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 27-MAR-2024, entry version 124. 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; OC Aspergillus subgen. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHF01000004; EAL90312.1; -; Genomic_DNA. DR RefSeq; XP_752350.1; XM_747257.1. DR PDB; 3SZ7; X-ray; 1.72 A; A=109-267. DR PDBsum; 3SZ7; -. DR AlphaFoldDB; Q4WTC0; -. DR SMR; Q4WTC0; -. DR STRING; 330879.Q4WTC0; -. DR EnsemblFungi; EAL90312; EAL90312; AFUA_1G09830. DR GeneID; 3510472; -. DR KEGG; afm:AFUA_1G09830; -. DR eggNOG; KOG0553; Eukaryota. DR HOGENOM; CLU_044224_1_1_1; -. DR InParanoid; Q4WTC0; -. DR OMA; ASGQHEK; -. DR OrthoDB; 1343678at2759; -. DR Proteomes; UP000002530; Chromosome 1. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0072380; C:TRC complex; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi. DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. 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 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_repeat. 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. 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 91..107 FT /note="Polar 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" 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 //