ID   G3VPQ0_SARHA            Unreviewed;       813 AA.
AC   G3VPQ0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
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:ENSSHAP00000005155.1};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000005155.1, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000005155.1, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000005155.1}
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   RefSeq; XP_003755945.1; XM_003755897.2.
DR   AlphaFoldDB; G3VPQ0; -.
DR   Ensembl; ENSSHAT00000005206.2; ENSSHAP00000005155.1; ENSSHAG00000004507.2.
DR   GeneID; 100918933; -.
DR   KEGG; shr:100918933; -.
DR   CTD; 7051; -.
DR   GeneTree; ENSGT01050000244939; -.
DR   HOGENOM; CLU_013435_0_2_1; -.
DR   InParanoid; G3VPQ0; -.
DR   OrthoDB; 5344745at2759; -.
DR   Proteomes; UP000007648; 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; 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:UP000007648}.
FT   DOMAIN          366..459
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        456
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         496
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         498
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         545
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         550
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   813 AA;  88966 MW;  65AC13BA88F71DC8 CRC64;
     MTDGSRSDVG RWGGSSWQPS VTPSPEPEPD TRSRGSGRSF WARCCSCCSC RGGADDDWGP
     EPAGPRGSGS RGSGRPGSRG SRGSGRPGSR GSGVNAAGDG VVRDGMLVVT GVDLMSGRSD
     QNRREHHTED YEYDDLIIRR GQPFLVTVSL SRPYSSSDRM ALELLIGANP EIGKGTHVII
     PVGKGGSGGW KAQVIKSNGQ HVDLKVHVSA NAIVGKFRFT VRTRTDAGEF QLPFDPRNEI
     YILFNPWCSD DPVYVEHESW RQEYVLNESG RIYYGTEAQI GERTWNYGQF DHGVLDACLY
     ILDRRGMPYA GRGDPVSVSR VISAMVNSLD DNGVLIGNWS GDYSRGTNPS AWVGSVEILL
     SYLRTGYSVP YGQCWVFAGV TTTVLRCLGI ATRTVTNYNS AHDTDTSLTM DIYFDENMKP
     LEHLNRDSVW NFHVWNDCWM RRSDLQSGFD GWQVVDATPQ ETSSGIFCCG PCSVESIKNG
     LVYMKYDTPF IFAEVNSDKV YWQRQDDGSF KIVYVEEKAI GTLICTKAVG SNMREDITHI
     YKHPEGSDAE RKAVETAAAH GSKPNIYSNR DSAEDVSVQV EAQDAVMGQD LVVNVVLTNR
     GSSRRTVKLH LYLSVTFYTG VTGPVFKDSK KEVALSPGSS ERVALPVAYS EYRPHLVDQG
     AMLLNVSGHV KENGQVIAKQ HTFRLRTPDL SLTVLGAAVV GQETEVQIIF RNPLPVTLTK
     VVFRLEGSGL QRPKVLNVGD IGGNETVTLR QTFVPVRPGR RQLIASLDSP QLSQVHGVIE
     VDVAPASGGN FFSGNRGSSR SGENVPMALR GEA
//