ID A0A1S3EMU6_DIPOR Unreviewed; 637 AA.
AC A0A1S3EMU6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Protein-glutamine gamma-glutamyltransferase 5 isoform X2 {ECO:0000313|RefSeq:XP_012865681.1};
GN Name=Tgm5 {ECO:0000313|RefSeq:XP_012865681.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012865681.1};
RN [1] {ECO:0000313|RefSeq:XP_012865681.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012865681.1};
RG RefSeq;
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 RefSeq; XP_012865681.1; XM_013010227.1.
DR AlphaFoldDB; A0A1S3EMU6; -.
DR GeneID; 105981165; -.
DR CTD; 9333; -.
DR OrthoDB; 5344745at2759; -.
DR Proteomes; UP000081671; Unplaced.
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; 2.
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:SF38; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 5; 1.
DR Pfam; PF00927; Transglut_C; 2.
DR Pfam; PF01841; Transglut_core; 1.
DR Pfam; PF00868; Transglut_N; 1.
DR PIRSF; PIRSF000459; TGM_EBP42; 2.
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 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:UP000081671}.
FT DOMAIN 188..281
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 383..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 278
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 637 AA; 71984 MW; 1E56BC71D3E9487E CRC64;
MAQGLEVAFV DFQSSRSNMQ HHTEEISLDH LVVRRGQPFN ITLYFRNQGF QPGLDSIIFV
AETGDAVYLD SEPQRQEYVV NDYGFIYQGN KNWIRPCPWN YGQFEENILD ICLELLDKSL
HFQIDPSTDC ALRGSPVYIS RVVCAMINSN DDNGVLNGNW SENYMDGINP AEWTGSVAIL
KQWHATGCQP VRYGQCWVFA AVMCTVMRCL GIPTRVITNF DSGHDTDGNL IIDEYYDNTG
RILENKKKDT VWNYHVWNEC WMDRKDLPSG YGGWQVLDAT PQETSNGLYC CGPASVRAIK
EGEVNLNYDT RFAFSMVNAD CMSWLVQGGK EQKLHQDTTT VGNFISTKSI QSDQRDDITE
NYKYEEGSPQ ERQVYYKALQ KLKDGRSQGS DSASSVPSRR MPPSQDTPRS LDTPALQPSS
VIQVSLKFKL LDPPNMGQDI NFALLALNMS PQFKDLKVNL SAQSLLHDGS PLWPFWQDTA
FITLFPEEAK TYPCKIPYSQ YSQYLSTDKL IRISALGEEK SSPEKILVNK IITLTFPGII
INVLGQAIVN QLLSIQVIFS NPLSEPVEDC VLTLEGSGFF KKQLRILIGD LKPHHKATIT
LKTIPFKSGQ RQIQANLSSN KFKDIKGYKN VYVDFGL
//
