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
//