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TGM3_RAT
ID   TGM3_RAT                Reviewed;         693 AA.
AC   D4A5U3;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase E;
DE            EC=2.3.2.13 {ECO:0000250|UniProtKB:Q08188};
DE   AltName: Full=Transglutaminase E;
DE            Short=TG(E);
DE            Short=TGE;
DE            Short=TGase E;
DE   AltName: Full=Transglutaminase-3;
DE            Short=TGase-3;
DE   Contains:
DE     RecName: Full=Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain;
DE   Contains:
DE     RecName: Full=Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain;
DE   Flags: Precursor;
GN   Name=Tgm3; Synonyms=Tgase3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the calcium-dependent formation of isopeptide
CC       cross-links between glutamine and lysine residues in various proteins,
CC       as well as the conjugation of polyamines to proteins. Involved in the
CC       formation of the cornified envelope (CE), a specialized component
CC       consisting of covalent cross-links of proteins beneath the plasma
CC       membrane of terminally differentiated keratinocytes. Catalyzes small
CC       proline-rich proteins and LOR cross-linking to form small interchain
CC       oligomers, which are further cross-linked by TGM1 onto the growing CE
CC       scaffold. In hair follicles, involved in cross-linking structural
CC       proteins to hardening the inner root sheath (By similarity).
CC       {ECO:0000250}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q08188, ECO:0000255|PROSITE-
CC         ProRule:PRU10024};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 3 Ca(2+) cations per subunit. Binds 1 Ca(2+) as a zymogen,
CC       and binds 2 more Ca(2+) cations, or other divalent metal cations, after
CC       proteolytic processing. {ECO:0000250};
CC   -!- SUBUNIT: Consists of two polypeptide chains, which are synthesized as a
CC       precursor form of a single polypeptide. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q08188}.
CC   -!- PTM: Activated by proteolytic processing. In vitro activation is
CC       commonly achieved by cleavage with dispase, a neutral bacterial
CC       protease. Physiological activation may be catalyzed by CTSL and, to a
CC       lesser extent, by CTSS (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
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DR   EMBL; CH473949; EDL80172.1; -; Genomic_DNA.
DR   RefSeq; NP_001102429.1; NM_001108959.1.
DR   AlphaFoldDB; D4A5U3; -.
DR   SMR; D4A5U3; -.
DR   BioGRID; 265783; 1.
DR   STRING; 10116.ENSRNOP00000059160; -.
DR   iPTMnet; D4A5U3; -.
DR   PhosphoSitePlus; D4A5U3; -.
DR   PaxDb; D4A5U3; -.
DR   PRIDE; D4A5U3; -.
DR   Ensembl; ENSRNOT00000063828; ENSRNOP00000059160; ENSRNOG00000006753.
DR   GeneID; 366189; -.
DR   KEGG; rno:366189; -.
DR   UCSC; RGD:1561831; rat.
DR   CTD; 7053; -.
DR   RGD; 1561831; Tgm3.
DR   eggNOG; ENOG502QUPB; Eukaryota.
DR   GeneTree; ENSGT01050000244866; -.
DR   HOGENOM; CLU_013435_1_0_1; -.
DR   InParanoid; D4A5U3; -.
DR   OMA; VDQNFDM; -.
DR   OrthoDB; 297055at2759; -.
DR   PhylomeDB; D4A5U3; -.
DR   TreeFam; TF324278; -.
DR   PRO; PR:D4A5U3; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Proteomes; UP000234681; Chromosome 3.
DR   Bgee; ENSRNOG00000006753; Expressed in esophagus and 12 other tissues.
DR   Genevisible; D4A5U3; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0003824; F:catalytic activity; ISO:RGD.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; ISO:RGD.
DR   GO; GO:0043163; P:cell envelope organization; ISO:RGD.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR   GO; GO:0018149; P:peptide cross-linking; 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   3: Inferred from homology;
KW   Acyltransferase; Calcium; Cytoplasm; Keratinization; Metal-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Zymogen.
FT   CHAIN           1..467
FT                   /note="Protein-glutamine gamma-glutamyltransferase E 50 kDa
FT                   catalytic chain"
FT                   /id="PRO_0000408951"
FT   CHAIN           468..693
FT                   /note="Protein-glutamine gamma-glutamyltransferase E 27 kDa
FT                   non-catalytic chain"
FT                   /id="PRO_0000408952"
FT   REGION          455..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT   BINDING         222
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         394
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         416
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         449
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   SITE            467..468
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         111
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08188"
FT   MOD_RES         112
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08188"
SQ   SEQUENCE   693 AA;  77230 MW;  CFE4D1B46960D4C2 CRC64;
     MSALEVQNIN WQMPMNRRAH HTDKFSSQDF IVRRGQPWEV ILLCNRSLES GDNLNFIVST
     GPQPSESART KAVFSISGRN TSGWSAALKA SNGNNLFIAI ASPVSAPIGL YTLNVEVSSK
     GRVSSVKLGT FTVLFNPWQQ GDDVFMSNHA ERQEYVEEDS GIIYVGSTNR IGMVGWNFGQ
     FEEDILSISL SILDRSLNFR RDPATDVARR NDPKYVCRVL SAMINANDDS GVLSGNWSGN
     YSGGVDPRTW NGSVEILKNW KKSGFRPVQF GQCWVFAGTL NTVLRCLGVP SRVITNFNSA
     HDTDRNLSVD VYYDAMGNPL EKGSDSVWNF HVWNEGWFVR TDLGPSYNGW QVLDATPQER
     SQGVFQCGPA SVNAIKDGEV DQNFDMIFIF AEVNADRITW IYNNRDGSQK QNSVDTYSIG
     KYISTKAVGS NSRMDVTIKY KHPEGSKEER QVQQKAMNKL KPNASFGATS SRGPQGEEKE
     PSISGKFKVT GVLAVGKEVS LALILKNTTS DRKTVTTNMT AWTIVYNGTL VHEVWKDSAT
     ISLDPEEEIQ YPVKIAYSQY DRYLKADNMI RITAVCKVPD EAEVVVERDV ILDNPTLTLE
     VLDQAQLRKP VVVQMLFSNP LDEPVKNCVL MVEGSGLLRG SLKIDVPALR PKEKSRVRFE
     IFPTRIGIKQ LLADFSCNKF PAIKAMLVIE VSE
 
 
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