ID   K7GLF7_PIG              Unreviewed;       826 AA.
AC   K7GLF7;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 74.
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:ENSSSCP00000028686.1,
GN   ECO:0000313|VGNC:VGNC:93936};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000028686.1, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000028686.1, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000028686.1,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HCZ90330.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000028686.1}
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; DQIR01034855; HCZ90330.1; -; Transcribed_RNA.
DR   RefSeq; XP_001927930.2; XM_001927895.4.
DR   STRING; 9823.ENSSSCP00000028686; -.
DR   PaxDb; 9823-ENSSSCP00000002179; -.
DR   Ensembl; ENSSSCT00000035836.4; ENSSSCP00000028686.1; ENSSSCG00000001993.6.
DR   VGNC; VGNC:93936; TGM1.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   GeneTree; ENSGT01050000244939; -.
DR   HOGENOM; CLU_013435_0_2_1; -.
DR   OMA; WSGNYSD; -.
DR   OrthoDB; 5344745at2759; -.
DR   Reactome; R-SSC-6809371; Formation of the cornified envelope.
DR   Proteomes; UP000008227; Chromosome 7.
DR   Bgee; ENSSSCG00000001993; Expressed in blood and 14 other cell types or tissues.
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; IBA:GO_Central.
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; 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.
DR   Genevisible; K7GLF7; SS.
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:UP000008227};
KW   Transferase {ECO:0000313|EMBL:HCZ90330.1}.
FT   DOMAIN          379..472
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        469
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         509
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         511
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         558
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         563
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   826 AA;  90879 MW;  57A0A33DE1F8DE4D CRC64;
     MPSPTPPSGT TDGARSDVGR WGGNPWQPPT TPSPEPEPEP DRRSRRDGRS FWARCCGCCS
     CRNTDDDWGP RGDRGAGSRD RGSGSGSRRP DSRGSDSRRP GSRGSGVNAA GDGTIREGML
     VVKGVDLLSS RSDQNRREHH TDEFEYDELI IRRGQPFYMV LLLSRPYESS DYVALELLIG
     NNPEVGKGTH IIIPVGKGGS GGWKAQVTKS SGQNLNLRVH TSPNAIIGKF QFTVRTRSEA
     GEFQLPFNPR NEIYILFNPW CPEDIVYVDH EDWRQEYVLN ESGRIYYGTE AQIGERTWNY
     GQFDHGVLDA CLYILDRRGM PYAGRGDPVS VSRVISAMVN SLDDNGVLIG NWSGDYSRGT
     NPSAWVGSVE ILLSYLRTGY SVPYGQCWVF AGVTTTVLRC LGLATRTVTN FNSAHDTDTS
     LTMDIYFDEN MKPLEHLNHD SVWNFHVWND CWMKRPDLPS GFNGWQVVDA TPQETSSGIF
     CCGPCSVESI KNGLVYMKYD TPFIFAEVNS DKVYWQRQND GSFKIVYVEE KAIGTLIVTK
     AIGSHMREDV THIYKHPEGS EAERKAVETA AAHGSKPNVY ATRDSAEDVA VQVEAQDAVM
     GQDLTVCVVL TNRGGSRRTV KLHLYLSVTF YTGVTGSVFK ESKKEVVLEP GASERVTMPV
     AYKEYQPHLV DQGAMLLNVS GHVKENGQVL AKQHTFRLRT PDLSLTLLGA AVVGQECEVQ
     IVFKNPLPVT LTNVVFRLEG SGLQRPKILN VGDIGGNETV TLRQTFVPVR PGPRQLIASL
     DSPQLSQVHG VIQVDVAPAA GGGVFSDARG NSRSGETIPM ASRGEA
//