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Database: UniProt
Entry: W5M2B5_LEPOC
LinkDB: W5M2B5_LEPOC
Original site: W5M2B5_LEPOC 
ID   W5M2B5_LEPOC            Unreviewed;       596 AA.
AC   W5M2B5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Transglutaminase 4 {ECO:0000313|Ensembl:ENSLOCP00000002523.1};
GN   Name=TGM4 {ECO:0000313|Ensembl:ENSLOCP00000002523.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002523.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000002523.1}
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};
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DR   EMBL; AHAT01012300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5M2B5; -.
DR   STRING; 7918.ENSLOCP00000002523; -.
DR   Ensembl; ENSLOCT00000002529.1; ENSLOCP00000002523.1; ENSLOCG00000002150.1.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   GeneTree; ENSGT01050000244939; -.
DR   HOGENOM; CLU_013435_1_0_1; -.
DR   InParanoid; W5M2B5; -.
DR   OMA; NKEFTCA; -.
DR   Proteomes; UP000018468; Linkage group LG11.
DR   Bgee; ENSLOCG00000002150; Expressed in pharyngeal gill and 6 other cell types or tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IBA:GO_Central.
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   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11590:SF70; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 4; 1.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 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   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   DOMAIN          161..254
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        251
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         291
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         293
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         344
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         349
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   596 AA;  66627 MW;  4C622D3B34A0189D CRC64;
     IEVEVKLAPN AIVGKYSFKV KIGEDYTYET ENGHFYVLFN PWCEDDDVHL PEENARQEYV
     LKDTGYIYTG SVNDITGKPW NFGQFERNVL DCCLYLLDKK GLKQSARREP VRVARAMSAV
     VNSNDENGVL YGNWSGNYAD GTPPVYWTGS SAILQQYYES REPVRYGQCW VFSGVLTTVM
     RCLGIPSRSV TNFCSAHDTE GNLTIDIYLN QKGEKLNDIT TDSVWNFHMW NDVWMKRPDL
     PEGYDGWQAL DATPQEESEG IFQCGPSPLS AIKKGEVYLA YDTKFIFAEV NADRIIWLVE
     NPKTDQQKTT RLRAHYSAVG KNISTKALGK DERQDITELY KFPEGTPEER KVMERASAVC
     FPDVPIPTPQ SIQLGFESDK SFLLGSPITF QISLSNNSSQ SQAVALTAAC QLQTYNGKTL
     ATIKALKQEV TVMANACTSV PVVIEASDYL QHLSMASDDL LVRVTAVGEN KDSNSVFADD
     TTLSFKYPPI TVDMPATAKT GEPFTCTFTF KNNIGVVMES CKLHVEGLGL FRLETFDQGN
     VRAGGIFRSK IICTPDRRGE RKIIAKITSD QLDDINGYLV LTCNQKQCII KTGYSS
//
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