ID A0A1S3EPN7_DIPOR Unreviewed; 712 AA.
AC A0A1S3EPN7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protein-glutamine gamma-glutamyltransferase Z {ECO:0000313|RefSeq:XP_012865437.1};
GN Name=Tgm7 {ECO:0000313|RefSeq:XP_012865437.1};
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_012865437.1};
RN [1] {ECO:0000313|RefSeq:XP_012865437.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012865437.1};
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_012865437.1; XM_013009983.1.
DR AlphaFoldDB; A0A1S3EPN7; -.
DR STRING; 10020.ENSDORP00000013167; -.
DR GeneID; 105980994; -.
DR KEGG; dord:105980994; -.
DR CTD; 116179; -.
DR InParanoid; A0A1S3EPN7; -.
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; 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:SF41; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE Z; 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 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 273..366
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 340
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 363
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 712 AA; 79661 MW; 3C6B3E5DAACCC6A9 CRC64;
MDPVADLELR SVDLQTPKNN KDHHTQEMGV KHLILRRGQA FNIRLNFNRP FQPRKDHITF
VAETGPKPTE LLGTQAIFSF NQTQTQHGNV WSTSDFILDS NSLQVSIFSS ASAVIGHYML
KLEISQGQGH SATYPVGAFI LLFNPWSPED DVYLPSEILL QEYIMSDYGF VYKGNKSAIT
SWPWNYGQFE EGILDICFEI LNKSLYFLMN PSKDCSQRNN VVYVCRVVSA MINSNDDNGV
LQGNWGEDYS TGISPLEWNG SVAILRQWSA SGGQPVKYGQ CWVFASVMCT VMRCLGVPTR
VVSNFRSAHS MDGNLTIDTY YDQNAEMLPT QKPDKVWNFH VWNECWMIRN DLPPGYNGWQ
VLDPTPQQTS SGMFCCGPAS VRAVREGDVH LDYDTSLVFA EVNADEVIWL LEKGQAQEIL
AHDTSSIGKE ISTKMVASDH RQDITNSYKY PEGSPEERSV FMKASRTLLG PQRASSSLLD
LLGSGEFEDP PVRLQLHLAR TPEWGQDVLF ILHVQTVPDR AHTQAPIRLL VHFCAQALLH
GGGARPPLWR QMVDLNVDVG KEIQSLLLLP YSNYREKLTD EKQIRVSGIA KVEGTGRNIL
VLKDFCLQPP RLTIEVSEKA VVGKILRVHI TLTNTLTVAL ANCVMVLEGS GLLSGQISEN
FGTLSPGHTI KVHLELYPIK AGPRQLQVLI SSNEVKEIKG YKRIFVAEAT TS
//
