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Database: UniProt
Entry: B4DU73_HUMAN
LinkDB: B4DU73_HUMAN
Original site: B4DU73_HUMAN 
ID   B4DU73_HUMAN            Unreviewed;       616 AA.
AC   B4DU73;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-NOV-2023, entry version 57.
DE   SubName: Full=cDNA FLJ58243, highly similar to Protein-glutamine gamma-glutamyltransferase 4 {ECO:0000313|EMBL:BAG62235.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG62235.1};
RN   [1] {ECO:0000313|EMBL:BAG62235.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Prostate {ECO:0000313|EMBL:BAG62235.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; AK300523; BAG62235.1; -; mRNA.
DR   AlphaFoldDB; B4DU73; -.
DR   PeptideAtlas; B4DU73; -.
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; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11590:SF70; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 4; 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.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Transferase {ECO:0000313|EMBL:BAG62235.1}.
FT   DOMAIN          192..285
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   ACT_SITE        200
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         322
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         324
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         374
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         379
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   616 AA;  69142 MW;  0D09CA96873C3904 CRC64;
     MGVPNEQSCV PARTPSDHYN WQATLQNESG KEVTVAVTSS PNAILGKYQL NVKTGNHILK
     SEENILYLLF NPWCKEDMVF MPDEDERKEY ILNDTGCHYV GAARSIKCKP WNFGQFEKNV
     LDCCISLLTE SSLKPTDRRD PVLVCRAMCA MMSFEKGQGV LIGNWTGDYE GGTAPYKWTG
     SAPILQQYYN TKQAVCFGQC WVFAGILTTV LRALGIPARS VTGFDSAHDT ERNLTVDTYV
     NENGEKITSM THDSVWNFHV WTDAWMKRPD LPKGYDGWQA VDATPQERSQ GVFCCGPSPL
     TAIRKGDIFI VYDTRFVFSE VNGDRLIWLV KMVNGQEELH VISMETTSIG KNISTKAVGQ
     DRRRDITYEY KYPEGSSEER QVMDHAFLLL SSEREHRRPV KENFLHMSVQ SDDVLLGNSV
     NFTVILKRKT AALQNVNILG SFELQLYTGK KMAKLCDLNK TSQIQGQVSE VTLTLDSKTY
     INSLAILDDE PVIRGFIIAE IVESKEIMAS EVFTSFQYPE FSIELPNTGR IGQLLVCNCI
     FKNTLAIPLT DVKFSLESLG ISSLQTSDHG TVQPGETIQS QIKCTPIKTG PKKFIVKLSS
     KQVKEINAQK IVLITK
//
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