ID A2ART8_MOUSE Unreviewed; 710 AA.
AC A2ART8;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 2.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Transglutaminase 7 {ECO:0000313|Ensembl:ENSMUSP00000106303.3};
GN Name=Tgm7 {ECO:0000313|Ensembl:ENSMUSP00000106303.3,
GN ECO:0000313|MGI:MGI:2151164};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000106303.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000106303.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000106303.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000106303.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000106303.3};
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};
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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DR RefSeq; NP_001153896.1; NM_001160424.1.
DR AlphaFoldDB; A2ART8; -.
DR SMR; A2ART8; -.
DR STRING; 10090.ENSMUSP00000106303; -.
DR PaxDb; 10090-ENSMUSP00000106303; -.
DR ProteomicsDB; 348997; -.
DR Antibodypedia; 23856; 157 antibodies from 29 providers.
DR Ensembl; ENSMUST00000110675.3; ENSMUSP00000106303.3; ENSMUSG00000079103.4.
DR GeneID; 640543; -.
DR KEGG; mmu:640543; -.
DR UCSC; uc012ccl.1; mouse.
DR AGR; MGI:2151164; -.
DR CTD; 116179; -.
DR MGI; MGI:2151164; Tgm7.
DR VEuPathDB; HostDB:ENSMUSG00000079103; -.
DR eggNOG; ENOG502QTRA; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR HOGENOM; CLU_013435_2_1_1; -.
DR InParanoid; A2ART8; -.
DR OMA; TDHITFV; -.
DR OrthoDB; 5344745at2759; -.
DR PhylomeDB; A2ART8; -.
DR TreeFam; TF324278; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2ART8; Protein.
DR Bgee; ENSMUSG00000079103; Expressed in zone of skin and 10 other cell types or tissues.
DR ExpressionAtlas; A2ART8; baseline and differential.
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 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:UP000000589}.
FT DOMAIN 271..364
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 338
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 361
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 710 AA; 79847 MW; CD5DE0D9376AF6C3 CRC64;
MDPVAALELR SVELQIPRNN KDHHTEDLGL SKLILRRGQI FILTIVFSRP FQPQKDHLTF
VAETGPEPTE LLGTRATFFL AQTRPENVWS ASDFMIDSNS LQVSIFSPAS AVIGHYTLKL
EISQGQGPGV TYPLGNFILL FNPWSTEDDV YLPSETLLRE YIMSDYGFIY KGQTNSITSR
PWNYGQFEED IVDICFEILN KSLYFLKNPS KDHSQRNNVV YVCRVVSAMI NSNDDSGVLQ
GNWGEDYSQG TSPLEWNGSV AILRQWSAKG GQPVKYGQCW VFASVMCTVM RCLGVPTRVV
SNFHSAHNTD GNLTIDTYYD RTAEMLTAQR PDKIWNFHVW NECWMIRKDL PPGYNGWQVL
DPTPQQTSSG LFCCGPASVK AIKEGDVQLP YDTPFVYAEV NADEVVWLFE GGQVQEILAH
NTSYIGKAIS TKMVGSDERL DITSSYKYPE GSSEERSAFI KASWKLLEPR RNASSLLDLL
GSENLKAKPV RLQLHLVRAP MWGQDLPLML YVQRVPVRDH VQGSVGLTVR FCAQALLHGG
GTRKPFWRHI VHLNVDFEKE LQWPFLLPYS SYRDKLTDER LIRVAGIAEV EETGQFILVL
KDFSLEPPHL SIEVFERAEV GKALDIHITL TNTLMVPLNN CTMVLEGSGL INGQMTKDLG
TLMAGHTIRI HLELYPIKAG PHQLQVLISS SEVKEIKGYK DILVAAAPAS
//
