ID MDY2_YEAST Reviewed; 212 AA. AC Q12285; D6W1V6; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 170. DE RecName: Full=Ubiquitin-like protein MDY2; DE AltName: Full=Golgi to ER traffic protein 5; DE AltName: Full=Mating-deficient protein 2; DE AltName: Full=Translation machinery-associated protein 24; GN Name=MDY2; Synonyms=GET5, TMA24; OrderedLocusNames=YOL111C; 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=7502582; DOI=10.1002/yea.320111108; RA Vandenbol M., Durand P., Portetelle D., Hilger F.; RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element."; RL Yeast 11:1069-1075(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(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 FUNCTION. RX PubMed=10514570; RX DOI=10.1002/(sici)1097-0061(199910)15:14<1529::aid-yea457>3.0.co;2-y; RA Iwanejko L., Smith K.N., Loeillet S., Nicolas A., Fabre F.; RT "Disruption and functional analysis of six ORFs on chromosome XV: YOL117w, RT YOL115w (TRF4), YOL114c, YOL112w (MSB4), YOL111c and YOL072w."; RL Yeast 15:1529-1539(1999). 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 FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16390866; DOI=10.1242/jcs.02754; RA Hu Z., Potthoff B., Hollenberg C.P., Ramezani-Rad M.; RT "Mdy2, a ubiquitin-like (UBL)-domain protein, is required for efficient RT mating in Saccharomyces cerevisiae."; RL J. Cell Sci. 119:326-338(2006). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1-59 IN COMPLEX WITH GET4, AND RP SUBCELLULAR LOCATION. RX PubMed=20106980; DOI=10.1074/jbc.m109.087098; RA Chang Y.W., Chuang Y.C., Ho Y.C., Cheng M.Y., Sun Y.J., Hsiao C.D., RA Wang C.; RT "Crystal structure of Get4-Get5 complex and its interactions with Sgt2, RT Get3, and Ydj1."; RL J. Biol. Chem. 285:9962-9970(2010). CC -!- FUNCTION: Required for efficient mating. Involved in the production of CC alpha-factor, the KAR9 and TUB1 location to the shmoo tip and nuclear CC migration into pheromone-induced shmoos. {ECO:0000269|PubMed:10514570, CC ECO:0000269|PubMed:16390866}. CC -!- SUBUNIT: Interacts with GET4. {ECO:0000269|PubMed:20106980}. CC -!- INTERACTION: CC Q12285; Q12154: GET3; NbExp=10; IntAct=EBI-34904, EBI-2989; CC Q12285; Q12125: GET4; NbExp=17; IntAct=EBI-34904, EBI-36940; CC Q12285; P31539: HSP104; NbExp=2; IntAct=EBI-34904, EBI-8050; CC Q12285; P22214: SEC22; NbExp=3; IntAct=EBI-34904, EBI-16577; CC Q12285; Q12118: SGT2; NbExp=15; IntAct=EBI-34904, EBI-31784; CC Q12285; P25491: YDJ1; NbExp=2; IntAct=EBI-34904, EBI-10420; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=Detected in CC both cytosol and nucleus but is predominantly cytosolic. CC -!- MISCELLANEOUS: Present with 6510 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; Z48149; CAA88151.1; -; Genomic_DNA. DR EMBL; Z74853; CAA99130.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10672.1; -; Genomic_DNA. DR PIR; S51888; S51888. DR RefSeq; NP_014530.1; NM_001183365.1. DR PDB; 2LNZ; NMR; -; A/B=152-212. DR PDB; 2LXA; NMR; -; A=74-151. DR PDB; 2LXC; NMR; -; A=74-151. DR PDB; 2WPV; X-ray; 1.99 A; B/D/F/H=1-59. DR PDB; 3LKU; X-ray; 2.80 A; B/D/F=3-56. DR PDB; 3VEJ; X-ray; 1.23 A; A/B=175-212. DR PDB; 3ZDM; X-ray; 1.80 A; C/F=71-151. DR PDB; 4A20; X-ray; 1.78 A; A=70-152. DR PDB; 4ASW; NMR; -; C=70-152. DR PDB; 4GOC; X-ray; 2.40 A; A/B/C=74-148. DR PDB; 4PWX; X-ray; 5.40 A; D/F=1-54. DR PDB; 5BW8; X-ray; 2.80 A; D=1-54. DR PDB; 5BWK; X-ray; 6.00 A; F/H/J/L/R/T/V/X=1-56. DR PDBsum; 2LNZ; -. DR PDBsum; 2LXA; -. DR PDBsum; 2LXC; -. DR PDBsum; 2WPV; -. DR PDBsum; 3LKU; -. DR PDBsum; 3VEJ; -. DR PDBsum; 3ZDM; -. DR PDBsum; 4A20; -. DR PDBsum; 4ASW; -. DR PDBsum; 4GOC; -. DR PDBsum; 4PWX; -. DR PDBsum; 5BW8; -. DR PDBsum; 5BWK; -. DR AlphaFoldDB; Q12285; -. DR BMRB; Q12285; -. DR SMR; Q12285; -. DR BioGRID; 34289; 350. DR ComplexPortal; CPX-1861; GET4-GET5 transmembrane domain recognition complex. DR DIP; DIP-1982N; -. DR IntAct; Q12285; 13. DR MINT; Q12285; -. DR STRING; 4932.YOL111C; -. DR TCDB; 3.A.21.1.1; the c-terminal tail-anchored membrane protein biogenesis/ insertion complex (tamp-b) family. DR MaxQB; Q12285; -. DR PaxDb; 4932-YOL111C; -. DR PeptideAtlas; Q12285; -. DR EnsemblFungi; YOL111C_mRNA; YOL111C; YOL111C. DR GeneID; 854038; -. DR KEGG; sce:YOL111C; -. DR AGR; SGD:S000005471; -. DR SGD; S000005471; MDY2. DR VEuPathDB; FungiDB:YOL111C; -. DR eggNOG; KOG0011; Eukaryota. DR HOGENOM; CLU_1294717_0_0_1; -. DR InParanoid; Q12285; -. DR OMA; NCMVSAP; -. DR OrthoDB; 2019738at2759; -. DR BioCyc; YEAST:G3O-33508-MONOMER; -. DR BioGRID-ORCS; 854038; 0 hits in 10 CRISPR screens. DR ChiTaRS; MDY2; yeast. DR EvolutionaryTrace; Q12285; -. DR PRO; PR:Q12285; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; Q12285; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0072380; C:TRC complex; IDA:SGD. DR GO; GO:0000753; P:cell morphogenesis involved in conjugation with cellular fusion; IMP:SGD. DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IDA:SGD. DR GO; GO:0045048; P:protein insertion into ER membrane; HGI:SGD. DR CDD; cd01805; Ubl_Rad23; 1. DR Gene3D; 1.10.286.70; Get5 dimerization domain; 1. DR Gene3D; 1.20.5.510; Single helix bin; 1. DR InterPro; IPR040474; Get5_C. DR InterPro; IPR031765; Mdy2_get4-bd. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR46555; UBIQUITIN-LIKE PROTEIN 4A; 1. DR PANTHER; PTHR46555:SF1; UBIQUITIN-LIKE PROTEIN 4A; 1. DR Pfam; PF16843; Get5_bdg; 1. DR Pfam; PF18514; Get5_C; 1. DR Pfam; PF00240; ubiquitin; 1. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Nucleus; Reference proteome. FT CHAIN 1..212 FT /note="Ubiquitin-like protein MDY2" FT /id="PRO_0000235917" FT DOMAIN 74..152 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT REGION 150..177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:3LKU" FT HELIX 8..20 FT /evidence="ECO:0007829|PDB:2WPV" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:2WPV" FT STRAND 74..80 FT /evidence="ECO:0007829|PDB:4A20" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:4A20" FT STRAND 86..92 FT /evidence="ECO:0007829|PDB:4A20" FT HELIX 98..107 FT /evidence="ECO:0007829|PDB:4A20" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:4A20" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:4A20" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:4A20" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:4A20" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:3ZDM" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:4A20" FT HELIX 179..189 FT /evidence="ECO:0007829|PDB:3VEJ" FT TURN 190..192 FT /evidence="ECO:0007829|PDB:3VEJ" FT HELIX 194..210 FT /evidence="ECO:0007829|PDB:3VEJ" SQ SEQUENCE 212 AA; 23732 MW; CE6FC4282E0E472C CRC64; MSTSASGPEH EFVSKFLTLA TLTEPKLPKS YTKPLKDVTN LGVPLPTLKY KYKQNRAKKL KLHQDQQGQD NAAVHLTLKK IQAPKFSIEH DFSPSDTILQ IKQHLISEEK ASHISEIKLL LKGKVLHDNL FLSDLKVTPA NSTITVMIKP NPTISKEPEA EKSTNSPAPA PPQELTVPWD DIEALLKNNF ENDQAAVRQV MERLQKGWSL AK //