ID   JEM1_YEAST              Reviewed;         645 AA.
AC   P40358; D6VWB0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 3.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=DnaJ-like chaperone JEM1;
DE   AltName: Full=DnaJ-like protein of the ER membrane 1;
DE   Flags: Precursor;
GN   Name=JEM1; Synonyms=KAR8; OrderedLocusNames=YJL073W;
GN   ORFNames=HRC558, J1083;
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], IDENTIFICATION OF INITIATION SITE,
RP   FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=9148890; DOI=10.1074/jbc.272.20.12889;
RA   Nishikawa S., Endo T.;
RT   "The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum
RT   membrane required for nuclear fusion.";
RL   J. Biol. Chem. 272:12889-12892(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RA   Sor F.J.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-645.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7762302; DOI=10.1002/yea.320110108;
RA   Vandenbol M., Durand P., Dion C., Portetelle D., Hilger F.;
RT   "Sequence of a 17.1 kb DNA fragment from chromosome X of Saccharomyces
RT   cerevisiae includes the mitochondrial ribosomal protein L8.";
RL   Yeast 11:57-60(1995).
RN   [6]
RP   INTERACTION WITH MPS3.
RX   PubMed=12493774; DOI=10.1074/jbc.m210934200;
RA   Nishikawa S., Terazawa Y., Nakayama T., Hirata A., Makio T., Endo T.;
RT   "Nep98p is a component of the yeast spindle pole body and essential for
RT   nuclear division and fusion.";
RL   J. Biol. Chem. 278:9938-9943(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   SUBCELLULAR LOCATION.
RX   PubMed=15282802; DOI=10.1002/yea.1133;
RA   Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.;
RT   "Localization of proteins that are coordinately expressed with Cln2 during
RT   the cell cycle.";
RL   Yeast 21:793-800(2004).
CC   -!- FUNCTION: Acts as a DnaJ-like chaperone required for nuclear membrane
CC       fusion during mating. {ECO:0000269|PubMed:9148890}.
CC   -!- SUBUNIT: Interacts with MPS3. {ECO:0000269|PubMed:12493774}.
CC   -!- INTERACTION:
CC       P40358; P47069: MPS3; NbExp=2; IntAct=EBI-25940, EBI-25811;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:9148890}; Single-pass type IV membrane protein
CC       {ECO:0000269|PubMed:9148890}. Nucleus membrane
CC       {ECO:0000269|PubMed:15282802}.
CC   -!- MISCELLANEOUS: Present with 3180 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA61312.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA89365.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X88851; CAA61312.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z49348; CAA89365.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z34288; CAA84049.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08726.1; -; Genomic_DNA.
DR   PIR; S56849; S56849.
DR   RefSeq; NP_012462.3; NM_001181506.3.
DR   AlphaFoldDB; P40358; -.
DR   SMR; P40358; -.
DR   BioGRID; 33682; 75.
DR   IntAct; P40358; 1.
DR   STRING; 4932.YJL073W; -.
DR   MaxQB; P40358; -.
DR   PaxDb; 4932-YJL073W; -.
DR   PeptideAtlas; P40358; -.
DR   EnsemblFungi; YJL073W_mRNA; YJL073W; YJL073W.
DR   GeneID; 853372; -.
DR   KEGG; sce:YJL073W; -.
DR   AGR; SGD:S000003609; -.
DR   SGD; S000003609; JEM1.
DR   VEuPathDB; FungiDB:YJL073W; -.
DR   eggNOG; KOG0715; Eukaryota.
DR   HOGENOM; CLU_030116_0_0_1; -.
DR   InParanoid; P40358; -.
DR   OMA; DMDYKPC; -.
DR   OrthoDB; 178259at2759; -.
DR   BioCyc; YEAST:G3O-31531-MONOMER; -.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 853372; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P40358; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P40358; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:SGD.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IGI:SGD.
DR   GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:SGD.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; IGI:SGD.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR44140; LD25575P; 1.
DR   PANTHER; PTHR44140:SF2; LD25575P; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..645
FT                   /note="DnaJ-like chaperone JEM1"
FT                   /id="PRO_0000043353"
FT   TOPO_DOM        23..190
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:9148890"
FT   TRANSMEM        191..211
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        212..645
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:9148890"
FT   DOMAIN          538..608
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          511..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  75144 MW;  43F219CD606F5D90 CRC64;
     MILISGYCLL VYSVILPVLI SASKLCDLAE LQRLNKNLKV DTESLPKYQW IAGQLEQNCM
     TADPASENMS DVIQLANQIY YKIGLIQLSN DQHLRAINTF EKIVFNETYK GSFGKLAEKR
     LQELYVDFGM WDKVHQKDDQ YAKYLSLNET IRNKISSKDV SVEEDISELL RITPYDVNVL
     STHIDVLFHK LAEEIDVSLA AAIILDYETI LDKHLASLSI DTRLSIHYVI SVLQTFVLNS
     DASFNIRKCL SIDMDYDKCK KLSLTISKLN KVNPSKRQIL DPATYAFENK KFRSWDRIIE
     FYLKDKKPFI TPMKILNKDT NFKNNYFFLE EIIKQLIEDV QLSRPLAKNL FEDPPITDGF
     VKPKSYYHTD YLVYIDSILC QASSMSPDVK RAKLAAPFCK KSLRHSLTLE TWKHYQDAKS
     EQKPLPETVL SDVWNSNPHL LMYMVNSILN KSRSKPHSQF KKQLYDQINK FFQDNGLSES
     TNPYVMKNFR LLQKQLQTYK EHKHRNFNQQ YFQQQQQQQQ HQRHQAPPAA PNYDPKKDYY
     KILGVSPSAS SKEIRKAYLN LTKKYHPDKI KANHNDKQES IHETMSQINE AYETLSDDDK
     RKEYDLSRSN PRRNTFPQGP RQNNMFKNPG SGFPFGNGFK MNFGL
//