SGTA_RAT
ID SGTA_RAT Reviewed; 314 AA.
AC O70593; Q548F5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha;
DE AltName: Full=Alpha-SGT;
DE AltName: Full=Small glutamine-rich protein with tetratricopeptide repeats 1;
GN Name=Sgta; Synonyms=Sgt, Sgt1, Stg;
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], AND INTERACTION WITH PARVOVIRUS NS1 (MICROBIAL
RP INFECTION).
RX PubMed=9557704; DOI=10.1128/jvi.72.5.4149-4156.1998;
RA Cziepluch C., Kordes E., Poirey R., Grewenig A., Rommelaere J.,
RA Jauniaux J.-C.;
RT "Identification of a novel cellular TPR-containing protein, SGT, that
RT interacts with the nonstructural protein NS1 of parvovirus H-1.";
RL J. Virol. 72:4149-4156(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 104-116 AND 165-174, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH HSP90AA1 AND HSPA8.
RX PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
RA Liou S.T., Wang C.;
RT "Small glutamine-rich tetratricopeptide repeat-containing protein is
RT composed of three structural units with distinct functions.";
RL Arch. Biochem. Biophys. 435:253-263(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81 AND SER-84, AND
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 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 (By
CC similarity). Binds directly to HSC70 and HSP70 and regulates their
CC ATPase activity (PubMed:12878599). {ECO:0000250|UniProtKB:O43765,
CC ECO:0000269|PubMed:12878599}.
CC -!- SUBUNIT: Homodimer (By similarity). Homooligomer (PubMed:12878599).
CC Interacts with DNAJC5 and DNAJC5B (By similarity). Interacts (via TPR
CC repeats) with HSP90AA1 (PubMed:15708368). Interacts (via Gln-rich
CC region) with SLC2A1 (By similarity). Interacts with HSP90AB1 (By
CC similarity). Interacts (via TPR repeats) with HSPA8/Hsc70; the
CC interaction is direct (PubMed:15708368). Interacts with BAG6 (via
CC ubiquitin-like domain); interaction prevents interaction between BAG6
CC and RNF126 (By similarity). Forms a multiprotein complex, at least
CC composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with
CC DNAJB14 and HSPA8/Hsc70 is direct (By similarity).
CC {ECO:0000250|UniProtKB:O43765, ECO:0000269|PubMed:12878599,
CC ECO:0000269|PubMed:15708368}.
CC -!- SUBUNIT: (Microbial infection) Interacts with NS1 from parvovirus H-1
CC (PubMed:9557704). {ECO:0000269|PubMed:9557704}.
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 {ECO:0000250|UniProtKB:O43765}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12878599}.
CC -!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
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DR EMBL; AJ222724; CAA10960.1; -; mRNA.
DR EMBL; AF368278; AAP29456.1; -; mRNA.
DR EMBL; BC087642; AAH87642.1; -; mRNA.
DR RefSeq; NP_073194.1; NM_022703.3.
DR AlphaFoldDB; O70593; -.
DR SMR; O70593; -.
DR BioGRID; 249184; 2.
DR STRING; 10116.ENSRNOP00000026960; -.
DR iPTMnet; O70593; -.
DR PhosphoSitePlus; O70593; -.
DR jPOST; O70593; -.
DR PaxDb; O70593; -.
DR PeptideAtlas; O70593; -.
DR PRIDE; O70593; -.
DR GeneID; 64667; -.
DR KEGG; rno:64667; -.
DR UCSC; RGD:620815; rat.
DR CTD; 6449; -.
DR RGD; 620815; Sgta.
DR VEuPathDB; HostDB:ENSRNOG00000019891; -.
DR eggNOG; KOG0553; Eukaryota.
DR HOGENOM; CLU_044224_0_0_1; -.
DR InParanoid; O70593; -.
DR OMA; MMCNLMS; -.
DR OrthoDB; 687493at2759; -.
DR PhylomeDB; O70593; -.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR PRO; PR:O70593; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000019891; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; O70593; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0072380; C:TRC complex; IBA:GO_Central.
DR GO; GO:1904288; F:BAT3 complex binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:SynGO.
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; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..314
FT /note="Small glutamine-rich tetratricopeptide repeat-
FT containing protein alpha"
FT /id="PRO_0000106367"
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 65..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
SQ SEQUENCE 314 AA; 34157 MW; 65EBBE9A773A7F28 CRC64;
MDNRKRLAYA IIQFLHGQLR HGGLSSDAQE SLEVAIQCLE TAFGVTLEDS DLALPQTLPE
IFEAATASKE MPQDPRGPDR TPPSEEDSAE AERLKTEGNE QMKLENFEAA VHLYGKAIEL
NPANAVYFCN RAAAYSKLGN YVGAVQDCER AIGIDPGYSK AYGRMGLALS SLNKHAEAVA
YYKKALELDP DNDTYKSNLK IAELKLREAP SPTGGVGSLD IAGLLNNPHF ITMASSLMNS
PQLQQLMSGM ISGGHNPLGT PGSSPQHSDL ASLIQAGQQF AQQMQQQNPE FVEQIRSQVV
RSRTPSASHE EQQE
