APJ1_YEAST
ID APJ1_YEAST Reviewed; 528 AA.
AC P53940; D6W1A2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=J domain-containing protein APJ1;
GN Name=APJ1; OrderedLocusNames=YNL077W; ORFNames=N2342;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701611;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n;
RA Poehlmann R., Philippsen P.;
RT "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT reveals 12 new open reading frames (ORFs) and an ancient duplication of six
RT ORFs.";
RL Yeast 12:391-402(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
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 [7]
RP DOMAIN.
RX PubMed=15170475; DOI=10.1038/sj.embor.7400172;
RA Walsh P., Bursac D., Law Y.C., Cyr D., Lithgow T.;
RT "The J-protein family: modulating protein assembly, disassembly and
RT translocation.";
RL EMBO Rep. 5:567-571(2004).
RN [8]
RP FUNCTION.
RX PubMed=17438278; DOI=10.1073/pnas.0702357104;
RA Sahi C., Craig E.A.;
RT "Network of general and specialty J protein chaperones of the yeast
RT cytosol.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7163-7168(2007).
RN [9]
RP IDENTIFICATION BY 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: Putative chaperone involved in protein folding. Interferes
CC with propagation of [PSI+] prion when overproduced.
CC {ECO:0000269|PubMed:17438278}.
CC -!- INTERACTION:
CC P53940; P10591: SSA1; NbExp=2; IntAct=EBI-2612341, EBI-8591;
CC P53940; P10592: SSA2; NbExp=2; IntAct=EBI-2612341, EBI-8603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z71353; CAA95951.1; -; Genomic_DNA.
DR EMBL; AY723859; AAU09776.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10468.1; -; Genomic_DNA.
DR PIR; S63009; S63009.
DR RefSeq; NP_014322.1; NM_001182915.1.
DR AlphaFoldDB; P53940; -.
DR SMR; P53940; -.
DR BioGRID; 35746; 663.
DR DIP; DIP-7817N; -.
DR IntAct; P53940; 5.
DR MINT; P53940; -.
DR STRING; 4932.YNL077W; -.
DR iPTMnet; P53940; -.
DR MaxQB; P53940; -.
DR PaxDb; P53940; -.
DR PRIDE; P53940; -.
DR EnsemblFungi; YNL077W_mRNA; YNL077W; YNL077W.
DR GeneID; 855647; -.
DR KEGG; sce:YNL077W; -.
DR SGD; S000005021; APJ1.
DR VEuPathDB; FungiDB:YNL077W; -.
DR eggNOG; KOG0712; Eukaryota.
DR GeneTree; ENSGT00940000170598; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; P53940; -.
DR OMA; GPMVQTW; -.
DR BioCyc; YEAST:G3O-33106-MON; -.
DR Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR PRO; PR:P53940; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53940; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IGI:SGD.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888; PTHR43888; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..528
FT /note="J domain-containing protein APJ1"
FT /id="PRO_0000071155"
FT DOMAIN 4..73
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REPEAT 206..213
FT /note="CXXCXGXG motif"
FT REPEAT 218..225
FT /note="CXXCXGXG motif"
FT REPEAT 246..253
FT /note="CXXCXGXG motif"
FT REPEAT 262..269
FT /note="CXXCXGXG motif"
FT ZN_FING 193..274
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT REGION 485..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 58889 MW; AD6038F5B4768F9D CRC64;
MQQNTSLYDS LNVTAAASTS EIKKAYRNAA LKYHPDKNNH TEESKRKFQE ICQAYEILKD
NRLRALYDQY GTTDEVLIQE QQAQAQRQQA GPFSSSSNFD TEAMSFPDLS PGDLFAQFFN
SSATPSSNGS KSSFNFSFNN SSTPSFSFVN GSGVNNLYSS SAKYNSNDED HHLDRGPDIK
HNLKCTLKEL YMGKTAKLGL NRTRICSVCD GHGGLKKCTC KTCKGQGIQT QTRRMGPLVQ
SWSQTCADCG GAGVFVKNKD ICQQCQGLGF IKERKILQVT VQPGSCHNQL IVLTGEGDEV
ISTKGGGHEK VIPGDVVITI LRLKDPNFQV INYSNLICKK CKIDFMTSLC GGVVYIEGHP
SGKLIKLDII PGEILKPGCF KTVEDMGMPK FINGVRSGFG HLYVKFDVTY PERLEPENAK
KIQNILANDK YIKAERSTME TADSDCYCDL EKSYDSVEEH VLSSFEAPNL NNEVIEDDDL
GDLINERDSR KRNNRRFDES NINNNNETKR NKYSSPVSGF YDHDINGY
