ID   SHE9_YEAS7              Reviewed;         456 AA.
AC   A6ZYZ4;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 36.
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; ORFNames=SCY_1282;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SHE9 family. {ECO:0000305}.
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DR   EMBL; AAFW02000145; EDN60724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZYZ4; -.
DR   SMR; A6ZYZ4; -.
DR   PRIDE; A6ZYZ4; -.
DR   EnsemblFungi; EDN60724; EDN60724; SCY_1282.
DR   HOGENOM; CLU_025632_5_1_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008839; MDM33_fungi.
DR   PANTHER; PTHR31961; PTHR31961; 2.
DR   Pfam; PF05546; She9_MDM33; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   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_0000351067"
FT   TOPO_DOM        32..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;  53561 MW;  F877ED23308B6F06 CRC64;
     MLRYYGATRN LPLVFSINKF MLRPSSFARP FHYSSYSLQN DDTPDKGSTN KSEIRTPNNT
     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
     DQGNTKNSIV EEHIEQRGEC KINTAETDRP EVATAEATTT AMKSFRDIWE RIKALFVTLK
     SIQYRKLDAP LVFDTLEFYL YSISLVSMTI LVSGLI