ID   TGM1_RAT                Reviewed;         824 AA.
AC   P23606; Q4QRA6;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-NOV-2008, entry version 70.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase K;
DE            EC=2.3.2.13;
DE   AltName: Full=Transglutaminase K;
DE            Short=TGase K;
DE            Short=TGK;
DE            Short=TG(K);
DE   AltName: Full=Transglutaminase-1;
DE   AltName: Full=Epidermal TGase;
GN   Name=Tgm1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91067700; PubMed=1979171;
RA   Phillips M.A., Stewart B.E., Qin Q., Chakravarty R., Floyd E.E.,
RA   Jetten A.M., Rice R.H.;
RT   "Primary structure of keratinocyte transglutaminase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9333-9337(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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.
CC   -!- CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N(5)-
CC       alkylglutamine + NH(3).
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family.
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DR   EMBL; M57263; AAA63495.1; -; mRNA.
DR   EMBL; BC097305; AAH97305.1; -; mRNA.
DR   PIR; B38423; B38423.
DR   RefSeq; NP_113847.1; -.
DR   UniGene; Rn.10039; -.
DR   HSSP; P00488; 1EVU.
DR   PhosphoSite; P23606; -.
DR   Ensembl; ENSRNOG00000020136; Rattus norvegicus.
DR   GeneID; 60335; -.
DR   KEGG; rno:60335; -.
DR   RGD; 61838; Tgm1.
DR   HOVERGEN; P23606; -.
DR   NextBio; 611983; -.
DR   ArrayExpress; P23606; -.
DR   GermOnline; ENSRNOG00000020136; Rattus norvegicus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase...; IEA:InterPro.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
DR   InterPro; IPR008957; Fibronectin_typ-III-like_fold.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR013808; Transglutaminase_CS.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   InterPro; IPR002931; Trnsglumase_like.
DR   Gene3D; G3DSA:2.60.40.30; FN_III-like; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   SMART; SM00460; TGc; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Calcium; Keratinization; Membrane; Metal-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN         1    824       Protein-glutamine gamma-
FT                                glutamyltransferase K.
FT                                /FTId=PRO_0000213704.
FT   ACT_SITE    385    385       By similarity.
FT   ACT_SITE    444    444       By similarity.
FT   ACT_SITE    467    467       By similarity.
FT   METAL       507    507       Calcium (By similarity).
FT   METAL       509    509       Calcium (By similarity).
FT   METAL       556    556       Calcium (By similarity).
FT   METAL       561    561       Calcium (By similarity).
FT   MOD_RES      70     70       Phosphoserine (By similarity).
FT   MOD_RES     100    100       Phosphoserine (By similarity).
FT   MOD_RES     103    103       Phosphoserine (By similarity).
SQ   SEQUENCE   824 AA;  90770 MW;  A7D81C148CEFD938 CRC64;
     MEGPRSDVGR WGRSPWQPTT PSPEPEPEPE PDRSSRSRRG GGRSFWARCC GCCSCGNRAD
     DDWGPEPSGS RSRGTSSRGG GSRGGDSRGR DSRGGRRPES RGSGVNAAGD GTIREGMLVV
     NGVDLLCSRS DQNRREHHTD EFEYDELILR RGQPFHIILF LNREYESSDR IALELLIGNN
     PEVGKGTHVI IPVGKGGSGG WKAQVTKTNG HNLTLRVHTS PNAIIGKFQF TVRTRSEAGE
     FQLPFDPRNE IYILFNPWCP EDIVYVDHED WRQEYVLNES GRIYYGTEAQ IGERTWNYGQ
     FDHGVLDACL YILDRRGMPY GGRGDPVSVS RVVSAMVNSL DDNGVLIGNW TGDYSRGTNP
     SAWVGSVEIL LSYLRTGYSV PYGQCWVFAG VTTTVLRCLG LATRTVTNFN SAHDTDTSLT
     MDIYFDENMK PLEHLNHDSV WNFHVWNDCW MKRPDLPSGF DGWQVVDATP QETSSGIFCC
     GPCSVESIKN GLVYMKYDTP FIFAEVNSDK VYWQRQDDGS FKIVYVEEKA IGTLIVTKAI
     NSNMREDITH IYKHPEGSEA ERKAVEKAAA HGSKPNVYAT RDSAEDVAMQ VEAQDAVMGQ
     DLTVSVVLTN RGSSRRTVKL HLYLCVTYYT GVSGPTFKET KKEVVLAPGA SDTVAMPVAY
     KEYKPHLVDQ GAMLLNVSGH VKESGQVLAK QHTFRLRTPD LSLTLLGAAV VGQECEVQIV
     FKNPLPITLT NVVFRLEGSG LQRPKVLNVG DIGGNETVTL RQTFVPVRPG PRQLIASLDS
     PQLSQVHGVI QVDVAPSSGG RGFSEAVGDS RSGENIPMAF RGGA
//