ID   SGT2_YEAST              Reviewed;         346 AA.
AC   Q12118; D6W273;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein 2;
DE   AltName: Full=SGT/UBP;
DE   AltName: Full=Viral protein U-binding protein;
GN   Name=SGT2; OrderedLocusNames=YOR007C; ORFNames=UNF346;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8896276;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA   Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT   "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT   Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT   correspond to previously identified genes.";
RL   Yeast 12:1091-1095(1996).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 131-142 AND 158-171, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RA   Bienvenut W.V., Peters C.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [5]
RP   FUNCTION.
RX   PubMed=12482202; DOI=10.1379/1466-1268(2002)007<0258:sgrpvp>2.0.co;2;
RA   Angeletti P.C., Walker D., Panganiban A.T.;
RT   "Small glutamine-rich protein/viral protein U-binding protein is a novel
RT   cochaperone that affects heat shock protein 70 activity.";
RL   Cell Stress Chaperones 7:258-268(2002).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   INTERACTION WITH HSC82; HSP104; MDY2; SSA1 AND SSA2.
RX   PubMed=17441508; DOI=10.1379/csc-220r.1;
RA   Liou S.-T., Cheng M.-Y., Wang C.;
RT   "SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces
RT   cerevisiae.";
RL   Cell Stress Chaperones 12:59-70(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Co-chaperone that binds to the molecular chaperone Hsp70
CC       (SSA1 and SSA2). Regulates Hsp70 ATPase activity (By similarity).
CC       Required for recovery from heat shock. {ECO:0000250,
CC       ECO:0000269|PubMed:12482202}.
CC   -!- SUBUNIT: Interacts with HSC82, HSP104, MDY2, SSA1 and SSA2.
CC       {ECO:0000269|PubMed:17441508}.
CC   -!- INTERACTION:
CC       Q12118; P40515: FIS1; NbExp=3; IntAct=EBI-31784, EBI-25059;
CC       Q12118; Q12125: GET4; NbExp=5; IntAct=EBI-31784, EBI-36940;
CC       Q12118; Q12285: MDY2; NbExp=15; IntAct=EBI-31784, EBI-34904;
CC       Q12118; P22214: SEC22; NbExp=4; IntAct=EBI-31784, EBI-16577;
CC       Q12118; Q12118: SGT2; NbExp=4; IntAct=EBI-31784, EBI-31784;
CC       Q12118; P25491: YDJ1; NbExp=2; IntAct=EBI-31784, EBI-10420;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 9424 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
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DR   EMBL; U43491; AAC49487.1; -; Genomic_DNA.
DR   EMBL; Z74915; CAA99195.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10789.1; -; Genomic_DNA.
DR   PIR; S61991; S61991.
DR   RefSeq; NP_014649.1; NM_001183426.1.
DR   PDB; 2LXB; NMR; -; A/B=2-72.
DR   PDB; 2LXC; NMR; -; B/C=2-72.
DR   PDB; 3ZDM; X-ray; 1.80 A; A/B/D/E=1-72.
DR   PDB; 4ASV; NMR; -; A/B=1-78.
DR   PDB; 4ASW; NMR; -; A/B=1-78.
DR   PDB; 5LYN; X-ray; 2.00 A; A/B=96-225.
DR   PDB; 5LYP; X-ray; 1.55 A; A=93-229.
DR   PDBsum; 2LXB; -.
DR   PDBsum; 2LXC; -.
DR   PDBsum; 3ZDM; -.
DR   PDBsum; 4ASV; -.
DR   PDBsum; 4ASW; -.
DR   PDBsum; 5LYN; -.
DR   PDBsum; 5LYP; -.
DR   AlphaFoldDB; Q12118; -.
DR   BMRB; Q12118; -.
DR   SMR; Q12118; -.
DR   BioGRID; 34410; 273.
DR   ComplexPortal; CPX-1861; GET4-GET5 transmembrane domain recognition complex.
DR   DIP; DIP-1983N; -.
DR   IntAct; Q12118; 19.
DR   MINT; Q12118; -.
DR   STRING; 4932.YOR007C; -.
DR   TCDB; 3.A.21.1.1; the c-terminal tail-anchored membrane protein biogenesis/ insertion complex (tamp-b) family.
DR   iPTMnet; Q12118; -.
DR   MaxQB; Q12118; -.
DR   PaxDb; 4932-YOR007C; -.
DR   PeptideAtlas; Q12118; -.
DR   EnsemblFungi; YOR007C_mRNA; YOR007C; YOR007C.
DR   GeneID; 854168; -.
DR   KEGG; sce:YOR007C; -.
DR   AGR; SGD:S000005533; -.
DR   SGD; S000005533; SGT2.
DR   VEuPathDB; FungiDB:YOR007C; -.
DR   eggNOG; KOG0553; Eukaryota.
DR   HOGENOM; CLU_044224_1_0_1; -.
DR   InParanoid; Q12118; -.
DR   OMA; ASGQHEK; -.
DR   OrthoDB; 1343678at2759; -.
DR   BioCyc; YEAST:G3O-33557-MONOMER; -.
DR   Reactome; R-SCE-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   BioGRID-ORCS; 854168; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q12118; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12118; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0072380; C:TRC complex; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR   GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0009408; P:response to heat; IMP:SGD.
DR   Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR047150; SGT.
DR   InterPro; IPR032374; SGTA_dimer.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45831; LD24721P; 1.
DR   PANTHER; PTHR45831:SF2; LD24721P; 1.
DR   Pfam; PF16546; SGTA_dimer; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..346
FT                   /note="Small glutamine-rich tetratricopeptide repeat-
FT                   containing protein 2"
FT                   /id="PRO_0000106370"
FT   REPEAT          102..135
FT                   /note="TPR 1"
FT   REPEAT          136..169
FT                   /note="TPR 2"
FT   REPEAT          170..203
FT                   /note="TPR 3"
FT   REPEAT          205..229
FT                   /note="TPR 4"
FT   REGION          219..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         308
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   HELIX           5..21
FT                   /evidence="ECO:0007829|PDB:3ZDM"
FT   HELIX           27..44
FT                   /evidence="ECO:0007829|PDB:3ZDM"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:3ZDM"
FT   HELIX           51..56
FT                   /evidence="ECO:0007829|PDB:3ZDM"
FT   HELIX           58..68
FT                   /evidence="ECO:0007829|PDB:3ZDM"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:2LXB"
FT   HELIX           96..114
FT                   /evidence="ECO:0007829|PDB:5LYP"
FT   HELIX           118..131
FT                   /evidence="ECO:0007829|PDB:5LYP"
FT   HELIX           136..148
FT                   /evidence="ECO:0007829|PDB:5LYP"
FT   HELIX           152..165
FT                   /evidence="ECO:0007829|PDB:5LYP"
FT   HELIX           170..182
FT                   /evidence="ECO:0007829|PDB:5LYP"
FT   HELIX           186..200
FT                   /evidence="ECO:0007829|PDB:5LYP"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:5LYP"
FT   HELIX           206..224
FT                   /evidence="ECO:0007829|PDB:5LYP"
SQ   SEQUENCE   346 AA;  37218 MW;  33539B74F742BD3C CRC64;
     MSASKEEIAA LIVNYFSSIV EKKEISEDGA DSLNVAMDCI SEAFGFEREA VSGILGKSEF
     KGQHLADILN SASRVPESNK KDDAENVEIN IPEDDAETKA KAEDLKMQGN KAMANKDYEL
     AINKYTEAIK VLPTNAIYYA NRAAAHSSLK EYDQAVKDAE SAISIDPSYF RGYSRLGFAK
     YAQGKPEEAL EAYKKVLDIE GDNATEAMKR DYESAKKKVE QSLNLEKTVP EQSRDADVDA
     SQGASAGGLP DLGSLLGGGL GGLMNNPQLM QAAQKMMSNP GAMQNIQKMM QDPSIRQMAE
     GFASGGGTPN LSDLMNNPAL RNMAGNLFGG AGAQSTDETP DNENKQ
//