ID   H2Q827_PANTR            Unreviewed;       818 AA.
AC   H2Q827;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 69.
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:ENSPTRP00000010543.5,
GN   ECO:0000313|VGNC:VGNC:3303};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000010543.5, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000010543.5, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000010543.5}
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; AACZ04059403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_009425864.2; XM_009427589.2.
DR   RefSeq; XP_016781417.1; XM_016925928.1.
DR   AlphaFoldDB; H2Q827; -.
DR   PaxDb; 9598-ENSPTRP00000010543; -.
DR   Ensembl; ENSPTRT00000011396.5; ENSPTRP00000010543.5; ENSPTRG00000006209.5.
DR   GeneID; 452814; -.
DR   KEGG; ptr:452814; -.
DR   CTD; 7051; -.
DR   VGNC; VGNC:3303; TGM1.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   GeneTree; ENSGT01050000244939; -.
DR   HOGENOM; CLU_013435_0_2_1; -.
DR   InParanoid; H2Q827; -.
DR   OMA; WSGNYSD; -.
DR   OrthoDB; 5344745at2759; -.
DR   TreeFam; TF324278; -.
DR   Proteomes; UP000002277; Chromosome 14.
DR   Bgee; ENSPTRG00000006209; Expressed in cerebellar cortex and 4 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.
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:UP000002277}.
FT   DOMAIN          370..463
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        378
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        437
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         500
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         502
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         549
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         554
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   818 AA;  89805 MW;  54823034F4EEAD88 CRC64;
     MMDGPRSDVG RWGGNPLQPP TTPSPEPEPE PDGRSRRGGG GRSFWARCCG CCSCRNAADD
     DWGPEPSDSR GRGSSSGTRR PGSRGSDSRR PVSRGSGVNA AGDGTIREGM LVVNGVDLLS
     SRSDQNRREH HTDEYEYDEL IVRRGQPFHM LLLLSRTYES SDRITLELLI GNNPEVGKGT
     HVIIPVGKGG SGGWKAQVVK ASGQNLNLRV HTSPNAIIGK FQFTVRTQSD AGEFQLPFDP
     RNEIYILFNP WCPEDIVYVD HEDWRQEYVL NESGRIYYGT EAQIGERTWN YGQFDHGVLD
     ACLYILDRRG MPYGGRGDPV SVSRVISAMV NSLDDNGVLI GNWSGDYSRG TNPSAWVGSV
     EILLSYLRTG YSVPYGQCWV FAGVTTTVLR CLGLATRTVT NFNSAHDTDT SLTMDIYFDE
     NMKPLEHLNH DSVWNFHVWN DCWMKRPDLP SGFDGWQVVD ATPQETSSGI FCCGPCSVES
     IKNGLVYMKY DTPFIFAEVN SDKVYWQRQD DGSFKIVYVE EKAIGTLIVT KAISSNMRED
     ITYLYKHPEG SDAERKAVET AAAHGSKPNV YANRGSAEDV AMQVEAQDAV MGQDLMVSVM
     LTNHSSSRRT VKLHLYLSVT FYTGVSGTIF KETKKEVELA PGASDRVTMP VAYKEYRPHL
     VDQGAMLLNV SGHVKESGQV LAKQHTFRLR TPDLSLTLLG AAVVGQECEV QIVFKNPLPV
     TLTNVVFRLE GSGLQRPKIL NVGDIGGNET VTLRQSFVPV RPGPRQLIAS LDSPQLSQVH
     GVIQVDVAPA PGDGGFFSDA GGDSHLGETI PMASRGGA
//