ID G3T574_LOXAF Unreviewed; 732 AA.
AC G3T574;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Coagulation factor XIII A chain {ECO:0000313|Ensembl:ENSLAFP00000008563.4};
GN Name=F13A1 {ECO:0000313|Ensembl:ENSLAFP00000008563.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000008563.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000008563.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008563.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000008563.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000008563.4};
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_003417911.1; XM_003417863.2.
DR AlphaFoldDB; G3T574; -.
DR STRING; 9785.ENSLAFP00000008563; -.
DR Ensembl; ENSLAFT00000010218.4; ENSLAFP00000008563.4; ENSLAFG00000010217.4.
DR GeneID; 100655577; -.
DR KEGG; lav:100655577; -.
DR CTD; 2162; -.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR GeneTree; ENSGT01050000244939; -.
DR HOGENOM; CLU_013435_0_2_1; -.
DR InParanoid; G3T574; -.
DR OMA; EEVCQPW; -.
DR OrthoDB; 5344745at2759; -.
DR TreeFam; TF324278; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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:UP000007646}.
FT DOMAIN 307..400
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..25
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; 83093 MW; 2F630356549F034C CRC64;
MSETTTATFG GRRSVPPNNS NAAEDDLPTM ELQGLVPRGV SLQDYLNVVN VYLFKERWDS
NKVDHHTDKY DNNKLIVRRG QPFYIQIDFN RAYDPRRDLF RVEYVIGRYP QENKGTYIPV
PVVPELQKGK WGAKVITRED KSVRLSVQPS PGCIVGKFRM YVAVWTPYGI IRTSRNPETD
TYILFNPWCE EDAVYLDDER QREEYVLNDI GVIFHGDFKD IKNRSWSYGQ FEDGILDACL
YVMDRAKMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNIYAYGVPP SAWTGSVDIL
LEYQSSKSPV RYGQCWVFAG VFNTFLRCLG IPARVVTNYF SAHDNDANLQ MDVFLEEDGN
VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQVVDSTP QENSDGMYRC GPASVQAIKH
GHVCFQFDAP FVFAEVNSDL VYITVKKDGT HVVETVDSTH IGKLIVTKEI GGDGVQDITD
TYKFQEGQEE ERLALETALM YGAKKRINTE GILKPRSKVD MNFGVENAVL GKDFKITITF
QNNSPNRYTI SAYLSGNITF YTGVAKVEFK KETFDVVLEP LSFKKEEVLV RAGEYMGQLL
EQASLHFFVT ARVNETQDIL AKQKSIVLTI PKVIIKVHGA KVVGSDMVVT VEFTNPLKET
LQNVWIYLDG PGLTRPRRKL FREIRPNATV QWEEVCRPWV SGRRKLIASM TSDTLRHVYG
ELGVEIQRQP SV
//
