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
//