ID   H2VAN1_TAKRU            Unreviewed;       672 AA.
AC   H2VAN1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Coagulation factor XIII A chain-like {ECO:0000313|Ensembl:ENSTRUP00000046272.2};
GN   Name=LOC101071398 {ECO:0000313|Ensembl:ENSTRUP00000046272.2};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000046272.2, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000046272.2, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000046272.2}
RP   IDENTIFICATION.
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   AlphaFoldDB; H2VAN1; -.
DR   STRING; 31033.ENSTRUP00000078184; -.
DR   Ensembl; ENSTRUT00000046428.3; ENSTRUP00000046272.2; ENSTRUG00000018071.3.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   GeneTree; ENSGT01050000244939; -.
DR   HOGENOM; CLU_013435_0_2_1; -.
DR   TreeFam; TF324278; -.
DR   Proteomes; UP000005226; Chromosome 8.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
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; 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; 1.
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.
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:UP000005226}.
FT   DOMAIN          301..394
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        368
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         431
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         433
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         480
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         485
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   672 AA;  75885 MW;  23F8902A5D672D12 CRC64;
     FNSGVGAPSA GRKPLPTPVL RNSGPCSELF LPPPPHPADY LDIVAVDMMS QSDGVNKQQH
     RTMFYNSNYL IVRRGQEFHV KLTFNRPYNP KEDKFALEFV IGANPDYSKG TYIPVFPNKE
     RQSRWAGRIA DSSNNDVTVG ITPLANCIVG KYHMYIAVMT PFGIRRTRKD PVRDLYILFN
     PWSPADDVFL DDEPERQECV MNEMGIIYHG AYDDIAERQW NYGQFNYGVL DACLYIMDRS
     EMPITNRGDP IKVTRKASAM INSRDDDGVL VGNWSGDYTY GVAPTSWTGS TEILLTYASS
     RMPVSYAQCW VYAAVFNTFL RCLGIPSRVV TNYYSAHDND GNLKTDIILD ENGKIDRSRT
     RDSIWNYHCW NECYMTRPDL PFGFGGWQVV DATPQETSDG MYRCGPASVQ AIKHGEMCYP
     FDAAFVFAEV NSDVVFYSRG KDGAMQPVRV NQTHVGRMVL TKAPGATTRR DITSQYKFPE
     GTSEERTVLE KAEGFGCHRE KSRPPEADVD LVLPTLEVPV GQDFELSLEF VNRSDQRRVV
     EAYISGNVVF YTGVTSAEFM LRDPTVTMKP NETVKETVVV ESKKYMKHLV EQANLHFIIT
     GKVKETGQIV TAMKVVALHN PKLSVKVSGE NRVSEEMMAT VEFTNPFSFA LADVYIRMEG
     PGVMMPTYKY YR
//