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
//