SGTA_MOUSE
ID SGTA_MOUSE Reviewed; 315 AA.
AC Q8BJU0; Q8BGA6; Q99L52;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha;
DE AltName: Full=Alpha-SGT;
GN Name=Sgta; Synonyms=Sgt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP INTERACTION WITH DNAJC5 AND DNAJC5B.
RX PubMed=17034881; DOI=10.1016/j.bbamcr.2006.08.054;
RA Boal F., Le Pevelen S., Cziepluch C., Scotti P., Lang J.;
RT "Cysteine-string protein isoform beta (Cspbeta) is targeted to the trans-
RT Golgi network as a non-palmitoylated CSP in clonal beta-cells.";
RL Biochim. Biophys. Acta 1773:109-119(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82; THR-305 AND SER-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (PubMed:17034881). Interacts (via TPR
CC repeats) with HSP90AA1. Interacts (via Gln-rich region) with SLC2A1 (By
CC similarity). Interacts with HSP90AB1 (By similarity). Interacts (via
CC TPR repeats) with HSPA8/Hsc70; the interaction is direct (By
CC similarity). Interacts with BAG6 (via ubiquitin-like domain);
CC interaction prevents interaction between BAG6 and RNF126 (By
CC similarity). Forms a multiprotein complex, at least composed of
CC DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and
CC HSPA8/Hsc70 is direct (By similarity). {ECO:0000250|UniProtKB:O43765,
CC ECO:0000250|UniProtKB:O70593, ECO:0000269|PubMed:17034881}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BJU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJU0-2; Sequence=VSP_009300;
CC -!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
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DR EMBL; AK039966; BAC30486.1; -; mRNA.
DR EMBL; AK051005; BAC34494.1; -; mRNA.
DR EMBL; AK079168; BAC37566.1; -; mRNA.
DR EMBL; BC003836; AAH03836.1; -; mRNA.
DR CCDS; CCDS35990.1; -. [Q8BJU0-1]
DR CCDS; CCDS88056.1; -. [Q8BJU0-2]
DR RefSeq; NP_078775.1; NM_024499.1. [Q8BJU0-1]
DR RefSeq; XP_006513939.1; XM_006513876.3.
DR RefSeq; XP_006513940.1; XM_006513877.1. [Q8BJU0-2]
DR RefSeq; XP_017169518.1; XM_017314029.1.
DR AlphaFoldDB; Q8BJU0; -.
DR SMR; Q8BJU0; -.
DR BioGRID; 206659; 33.
DR CORUM; Q8BJU0; -.
DR IntAct; Q8BJU0; 1.
DR MINT; Q8BJU0; -.
DR STRING; 10090.ENSMUSP00000005067; -.
DR iPTMnet; Q8BJU0; -.
DR PhosphoSitePlus; Q8BJU0; -.
DR SwissPalm; Q8BJU0; -.
DR EPD; Q8BJU0; -.
DR jPOST; Q8BJU0; -.
DR MaxQB; Q8BJU0; -.
DR PaxDb; Q8BJU0; -.
DR PeptideAtlas; Q8BJU0; -.
DR PRIDE; Q8BJU0; -.
DR ProteomicsDB; 256993; -. [Q8BJU0-1]
DR ProteomicsDB; 256994; -. [Q8BJU0-2]
DR Antibodypedia; 23040; 278 antibodies from 33 providers.
DR DNASU; 52551; -.
DR Ensembl; ENSMUST00000005067; ENSMUSP00000005067; ENSMUSG00000004937. [Q8BJU0-1]
DR Ensembl; ENSMUST00000218208; ENSMUSP00000151949; ENSMUSG00000004937. [Q8BJU0-2]
DR GeneID; 52551; -.
DR KEGG; mmu:52551; -.
DR UCSC; uc007gft.1; mouse. [Q8BJU0-1]
DR CTD; 6449; -.
DR MGI; MGI:1098703; Sgta.
DR VEuPathDB; HostDB:ENSMUSG00000004937; -.
DR eggNOG; KOG0553; Eukaryota.
DR GeneTree; ENSGT00940000159037; -.
DR HOGENOM; CLU_044224_0_0_1; -.
DR InParanoid; Q8BJU0; -.
DR OMA; MMCNLMS; -.
DR OrthoDB; 687493at2759; -.
DR PhylomeDB; Q8BJU0; -.
DR TreeFam; TF313092; -.
DR Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR BioGRID-ORCS; 52551; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Sgta; mouse.
DR PRO; PR:Q8BJU0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BJU0; protein.
DR Bgee; ENSMUSG00000004937; Expressed in embryonic brain and 262 other tissues.
DR ExpressionAtlas; Q8BJU0; baseline and differential.
DR Genevisible; Q8BJU0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0072380; C:TRC complex; IBA:GO_Central.
DR GO; GO:1904288; F:BAT3 complex binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:MGI.
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:MGI.
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; Alternative splicing; Chaperone; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..315
FT /note="Small glutamine-rich tetratricopeptide repeat-
FT containing protein alpha"
FT /id="PRO_0000106366"
FT REPEAT 92..125
FT /note="TPR 1"
FT REPEAT 126..159
FT /note="TPR 2"
FT REPEAT 160..193
FT /note="TPR 3"
FT REGION 65..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70593"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43765"
FT MOD_RES 305
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 70
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009300"
FT CONFLICT 207
FT /note="L -> F (in Ref. 1; BAC37566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 34322 MW; 6FB8D3978CF56D4C CRC64;
MDNRKRLAYA IIQFLHGQLR HGGLSCDAQE SLEVAIQCLE TAFGVTLEDS DLALPQTLPE
IFEAATSSKQ EMPQDPRAPD RTPPSEEDSA EAERLKTEGN EQMKLENFEA AVHLYGKAIE
LNPANAVYFC NRAAAYSKLG NYVGAVQDCE RAIGIDPGYS KAYGRMGLAL SSLNKHAEAV
AYYKKALELD PDNDTYKSNL KIAELKLREA PSPTGGVGSL DIAGLLNNPH FITMASSLMN
SPQLQQLMSG MISGGHNPLG TPGSSPQQSD LASLIQAGQQ FAQQMQQQNP EFVEQIRSQV
VRSRTPSASH EEQQE
