IMP2L_SCHPO
ID IMP2L_SCHPO Reviewed; 180 AA.
AC Q9UST2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Mitochondrial inner membrane protease subunit 2;
DE EC=3.4.21.-;
GN ORFNames=SPBC336.13c;
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).
CC -!- FUNCTION: Catalyzes the removal of transit peptides required for the
CC targeting of proteins from the mitochondrial matrix, across the inner
CC membrane, into the inter-membrane space. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of 2 subunits, imp1 and imp2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB58165.1; -; Genomic_DNA.
DR PIR; T40251; T40251.
DR RefSeq; NP_596133.1; NM_001022051.2.
DR AlphaFoldDB; Q9UST2; -.
DR SMR; Q9UST2; -.
DR BioGRID; 276767; 20.
DR STRING; 4896.SPBC336.13c.1; -.
DR MaxQB; Q9UST2; -.
DR PaxDb; Q9UST2; -.
DR EnsemblFungi; SPBC336.13c.1; SPBC336.13c.1:pep; SPBC336.13c.
DR GeneID; 2540235; -.
DR KEGG; spo:SPBC336.13c; -.
DR PomBase; SPBC336.13c; -.
DR VEuPathDB; FungiDB:SPBC336.13c; -.
DR eggNOG; KOG1568; Eukaryota.
DR HOGENOM; CLU_028723_4_1_1; -.
DR InParanoid; Q9UST2; -.
DR OMA; IVWPPQR; -.
DR PhylomeDB; Q9UST2; -.
DR PRO; PR:Q9UST2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:PomBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; ISS:PomBase.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR037730; IMP2.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019533; Peptidase_S26.
DR PANTHER; PTHR46041; PTHR46041; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
PE 3: Inferred from homology;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion inner membrane; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..180
FT /note="Mitochondrial inner membrane protease subunit 2"
FT /id="PRO_0000259581"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 46
FT /evidence="ECO:0000250"
FT ACT_SITE 92
FT /evidence="ECO:0000250"
SQ SEQUENCE 180 AA; 20546 MW; BAEB6160B24FC0C3 CRC64;
MANPFVRNQS FKSVFFKNLV GITLWVPVLM FVEQHVVSVG TIEGRSMKPA FNPETNMLQR
DRVLLWKWNK DYKRGDVVIL RSPENPEELL VKRVLGVEYD IMKTRPPKKL SLVPVPEGHV
WVEGDEQFHS IDSNKFGPVS TGLITAKVIA ILFPFSRAGR IDHEGFRKNA VFLSGKRSVK