SHE9_YEAST
ID SHE9_YEAST Reviewed; 456 AA.
AC Q04172; D6VT27;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Sensitive to high expression protein 9, mitochondrial;
DE AltName: Full=Mitochondrial distribution and morphology protein 33;
DE Flags: Precursor;
GN Name=SHE9; Synonyms=MDM33; OrderedLocusNames=YDR393W; ORFNames=D9509.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=7762298; DOI=10.1002/yea.320110104;
RA Espinet C., de la Torre M.A., Aldea M., Herrero E.;
RT "An efficient method to isolate yeast genes causing overexpression-mediated
RT growth arrest.";
RL Yeast 11:25-32(1995).
RN [4]
RP FUNCTION.
RX PubMed=11907266; DOI=10.1091/mbc.01-12-0588;
RA Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N., Neupert W.,
RA Westermann B.;
RT "Genetic basis of mitochondrial function and morphology in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:847-853(2002).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12591915; DOI=10.1083/jcb.200211113;
RA Messerschmitt M., Jakobs S., Vogel F., Fritz S., Dimmer K.S., Neupert W.,
RA Westermann B.;
RT "The inner membrane protein Mdm33 controls mitochondrial morphology in
RT yeast.";
RL J. Cell Biol. 160:553-564(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).
CC -!- FUNCTION: Required for the maintenance of the structure of the
CC mitochondrial inner membrane. Involved in mitochondrial morphology.
CC Causes growth arrest when highly overexpressed.
CC {ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:12591915,
CC ECO:0000269|PubMed:7762298}.
CC -!- SUBUNIT: Homooligomer. Participates in a complex of about 300 kDa.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12591915}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12591915}.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SHE9 family. {ECO:0000305}.
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DR EMBL; U32274; AAB64835.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12237.1; -; Genomic_DNA.
DR PIR; S69677; S69677.
DR RefSeq; NP_010681.1; NM_001180701.1.
DR AlphaFoldDB; Q04172; -.
DR SMR; Q04172; -.
DR BioGRID; 32455; 294.
DR IntAct; Q04172; 11.
DR STRING; 4932.YDR393W; -.
DR iPTMnet; Q04172; -.
DR MaxQB; Q04172; -.
DR PaxDb; Q04172; -.
DR PRIDE; Q04172; -.
DR EnsemblFungi; YDR393W_mRNA; YDR393W; YDR393W.
DR GeneID; 852002; -.
DR KEGG; sce:YDR393W; -.
DR SGD; S000002801; SHE9.
DR VEuPathDB; FungiDB:YDR393W; -.
DR eggNOG; ENOG502QQ1E; Eukaryota.
DR HOGENOM; CLU_025632_5_1_1; -.
DR InParanoid; Q04172; -.
DR OMA; DIWERIK; -.
DR BioCyc; YEAST:G3O-29941-MON; -.
DR PRO; PR:Q04172; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04172; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR InterPro; IPR008839; MDM33_fungi.
DR PANTHER; PTHR31961; PTHR31961; 2.
DR Pfam; PF05546; She9_MDM33; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..456
FT /note="Sensitive to high expression protein 9,
FT mitochondrial"
FT /id="PRO_0000022344"
FT TOPO_DOM 31..296
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..435
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 71..128
FT /evidence="ECO:0000255"
FT COILED 178..277
FT /evidence="ECO:0000255"
SQ SEQUENCE 456 AA; 53571 MW; 0F24869626778766 CRC64;
MLRYYGATRN LPLVFSINKL MLRASSFTRP FHYSSYSLQN GDTPDKGSTN KNEIRTPNNA
VWKENIELQW QHLKKKLNEL YSRFNFHRDQ LSFQVNKAKK SIQEANRKLS EQENEINDSR
LNYNKDELTS AKIEGLPSER EQHRKKWSRK LEFYFDSLQE TLFTATRALN DVTGYSGIQK
LKSSISLMEK KLEATKKEHK LFKAQYANAI DERAQSQREV NELLQRQSAW SSSDLERFTQ
LYKNDALNAR QEQELKNKVK EIESKEEQLN DDLYRAILTR YHEEQIWSDK IRRTSTWGTF
ILMGMNIFLF IVLQLLLEPW KRKRLVGSFE DKVKSALNEY AKEQNMKMDK LLPGKSSEVT
DQGNTENSIV EEHIEQRGEC KINTAEIDRP EVATAETTTT EMKSFRDIWE RIKALFVTLK
SIQYRKLDAP LVFDTLEFYL YSISLVSMTI LVSGLI
