TGM1_CANLF
ID TGM1_CANLF Reviewed; 815 AA.
AC Q9GLK0;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase K;
DE EC=2.3.2.13;
DE AltName: Full=Epidermal TGase;
DE AltName: Full=Transglutaminase K;
DE Short=TG(K);
DE Short=TGK;
DE Short=TGase K;
DE AltName: Full=Transglutaminase-1;
DE Short=TGase-1;
GN Name=TGM1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11474183; DOI=10.1159/000056952;
RA Credille K.M., Venta P.J., Breen M., Lowe J.K., Murphy K.E.,
RA Ostrander E.A., Galibert F., Dunstan R.W.;
RT "DNA sequence and physical mapping of the canine transglutaminase 1 gene.";
RL Cytogenet. Cell Genet. 93:73-76(2001).
CC -!- FUNCTION: Catalyzes the cross-linking of proteins and the conjugation
CC of polyamines to proteins. Responsible for cross-linking epidermal
CC proteins during formation of the stratum corneum. Involved in cell
CC proliferation (By similarity). {ECO:0000250|UniProtKB:P22735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10024};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with PLAAT4. {ECO:0000250|UniProtKB:P22735}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P22735}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P22735}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:P22735}.
CC -!- PTM: The membrane anchorage region possesses a cluster of five
CC cysteines within which fatty acid(s) may become thioester-linked. It is
CC subject to phorbol ester-stimulated phosphorylation and is
CC hypersensitive to proteolysis, which releases the enzyme in a soluble
CC form. {ECO:0000250|UniProtKB:P22735}.
CC -!- PTM: Tyrosine-phosphorylated. {ECO:0000250|UniProtKB:Q9JLF6}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
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DR EMBL; AF262219; AAG13662.1; -; mRNA.
DR RefSeq; NP_001003079.1; NM_001003079.1.
DR AlphaFoldDB; Q9GLK0; -.
DR SMR; Q9GLK0; -.
DR STRING; 9612.ENSCAFP00000017949; -.
DR PaxDb; Q9GLK0; -.
DR PRIDE; Q9GLK0; -.
DR GeneID; 403630; -.
DR KEGG; cfa:403630; -.
DR CTD; 7051; -.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR InParanoid; Q9GLK0; -.
DR OrthoDB; 297055at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
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:0018149; P:peptide cross-linking; IBA:GO_Central.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.90.260.10; -; 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 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; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Calcium; Keratinization; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..815
FT /note="Protein-glutamine gamma-glutamyltransferase K"
FT /id="PRO_0000213700"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 434
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 497
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 551
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLF6"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22735"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22735"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22735"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22735"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLF6"
SQ SEQUENCE 815 AA; 89757 MW; 82C49D15DDD25BE4 CRC64;
MDGPRSDVGR WGGNPWQPPT TPSPEPEPEP EPERRSRRGG RSFWARCCGC CSCRNRADDD
WGPEPHRDRG SGSGRRRPDS RGSDSRRPGS RASGVNAAGD GTIREGMLVV TGVDLLSSRS
DQNRREHHTD EFEYDELIIR RGQPFHMVLH FSRPYESSDR VALELLIGNN PEVGKGTHVI
IPVGKGGSGG WKAQVTKASG QNLNLRVHTS PNAIIGKFQF TVRTHSEAGE FQLPFDPHNE
IYILFNPWCP EDIVYVDHED WRQEYVLNES GRIYYGTEAQ IGERTWNYGQ FDHGVLDACL
YILDRRGMPY GGRGDPVSVS RVISAMVNSL DDNGVLIGNW SGDYSRGTNP SAWVGSVEIL
LSYLRTGYSV PYGQCWVFAG VTTTVLRCLG LATRTVTNFN SAHDTDTSLT MDIYFDENMK
PLEHLNHDSV WNFHVWNDCW MKRPDLPSGF DGWQVVDATP QETSSGIFCC GPCSVESIKN
GLVYMKYDTP FIFAEVNSDK VYWQRQDDGS FKIVYVEEKA IGTLIVTKAV GSNMQDDVTH
IYKHPEGSEA ERKAVETAAA HGSKPNVYTN RDSAEDVALQ VEAQDAVMGQ DLTVSVVLTN
RGSSTRTVKL HLYLSVTFYT GVTGPVFKES KKEVVLAPGA TERVSMPVAY KEYRPQIVDQ
GSMLLNVSGH VKENGQVLAK QHTFRLRTPD LSLTLLGAAV VGQECEVQIV FKNPLPVTLT
NVVFRLEGSG LQRPKILNVG DIGGNETVTL HQKFVPVRPG PRQLIASLDS PQLSQVHGVI
QVDVAPAPGG GGFFSNAGGN SPLGETIPMA SRGGA
