ID   MIM1_SCHPO              Reviewed;          71 AA.
AC   Q9C1W7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Mitochondrial import protein 1;
GN   Name=mim1 {ECO:0000303|PubMed:33138913};
GN   ORFNames=SPBC713.08 {ECO:0000312|PomBase:SPBC713.08};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, IDENTIFICATION IN THE MIM COMPLEX, INTERACTION WITH MIM2 AND
RP   ATG43, AND DISRUPTION PHENOTYPE.
RX   PubMed=33138913; DOI=10.7554/elife.61245;
RA   Fukuda T., Ebi Y., Saigusa T., Furukawa K., Yamashita S.I., Inoue K.,
RA   Kobayashi D., Yoshida Y., Kanki T.;
RT   "Atg43 tethers isolation membranes to mitochondria to promote starvation-
RT   induced mitophagy in fission yeast.";
RL   Elife 9:61245-61245(2020).
CC   -!- FUNCTION: Component of the mitochondrial outer import machinery (MIM)
CC       complex that mediates transport of proteins into mitochondrial
CC       compartments (PubMed:33138913). Promotes the insertion of tom70 into
CC       the outer mitochondrial membrane (PubMed:33138913). Promotes the
CC       insertion of atg43 into the outer mitochondrial membrane
CC       (PubMed:33138913). The MIM complex cooperates with the receptor tom70
CC       in binding of precursor proteins and promotes their insertion and
CC       assembly into the outer membrane (By similarity). Involved in import of
CC       the subset of proteins with multiple alpha-helical transmembrane
CC       segments (By similarity). Required for the assembly of the TOM
CC       (translocase of outer membrane) receptor complex, which is responsible
CC       for the recognition and translocation of cytosolically synthesized
CC       mitochondrial preproteins (By similarity).
CC       {ECO:0000250|UniProtKB:Q08176, ECO:0000269|PubMed:33138913}.
CC   -!- SUBUNIT: Component of the mitochondrial outer import machinery (MIM)
CC       complex containing at least mim1 and mim2 (PubMed:33138913). Interacts
CC       with mim2 (PubMed:33138913). Interacts with mitophagy receptor atg43
CC       (PubMed:33138913). {ECO:0000269|PubMed:33138913}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q08176}.
CC   -!- DISRUPTION PHENOTYPE: Abnormal localization of atg43 to the outer
CC       mitochondrial membrane (PubMed:33138913). Severely decreases vegetative
CC       cell population growth (PubMed:33138913).
CC       {ECO:0000269|PubMed:33138913}.
CC   -!- SIMILARITY: Belongs to the MIM1 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAC22609.1; -; Genomic_DNA.
DR   RefSeq; NP_595347.1; NM_001021255.2.
DR   AlphaFoldDB; Q9C1W7; -.
DR   BioGRID; 277633; 3.
DR   MaxQB; Q9C1W7; -.
DR   PaxDb; Q9C1W7; -.
DR   EnsemblFungi; SPBC713.08.1; SPBC713.08.1:pep; SPBC713.08.
DR   GeneID; 2541118; -.
DR   KEGG; spo:SPBC713.08; -.
DR   PomBase; SPBC713.08; mim1.
DR   VEuPathDB; FungiDB:SPBC713.08; -.
DR   HOGENOM; CLU_2741478_0_0_1; -.
DR   InParanoid; Q9C1W7; -.
DR   OMA; HTRIYSI; -.
DR   PhylomeDB; Q9C1W7; -.
DR   PRO; PR:Q9C1W7; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:PomBase.
DR   GO; GO:0140595; C:MIM complex; IPI:PomBase.
DR   GO; GO:0005739; C:mitochondrion; EXP:PomBase.
DR   GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IBA:GO_Central.
DR   GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IMP:PomBase.
DR   InterPro; IPR013262; OMP_MIM1/TOM13_mt.
DR   PANTHER; PTHR28241; PTHR28241; 1.
DR   Pfam; PF08219; TOM13; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..71
FT                   /note="Mitochondrial import protein 1"
FT                   /id="PRO_0000218766"
FT   TRANSMEM        22..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   71 AA;  8041 MW;  3533A758727C03D6 CRC64;
     MEKNTVTVPK TLFSQVIHIF KYAAINLGLP FLNGVMLGFG EIFAHAFIHS LGWAPGHTRI
     YSIQRHQYIQ A