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Database: UniProt/SWISS-PROT
Entry: TGM1_CANLF
LinkDB: TGM1_CANLF
Original site: 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   07-JUN-2017, entry version 97.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11474183;
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
RT   gene.";
RL   Cytogenet. Cell Genet. 93:73-76(2001).
CC   -!- FUNCTION: Catalyzes the cross-linking of proteins and the
CC       conjugation of polyamines to proteins. Responsible for cross-
CC       linking epidermal proteins during formation of the stratum
CC       corneum. Involved in cell proliferation (By similarity).
CC       {ECO:0000250|UniProtKB:P22735}.
CC   -!- CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N(5)-
CC       alkylglutamine + NH(3). {ECO:0000255|PROSITE-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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
DR   EMBL; AF262219; AAG13662.1; -; mRNA.
DR   RefSeq; NP_001003079.1; NM_001003079.1.
DR   UniGene; Cfa.3494; -.
DR   ProteinModelPortal; Q9GLK0; -.
DR   SMR; Q9GLK0; -.
DR   STRING; 9615.ENSCAFP00000017949; -.
DR   PaxDb; Q9GLK0; -.
DR   PRIDE; Q9GLK0; -.
DR   GeneID; 403630; -.
DR   KEGG; cfa:403630; -.
DR   CTD; 7051; -.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; Q9GLK0; -.
DR   KO; K05619; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
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; IPR002931; Transglutaminase-like.
DR   InterPro; IPR023608; Transglutaminase_animal.
DR   InterPro; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
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; SSF81296; SSF81296; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Calcium; Complete proteome; Keratinization; Membrane;
KW   Metal-binding; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    815       Protein-glutamine gamma-
FT                                glutamyltransferase K.
FT                                /FTId=PRO_0000213700.
FT   ACT_SITE    375    375       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    434    434       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    457    457       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       497    497       Calcium. {ECO:0000250}.
FT   METAL       499    499       Calcium. {ECO:0000250}.
FT   METAL       546    546       Calcium. {ECO:0000250}.
FT   METAL       551    551       Calcium. {ECO:0000250}.
FT   MOD_RES      21     21       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9JLF6}.
FT   MOD_RES      23     23       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22735}.
FT   MOD_RES      80     80       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22735}.
FT   MOD_RES      83     83       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22735}.
FT   MOD_RES      90     90       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22735}.
FT   MOD_RES      93     93       Phosphoserine.
FT                                {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
//
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