ID   SGTB_RAT                Reviewed;         304 AA.
AC   Q80W98;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein beta;
DE   AltName: Full=Beta-SGT;
DE   AltName: Full=Small glutamine-rich protein with tetratricopeptide repeats 2;
GN   Name=Sgtb; Synonyms=Sgt2;
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 [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=12878599; DOI=10.1074/jbc.m301558200;
RA   Tobaben S., Varoqueaux F., Brose N., Stahl B., Meyer G.;
RT   "A brain-specific isoform of small glutamine-rich tetratricopeptide repeat-
RT   containing protein binds to Hsc70 and the cysteine string protein.";
RL   J. Biol. Chem. 278:38376-38383(2003).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Co-chaperone that binds directly to HSC70 and HSP70 and
CC       regulates their ATPase activity. {ECO:0000269|PubMed:12878599}.
CC   -!- SUBUNIT: Homooligomerize. {ECO:0000269|PubMed:12878599}.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in brain.
CC       {ECO:0000269|PubMed:12878599}.
CC   -!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
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DR   EMBL; AF368280; AAP29458.1; -; mRNA.
DR   RefSeq; NP_853660.1; NM_181629.3.
DR   RefSeq; XP_006231944.1; XM_006231882.3.
DR   AlphaFoldDB; Q80W98; -.
DR   SMR; Q80W98; -.
DR   BioGRID; 254771; 1.
DR   STRING; 10116.ENSRNOP00000016129; -.
DR   PaxDb; Q80W98; -.
DR   PRIDE; Q80W98; -.
DR   Ensembl; ENSRNOT00000016129; ENSRNOP00000016129; ENSRNOG00000011937.
DR   GeneID; 294708; -.
DR   KEGG; rno:294708; -.
DR   UCSC; RGD:727976; rat.
DR   CTD; 54557; -.
DR   RGD; 727976; Sgtb.
DR   eggNOG; KOG0553; Eukaryota.
DR   GeneTree; ENSGT00940000158321; -.
DR   HOGENOM; CLU_044224_0_0_1; -.
DR   InParanoid; Q80W98; -.
DR   OMA; ASGQHEK; -.
DR   OrthoDB; 687493at2759; -.
DR   PhylomeDB; Q80W98; -.
DR   TreeFam; TF313092; -.
DR   PRO; PR:Q80W98; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000011937; Expressed in frontal cortex and 17 other tissues.
DR   Genevisible; Q80W98; RN.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0072380; C:TRC complex; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; TAS:RGD.
DR   GO; GO:0030544; F:Hsp70 protein binding; TAS:RGD.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0008022; F:protein C-terminus binding; TAS:RGD.
DR   GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; TAS:RGD.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR032374; SGTA_dimer.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF16546; SGTA_dimer; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Phosphoprotein; Reference proteome; Repeat;
KW   TPR repeat.
FT   CHAIN           1..304
FT                   /note="Small glutamine-rich tetratricopeptide repeat-
FT                   containing protein beta"
FT                   /id="PRO_0000333275"
FT   REPEAT          15..49
FT                   /note="TPR 1"
FT   REPEAT          85..118
FT                   /note="TPR 2"
FT   REPEAT          120..152
FT                   /note="TPR 3"
FT   REPEAT          153..186
FT                   /note="TPR 4"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43765"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43765"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EQ0"
FT   MOD_RES         297
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EQ0"
SQ   SEQUENCE   304 AA;  33488 MW;  3D523C528E5DDCEA CRC64;
     MSSVKPLVYA VIRFLREQSQ MDAYTSDEQE SLEVAIQCLE TVFKISPEDT HLAVSQPLTE
     MFTNSVCKND IRPLSNSVPE DVGKADQLKD EGNNHMKEEN YAAAVDCYTQ AIELDPNNAV
     YYCNRAAAQS KLSHYTDAIK DCEKAIAIDS KYSKAYGRMG LALTAMNKFE EAVTSYQKAL
     DLDPENDSYK SNLKIAEQKL REVSSPTGTG LTFDMASLIN NPAFITMAAS LMQNPQVQQL
     MSGMMTNAIG GPAAGVGGLT DLSSLIQAGQ QFAQQIQQQN PELIEQLRNH IRSRSFSSST
     EEHS