MIM2_SCHPO
ID MIM2_SCHPO Reviewed; 72 AA.
AC G2TRP0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Mitochondrial import protein 2 {ECO:0000250|UniProtKB:Q3E798};
DE AltName: Full=Transcripts altered in meiosis protein 7;
GN Name=mim2 {ECO:0000303|PubMed:33138913};
GN Synonyms=tam7 {ECO:0000303|PubMed:21270388};
GN ORFNames=SPBC409.23 {ECO:0000312|PomBase:SPBC409.23};
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 IDENTIFICATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE MIM COMPLEX, INTERACTION WITH MIM1 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). Involved in import of the subset of proteins with
CC multiple alpha-helical transmembrane segments (By similarity).
CC {ECO:0000250|UniProtKB:Q3E798, 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 mim1 (PubMed:33138913). Interacts with mitophagy receptor atg43
CC (PubMed:33138913). {ECO:0000269|PubMed:33138913}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q3E798}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Differentially expressed during meiosis.
CC {ECO:0000269|PubMed:21270388}.
CC -!- DISRUPTION PHENOTYPE: Abnormal localization of atg43 to the outer
CC mitochondrial membrane leading to abnormal mitophagy during nitrogen
CC starvation (PubMed:33138913). Leads to extremely slow growth at various
CC temperatures and delayed commitment to mitosis (PubMed:21270388,
CC PubMed:33138913). {ECO:0000269|PubMed:21270388,
CC ECO:0000269|PubMed:33138913}.
CC -!- SIMILARITY: Belongs to the MIM2 family. {ECO:0000305}.
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DR EMBL; CU329671; CCD31358.1; -; Genomic_DNA.
DR RefSeq; XP_004001705.1; XM_004001656.1.
DR AlphaFoldDB; G2TRP0; -.
DR SMR; G2TRP0; -.
DR STRING; 4896.SPBC409.23.1; -.
DR MaxQB; G2TRP0; -.
DR PaxDb; G2TRP0; -.
DR EnsemblFungi; SPBC409.23.1; SPBC409.23.1:pep; SPBC409.23.
DR PomBase; SPBC409.23; mim2.
DR VEuPathDB; FungiDB:SPBC409.23; -.
DR HOGENOM; CLU_2759254_0_0_1; -.
DR InParanoid; G2TRP0; -.
DR OMA; FHVWARW; -.
DR PRO; PR:G2TRP0; -.
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; IPR037652; Mim2.
DR PANTHER; PTHR28230; PTHR28230; 1.
DR Pfam; PF19117; Mim2; 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..72
FT /note="Mitochondrial import protein 2"
FT /id="PRO_0000416516"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3E798"
FT TRANSMEM 35..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..72
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q3E798"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 72 AA; 8397 MW; C72F39FFD5A07ABF CRC64;
MAEVLDLEID PISDGEDDTY SSELDDDLKD SIEQLERVLC LVVFPLLGKF LGRKFAFHAW
ARWLERRRLV SN
