ID   SGT12_ASPFU             Reviewed;         341 AA.
AC   Q4WTC0;
DT   24-JAN-2024, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   02-SEP-2026, entry version 132.
DE   RecName: Full=Heat-shock protein cognate (HSC) co-chaperone sgt12 {ECO:0000303|PubMed:22262836};
GN   Name=sgt12 {ECO:0000303|PubMed:22262836}; ORFNames=AFUA_1G09830;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=22262836; DOI=10.1074/jbc.m111.333252;
RA   Chartron J.W., VanderVelde D.G., Rao M., Clemons W.M.;
RT   "Get5 carboxyl-terminal domain is a novel dimerization motif that tethers
RT   an extended Get4/Get5 complex.";
RL   J. Biol. Chem. 287:8310-8317(2012).
RN   [3] {ECO:0007744|PDB:3SZ7}
RP   X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 109-267, FUNCTION, SUBUNIT,
RP   INTERACTION WITH GET5; SSA1; SSE1; HSC82 AND HSP107, AND MUTAGENESIS OF
RP   TYR-181; LYS-183 AND ARG-187.
RX   PubMed=21832041; DOI=10.1074/jbc.m111.277798;
RA   Chartron J.W., Gonzalez G.M., Clemons W.M.;
RT   "A structural model of the Sgt2 protein and its interactions with
RT   chaperones and the Get4/Get5 complex.";
RL   J. Biol. Chem. 286:34325-34334(2011).
CC   -!- FUNCTION: Heat-shock protein cognate (HSC) co-chaperone that
CC       preferentially binds endoplasmic reticulum-destined tail-anchored (TA)
CC       proteins and directs them to the GET (guided entry of TA proteins)
CC       pathway via get4 and get5 (PubMed:21832041, PubMed:22262836). Get4 and
CC       get5 form an obligate complex that catalyzes the transfer of tail-
CC       anchored proteins destined to the endoplasmic reticulum from sgt2 to
CC       the cytosolic targeting factor which then targets the TA protein to the
CC       ER membrane via get1/get2 (PubMed:21832041, PubMed:22262836).
CC       {ECO:0000269|PubMed:21832041, ECO:0000269|PubMed:22262836}.
CC   -!- SUBUNIT: Forms homodimers (PubMed:21832041). Component of the
CC       get4/get5/sgt2 sorting complex (PubMed:21832041, PubMed:22262836).
CC       Dimers of sgt2 bind directly a single get5 (PubMed:21832041). Binds HSC
CC       family members ssa1, sse1, hsp104 and hsc82 via its TPR domain
CC       (PubMed:21832041). {ECO:0000269|PubMed:21832041,
CC       ECO:0000269|PubMed:22262836}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12118}.
CC   -!- DOMAIN: The tetratrico-repeat (TPR) region has the ability to directly
CC       bind multiple HSC family members including ssa1, sse1, hsp104 and
CC       hsc82. {ECO:0000269|PubMed:21832041}.
CC   -!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
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DR   EMBL; AAHF01000004; EAL90312.1; -; Genomic_DNA.
DR   PDB; 3SZ7; X-ray; 1.72 A; A=109-267.
DR   AlphaFoldDB; Q4WTC0; -.
DR   SMR; Q4WTC0; -.
DR   FunCoup; Q4WTC0; 599.
DR   STRING; 330879.Q4WTC0; -.
DR   EnsemblFungi; Afu1g09830-T; Afu1g09830-T-p1; Afu1g09830.
DR   KEGG; afm:AFUA_1G09830; -.
DR   eggNOG; KOG0553; Eukaryota.
DR   HOGENOM; CLU_044224_1_1_1; -.
DR   InParanoid; Q4WTC0; -.
DR   OMA; DMARNMM; -.
DR   OrthoDB; 2335338at2759; -.
DR   EvolutionaryTrace; Q4WTC0; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0072380; C:TRC complex; IBA:GO_Central.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:EnsemblFungi.
DR   GO; GO:0051879; F:Hsp90 protein binding; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblFungi.
DR   FunFam; 1.20.5.420:FF:000005; Hsc70 cochaperone (SGT), putative; 1.
DR   FunFam; 1.25.40.10:FF:000207; Small glutamine-rich tetratricopeptide repeat-containing protein; 1.
DR   FunFam; 1.10.260.100:FF:000011; TPR Domain containing protein; 1.
DR   Gene3D; 1.10.260.100; -; 1.
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; IPR006636; STI1_HS-bd.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR45831; LD24721P; 1.
DR   PANTHER; PTHR45831:SF2; LD24721P; 1.
DR   Pfam; PF16546; SGTA_dimer; 1.
DR   Pfam; PF13414; TPR_11; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00727; STI1; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PDBsum; 3SZ7; -.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..341
FT                   /note="Heat-shock protein cognate (HSC) co-chaperone sgt12"
FT                   /id="PRO_0000459360"
FT   REPEAT          114..147
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          148..181
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          182..215
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REGION          86..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..278
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         181
FT                   /note="Y->A: Impairs binding to HSC proteins; when
FT                   associated with A-183 and A-187."
FT                   /evidence="ECO:0000303|PubMed:21832041"
FT   MUTAGEN         183
FT                   /note="K->A: Impairs binding to HSC proteins; when
FT                   associated with A-181 and A-187."
FT                   /evidence="ECO:0000303|PubMed:21832041"
FT   MUTAGEN         187
FT                   /note="R->A: Impairs binding to HSC proteins; when
FT                   associated with A-181 and A-183."
FT                   /evidence="ECO:0000303|PubMed:21832041"
FT   HELIX           112..126
FT                   /evidence="ECO:0007829|PDB:3SZ7"
FT   HELIX           130..143
FT                   /evidence="ECO:0007829|PDB:3SZ7"
FT   HELIX           148..160
FT                   /evidence="ECO:0007829|PDB:3SZ7"
FT   HELIX           164..177
FT                   /evidence="ECO:0007829|PDB:3SZ7"
FT   HELIX           182..194
FT                   /evidence="ECO:0007829|PDB:3SZ7"
FT   HELIX           198..212
FT                   /evidence="ECO:0007829|PDB:3SZ7"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:3SZ7"
FT   HELIX           218..236
FT                   /evidence="ECO:0007829|PDB:3SZ7"
FT   HELIX           240..246
FT                   /evidence="ECO:0007829|PDB:3SZ7"
FT   HELIX           250..253
FT                   /evidence="ECO:0007829|PDB:3SZ7"
SQ   SEQUENCE   341 AA;  35744 MW;  8CBE2300CF2D06C6 CRC64;
     MVRLSDTPAP TESQKRLALA IIDFLNSSLK DGTLTADDAE SIEIAQSCIA DTFKVDPSDE
     AAVKDALGGQ SLASIFSVYE KLRQKPSKEP ASAGAQAQST EAQQPKAGAP TPESDKLKSE
     GNAAMARKEY SKAIDLYTQA LSIAPANPIY LSNRAAAYSA SGQHEKAAED AELATVVDPK
     YSKAWSRLGL ARFDMADYKG AKEAYEKGIE AEGNGGSDAM KRGLETTKRK IEEANRGAEP
     PADDVDDAAG ASRGAGGMPD LSSLASMLGG RGGGGGGMPD LSSIMSNPMF ASMAQNLMSN
     PDMLNNLMNN PQLRQMAENF GRGGGMPDMS SLMSDPSLAE M
//