ID G3TGS0_LOXAF Unreviewed; 805 AA.
AC G3TGS0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase K {ECO:0000256|ARBA:ARBA00040559};
DE EC=2.3.2.13 {ECO:0000256|ARBA:ARBA00024222};
DE AltName: Full=Epidermal TGase {ECO:0000256|ARBA:ARBA00043229};
DE AltName: Full=Transglutaminase K {ECO:0000256|ARBA:ARBA00041726};
DE AltName: Full=Transglutaminase-1 {ECO:0000256|ARBA:ARBA00041651};
GN Name=TGM1 {ECO:0000313|Ensembl:ENSLAFP00000013696.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000013696.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000013696.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013696.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000013696.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000013696.2};
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 -!- SUBUNIT: Interacts with PLAAT4. {ECO:0000256|ARBA:ARBA00038573}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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DR Ensembl; ENSLAFT00000016311.2; ENSLAFP00000013696.2; ENSLAFG00000016309.2.
DR GeneTree; ENSGT01050000244939; -.
DR HOGENOM; CLU_013435_0_2_1; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
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:SF49; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE K; 1.
DR Pfam; PF00927; Transglut_C; 2.
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 Keratinization {ECO:0000256|ARBA:ARBA00023249};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT DOMAIN 358..451
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 366
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 425
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 448
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 488
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 537
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 805 AA; 88699 MW; 7C47EB728C2EAFA2 CRC64;
MDGPRSDVGR WGRSPWQPTA TPSPEPEPEP DRRSRGSGRS FWARCCSCCS SRNVDDDWGR
GSGARVSGPD SRGSDSHRPV SRGTGVNAAG DGTVREGMLV VTGVDLLSSR SDQNRREHHT
DEFEYNELIV RRGQPFDIVL FLSRPYGSSD HITLELLIGN NPEVGKSTHV IIPVGKGGSG
GWKAQVIKAN GQNLNLRVYT SPNSIIGKFQ FTVRTHSDAG EFQLPFDPRN EIYILFNPWC
PEDIVYVDHE DWRQEYVLNE SGRIYYGTEA QIGERTWNYG QFDHGVLDAC LCILDRRGMP
YGGRGDPVSV SRVISAMVNS LDDNGVLIGN WSGDYSRGTN PSAWVGSVEI LLSYLRTGYS
VPYGQCWVFA GVTTTVLRCL GLATRTVTNF NSAHDTDTSL TMDIYFDENM KPLEHLNRDS
VWNFHVWNDC WMKRPDLPSG FNGWQVVDAT PQETSSGIFC CGPCSVESIK NGLVYMKYDT
PFIFAEVNSD KVYWQRQDDG SFKIVYVEEK AIGTLIITKA IGSNMRDDVT HLYKHPEGSE
AERKAVETAA AHGSKPNVYA TRDSAEDVAV QVETQDVVTG QDLTVCVVLS NRGSSRRTVK
LHLYLSVTFY TGVTGPVFKD SKKEVVLEPG ASERVVMPVA YQEYQPHLVD QGAMLLNISG
HVKENGQVLA KQHTFRLRTP DLSLTLLGAA VVGQECEVQI VFKNPLPVTL TNVVFRLEGS
GLQRPKILNV GXXXXXXXXX XRQTFMPVRP GPRQLIASLD SPQLSQVHGV IQVDVAPASG
GWALSDPGGD SHSGETIPMA SRGGA
//
