SGTA_BOVIN
ID SGTA_BOVIN Reviewed; 313 AA.
AC Q32LM2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha;
DE AltName: Full=Alpha-SGT;
GN Name=SGTA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Co-chaperone that binds misfolded and hydrophobic patches-
CC containing client proteins in the cytosol. Mediates their targeting to
CC the endoplasmic reticulum but also regulates their sorting to the
CC proteasome when targeting fails. Functions in tail-anchored/type II
CC transmembrane proteins membrane insertion constituting with ASNA1 and
CC the BAG6 complex a targeting module. Functions upstream of the BAG6
CC complex and ASNA1, binding more rapidly the transmembrane domain of
CC newly synthesized proteins. It is also involved in the regulation of
CC the endoplasmic reticulum-associated misfolded protein catabolic
CC process via its interaction with BAG6: collaborates with the BAG6
CC complex to maintain hydrophobic substrates in non-ubiquitinated states.
CC Competes with RNF126 for interaction with BAG6, preventing the
CC ubiquitination of client proteins associated with the BAG6 complex.
CC Binds directly to HSC70 and HSP70 and regulates their ATPase activity.
CC {ECO:0000250|UniProtKB:O43765}.
CC -!- SUBUNIT: Homodimer (By similarity). Homooligomer (By similarity).
CC Interacts with DNAJC5 and DNAJC5B. Interacts (via TPR repeats) with
CC HSP90AA1. Interacts (via Gln-rich region) with SLC2A1. Interacts with
CC HSP90AB1. Interacts (via TPR repeats) with HSPA8/Hsc70; the interaction
CC is direct. Interacts with BAG6 (via ubiquitin-like domain); interaction
CC prevents interaction between BAG6 and RNF126. Forms a multiprotein
CC complex, at least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA;
CC interaction with DNAJB14 and HSPA8/Hsc70 is direct (By similarity).
CC {ECO:0000250|UniProtKB:O43765, ECO:0000250|UniProtKB:O70593}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43765}. Nucleus
CC {ECO:0000250|UniProtKB:O43765}. Note=Co-localizes with HSP90AB1 in the
CC cytoplasm. Increased nuclear accumulation seen during cell apoptosis.
CC Interacts with BAG6 (via ubiquitin-like domain); interaction prevents
CC interaction between BAG6 and RNF126. {ECO:0000250|UniProtKB:O43765}.
CC -!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
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DR EMBL; BC109513; AAI09514.1; -; mRNA.
DR RefSeq; NP_001033119.1; NM_001038030.2.
DR RefSeq; XP_005209059.1; XM_005209002.3.
DR RefSeq; XP_010805314.1; XM_010807012.2.
DR RefSeq; XP_010805315.1; XM_010807013.2.
DR AlphaFoldDB; Q32LM2; -.
DR SMR; Q32LM2; -.
DR STRING; 9913.ENSBTAP00000020081; -.
DR PaxDb; Q32LM2; -.
DR PeptideAtlas; Q32LM2; -.
DR PRIDE; Q32LM2; -.
DR Ensembl; ENSBTAT00000020081; ENSBTAP00000020081; ENSBTAG00000015090.
DR Ensembl; ENSBTAT00000080874; ENSBTAP00000067531; ENSBTAG00000015090.
DR GeneID; 504701; -.
DR KEGG; bta:504701; -.
DR CTD; 6449; -.
DR VEuPathDB; HostDB:ENSBTAG00000015090; -.
DR VGNC; VGNC:34553; SGTA.
DR eggNOG; KOG0553; Eukaryota.
DR GeneTree; ENSGT00940000159037; -.
DR HOGENOM; CLU_044224_0_0_1; -.
DR InParanoid; Q32LM2; -.
DR OMA; MMCNLMS; -.
DR OrthoDB; 687493at2759; -.
DR TreeFam; TF313092; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000015090; Expressed in floor plate of diencephalon and 105 other tissues.
DR ExpressionAtlas; Q32LM2; baseline and differential.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0072380; C:TRC complex; IBA:GO_Central.
DR GO; GO:1904288; F:BAT3 complex binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:1903070; P:negative regulation of ER-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
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; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chaperone; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..313
FT /note="Small glutamine-rich tetratricopeptide repeat-
FT containing protein alpha"
FT /id="PRO_0000333273"
FT REPEAT 91..124
FT /note="TPR 1"
FT REPEAT 125..158
FT /note="TPR 2"
FT REPEAT 159..192
FT /note="TPR 3"
FT REGION 69..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70593"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
SQ SEQUENCE 313 AA; 34213 MW; 67075AC382E5D7CE CRC64;
MDNKKRLAYA IIRFLHDQLR HGELSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE
IFEAAAAGKE LPPDLRSPQE TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL
NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPSYSK AYGRMGLALS SLNKHTEAVA
YYRKALELDP DNETYKSNLK VAELRLREAP SPTGGVGSFD IAGLLNNPSF MSMASNLMNN
PQVQQLMSGM ISGGHNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR
SRTPSASNDD QQE
