ID S7MJK3_MYOBR Unreviewed; 817 AA.
AC S7MJK3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=D623_10003703 {ECO:0000313|EMBL:EPQ03550.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ03550.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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 EMBL; KE161388; EPQ03550.1; -; Genomic_DNA.
DR RefSeq; XP_005859639.1; XM_005859577.2.
DR RefSeq; XP_014389752.1; XM_014534266.1.
DR AlphaFoldDB; S7MJK3; -.
DR GeneID; 102249978; -.
DR KEGG; myb:102249978; -.
DR CTD; 7051; -.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR OrthoDB; 5344745at2759; -.
DR Proteomes; UP000052978; 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; 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.
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:UP000052978};
KW Transferase {ECO:0000313|EMBL:EPQ03550.1}.
FT DOMAIN 368..461
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 376
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 435
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 458
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 817 AA; 89752 MW; B335E318D1276272 CRC64;
MMDGPRSDVG RWGVSPWQPP TSPSPEPEPE PDRRSRRGSR SFWARCCSCC SCRSGADDDW
GTEPHRDRGG GSSSGGRRPG SRGSDSRRPI SRGSGVNAAG DGAIREGMLV VTGVDLMCSR
SDQNRREHHT DEFEYDELIL RRGQPFHMVL YLSRPYESSD RVILELHIGN NPEVGKGTHV
IIPVGKGGSG GWKAQVTKSS GQNLNLRVHT SPNAIIGKFQ FTVRTHSEAG EFLLPFDPHN
EIYILFNPWC PEDIVYVDRE DWRQEYVLNE SGRIYYGTEA QIGERTWNYG QFDHGVLDAC
LYILDRRGMP YGGRGDPVSV SRVISAMVNS LDDNGVLIGN WSGDYSRGTN PSAWVGSVEI
LLSYLRTGSS VPYGQCWVFA GVTTSVLRCL GLATRTVTNF NSAHDTDTSL TMDIYFDENM
KPLEHLNHDS VWNFHVWNDC WMKRPDLPSG FDGWQVVDAT PQETSSGIFC CGPCSLQSIK
NGLVYMKYDT PFIFAEVNSD KVYWQRQDDG SFKIVYVEEK AIGTLIITKA IGSNMQEDVT
HLYKHPEGSA AERKAVETAT AHGSKPNVYA TRDSAEDVAI QVEAQDAVMG QDLTVSVVLT
NRSSSSSRTV KLHLYLSVTF YTGVTGSVFK ENKKEVVLAP GASDRVTMPV AYQEYKPHLV
DQGAMLLNVS GHVKESGQVL AKQHTFRLRT PDLSLTLLGA AMVGQECEVQ IVFKNPLPIT
LTNVVFRLEG SGLQRPKILN VGDIGGNETV TLRQTFVPVR PGPRQLIASL DSPQLSQVHG
VIQVDVAPAS GSRGVFSDAG GSSRSGETIP MASRGGA
//
