TIM22_ASHGO
ID TIM22_ASHGO Reviewed; 201 AA.
AC Q75E80;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM22;
GN Name=TIM22; OrderedLocusNames=ABL148C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Essential core component of the TIM22 complex, a complex that
CC mediates the import and insertion of multi-pass transmembrane proteins
CC into the mitochondrial inner membrane. In the TIM22 complex, it
CC constitutes the voltage-activated and signal-gated channel. Forms a
CC twin-pore translocase that uses the membrane potential as external
CC driving force in 2 voltage-dependent steps (By similarity).
CC {ECO:0000250|UniProtKB:Q12328}.
CC -!- SUBUNIT: Component of the TIM22 complex, whose core is composed of
CC TIM22 and TIM54, associated with the 70 kDa heterohexamer composed of
CC TIM9 and TIM10 (or TIM8 and TIM13). {ECO:0000250|UniProtKB:Q12328}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q12328}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {ECO:0000305}.
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DR EMBL; AE016815; AAS50623.1; -; Genomic_DNA.
DR RefSeq; NP_982799.1; NM_208152.1.
DR AlphaFoldDB; Q75E80; -.
DR SMR; Q75E80; -.
DR STRING; 33169.AAS50623; -.
DR EnsemblFungi; AAS50623; AAS50623; AGOS_ABL148C.
DR GeneID; 4618879; -.
DR KEGG; ago:AGOS_ABL148C; -.
DR eggNOG; KOG3225; Eukaryota.
DR HOGENOM; CLU_091077_1_0_1; -.
DR InParanoid; Q75E80; -.
DR OMA; THSYAKN; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IBA:GO_Central.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
DR InterPro; IPR039175; TIM22.
DR PANTHER; PTHR14110; PTHR14110; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..201
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM22"
FT /id="PRO_0000228086"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 42..135
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PI78"
FT DISULFID 154..173
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PI78"
SQ SEQUENCE 201 AA; 21099 MW; E5257C12FA240545 CRC64;
MVYRGFGLEH ISPPVNKPFA EMTPEEQGER GAQMMMEFMT SCPGKSAISG VTGFALGGVF
GLFMASMAYD TPLHTPAPVG AGPGAGIPGA PTLQQMADLP LKQQIKIQFA DMGRRAYSSA
KNFGYIGMIY SGVECTIESL RAKNDLYNGV AAGCLTGGGL AYKSGPSAAL IGCAGFAAFS
TAIDLYMRSE NGRPPKNDFD E