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Database: UniProt/TrEMBL
Entry: G1RZJ6_NOMLE
LinkDB: G1RZJ6_NOMLE
Original site: G1RZJ6_NOMLE 
ID   G1RZJ6_NOMLE            Unreviewed;       808 AA.
AC   G1RZJ6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-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:ENSNLEP00000018673.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000018673.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000018673.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000018673.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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; ADFV01192214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003260733.1; XM_003260685.3.
DR   AlphaFoldDB; G1RZJ6; -.
DR   STRING; 61853.ENSNLEP00000018673; -.
DR   Ensembl; ENSNLET00000019607.2; ENSNLEP00000018673.1; ENSNLEG00000015377.2.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   GeneTree; ENSGT01050000244939; -.
DR   HOGENOM; CLU_013435_0_2_1; -.
DR   InParanoid; G1RZJ6; -.
DR   OMA; WSGNYSD; -.
DR   TreeFam; TF324278; -.
DR   Proteomes; UP000001073; Chromosome 22a.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
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:0030216; P:keratinocyte differentiation; IEA:Ensembl.
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:UP000001073}.
FT   DOMAIN          360..453
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          62..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        368
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        450
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         490
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         492
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         539
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         544
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   808 AA;  89055 MW;  B389BA8F249F6EA4 CRC64;
     MMDGPRSDVG RWGGNPLQPP TTPSPEPEPE PEPDRRSRRG GGGRSFWARC CGCCSCRNAV
     DDDWGPEPSD SRGRGSSSGT RRPVSRGSGV NAAGDGTIRE GMLVVNGVDL LSSRSDQNRR
     QHHTEEYEYD ELIVRRGQPF HMLLLLSRTY ESSDRITLEL LIGNNPEVGK GTHVIIPVGK
     GGSGGWKAQV VKASGQNLNL RVHTSPNAII GKFQFTVRTQ SDAGEFQLPF DPRNEIYILF
     NPWCPEDIVY VDHEDWRQEY VLNESGRIYY GTEAQIGERT WNYGQFDHGV LDACLYILDR
     RGMPYGGRGD PVSVSRVISA MVNSLDDNGV LIGTGSGDYS RAPTHQRGGQ REILLSYLRG
     LFRPYGQCWV FAGVTTTVLR CLGLATRTVT NFNSAHDTDT SLTMDIYFDE NMKPLEHLNH
     DSVWNFHVWN DCWMKRPDLP SGFDGWQVVD ATPQETSSGI FCCGPCSVES IKNGLVYMKY
     DTPFIFAEVN SDKVYWQRQD DGSFKIVYVE EKAIGTLIVT KAIGSNMRED ITYLYKHPEG
     SDAERKAVET AAAHGSKPNV YANRGSAEDV AMQVEAQDAV MGQDLMVSVM LTNHSSSRRT
     VKLHLYLSVT FYTGVSGTIF KETKKEVELA PGASDRVTMP VAYKEYRPHL VDQGAMLLNV
     SGHVKESGQV LAKQHTFRLR TPDLSLTLLG AAVVGQECEV QIVFKNPLPV TLTNVVFRLE
     GSGLQRPKIL NVGDIGGNET VTLRQTFVPV RPGPRQLIAS LDSPQLSQVH GVIQVDVAPA
     PGDRGFFSDA GGDSHLGETI PMASRGGA
//
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