGN
     VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAIKH
     GHICFQFDAP FVFAEVNSDL IYVTAKKDGT HVVEAVDTAH IGKMIVTKEV GGDGIKDITD
     TYKFQEGQEE ERLALETALM YGAKKPINTD GILKPRSDVT MNFEVENAVL GRDFKLTITF
     QNNSHNRYTL SAYLSGNVVF YTGVSKTEFK KEAFEVTLEP LSLKKEEVLI RAGEYMSQLL
     EQAYLHFFVT ARVNETKDVL AKQKSTMLII PQLVIKVRGA RMVGSDMVVT VEFTNPLKET
     LRNVWIHLDG PGVLKPRRKM FREIQPNSTV QWEEVCRPWV SGHRKLIASM TSDALRHVYG
     ELDLQIQRQP SE
//
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