JEM1_YEAST
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 03-AUG-2022, entry version 178.
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; 71.
DR IntAct; P40358; 1.
DR STRING; 4932.YJL073W; -.
DR MaxQB; P40358; -.
DR PaxDb; P40358; -.
DR PRIDE; P40358; -.
DR EnsemblFungi; YJL073W_mRNA; YJL073W; YJL073W.
DR GeneID; 853372; -.
DR KEGG; sce:YJL073W; -.
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 BioCyc; YEAST:G3O-31531-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0051087; F:chaperone binding; IGI:SGD.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 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
