ID G1PRJ0_MYOLU Unreviewed; 817 AA.
AC G1PRJ0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:ENSMLUP00000013759.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000013759.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000013759.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000013759.2}
RP IDENTIFICATION.
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 EMBL; AAPE02044603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PRJ0; -.
DR STRING; 59463.ENSMLUP00000013759; -.
DR Ensembl; ENSMLUT00000015106.2; ENSMLUP00000013759.2; ENSMLUG00000015102.2.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR GeneTree; ENSGT01050000244939; -.
DR HOGENOM; CLU_013435_0_2_1; -.
DR InParanoid; G1PRJ0; -.
DR OMA; WSGNYSD; -.
DR TreeFam; TF324278; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:Ensembl.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IEA:Ensembl.
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:UP000001074}.
FT DOMAIN 368..461
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..97
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 COMPBIAS 61..82
FT /note="Basic and acidic residues"
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; 89850 MW; 858DF90324469DEE CRC64;
MMDGPRSDVG RWGLSPWQPP TSPSPEPEPE PEPDRRSRRG SRSFWARCCS CCSCRSGADD
DWGTEPHRDR GGGRRPGSRG SDSRRPISRG SGVNAAGDGA IREGMLVVTG VDLMCSRSDQ
NRREHHTDEF EYDELILRRG QPFHMVLYLS RPYESSDRVI LELHIGNNPE VGKGTHVIIP
VGKGGSGGWK AQVTKSSGQN LNLRVHTSPN AIIGKFQFTV RTHSEAGEFL LPFDPHNEIY
ILFNPWCPGD AEDTVYVDRE 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 AIGTLIVTKA IGSNMQEDVT
HLYKHPEGSA AERKAVETAT AHGSKPNVYA TRDSAEDVAI QVEAQDAVMG QDLTVSVVLT
NRSSSSSRTV KLHLYLSVTF YTGVTGSVFK ENKKEVVLAP GASDRVTMPV SYQEYKPHLV
DQGAMLLNVS GHVKESGQVL AKQHTFRLRT PDLSLTLLGA AMVGQECEVQ IVFKNPLPIT
LTNVVFRLEG SGLQRPKILN VGDIGGNETV TLRQTFVPVR PGPRQLIASL DSPQLSQVHG
VIQVDVAPAS GSRGVFSDAG GSSRSGETIP MASRGGA
//
