ID   F6PW39_HORSE            Unreviewed;       821 AA.
AC   F6PW39;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 76.
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:ENSECAP00000015519.3,
GN   ECO:0000313|VGNC:VGNC:24060};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000015519.3, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000015519.3, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000015519.3,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000015519.3}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000015519.3};
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   RefSeq; XP_001489215.1; XM_001489165.3.
DR   RefSeq; XP_014589564.1; XM_014734078.1.
DR   AlphaFoldDB; F6PW39; -.
DR   SMR; F6PW39; -.
DR   STRING; 9796.ENSECAP00000015519; -.
DR   PaxDb; 9796-ENSECAP00000015519; -.
DR   Ensembl; ENSECAT00000018986.4; ENSECAP00000015519.3; ENSECAG00000017485.4.
DR   GeneID; 100054584; -.
DR   KEGG; ecb:100054584; -.
DR   CTD; 7051; -.
DR   VGNC; VGNC:24060; TGM1.
DR   GeneTree; ENSGT01050000244939; -.
DR   HOGENOM; CLU_013435_0_2_1; -.
DR   InParanoid; F6PW39; -.
DR   OMA; WSGNYSD; -.
DR   OrthoDB; 5344745at2759; -.
DR   TreeFam; TF324278; -.
DR   Proteomes; UP000002281; Chromosome 1.
DR   Bgee; ENSECAG00000017485; Expressed in zone of skin and 23 other cell types or tissues.
DR   ExpressionAtlas; F6PW39; baseline.
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:UP000002281}.
FT   DOMAIN          373..466
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        440
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        463
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         503
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         505
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"
FT   BINDING         557
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   821 AA;  90387 MW;  7912B3E509F98BA7 CRC64;
     MTDGPRSDVG RWGGNAWQPP TTPSPEPEPE PEPDSRSRRG GRSFWARCCG CCSCRNDDDW
     GREPYRDRGS GSRGRGSRSG GRRPDSRGSD SRQPGSRGSG VNAAGDGTIR EGMLVVTGVD
     LLSSRSDQNR REHHTDEFEY DELIVRRGQP FHMVLLLSRP YESSDHIALE LLIGNNPEVG
     KGTHVIIPVG KGGSGGWKAQ VTKANGQNLN LRVHTSPNAI IGKFQFTVRT RTEAGEFQLP
     FDPHNEIYIL FNPWCPEDIV YVDHEDWRQE YVLNESGRIY YGTEAQIGER TWNYGQFDHG
     VLDACLYILD RRGMPYGGRG DPVNVSRVIS AMVNSLDDNG VLIGNWSGDY SRGTNPSAWV
     GSVEILLSYL RTGYSVPYGQ CWVFAGVTTT VLRCLGLATR TVTNFNSAHD TDTSLTMDIY
     FDENMKPLEH LNHDSVWNFH VWNDCWMKRP DLPSGFDGWQ VVDATPQETS SGIFCCGPCS
     VESIKNGLVY MKYDTPFIFA EVNSDKVYWQ RQDDGSFKIV YVEEKAIGTL IITKAIGSSM
     REDVTHIYKH PEGSEAERKA VETAAAHGSK PNVYANRDTA EDVAMQVEAQ DAVMGQDLTV
     SVVLTNRGSS RRTVKLHLYL SVTFYTGVTG SVFKESKKEV VLQPGASDRV AMPVAYTEYK
     PHLVDQGAML LNVSGHVKES GQVLAKQHTF RLRTPDLSLS LLGAAVVGQE CEVQIVFKNP
     LPVTLTNVVF RLEGSGLQRP KILNVGDIGG NETVTLRQTF VPVRPGPRQL IASLDSPQLS
     QVHGVIQVDV APAPGGGSFF SDARGNSRSG ETIPMASRGG A
//