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Database: UniProt
Entry: MSS51_SCHPO
LinkDB: MSS51_SCHPO
Original site: MSS51_SCHPO 
ID   MSS51_SCHPO             Reviewed;         378 AA.
AC   Q9UTB4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Protein mss51;
GN   Name=mss51; ORFNames=SPAC25B8.04c;
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: Has a dual role in the assembly of cytochrome oxidase subunit
CC       1 (cox1). It has a regulative function on cox1 synthesis, acting as a
CC       translational activator specific for the cox1 mRNA, and it also binds
CC       to newly synthesized cox1 protein (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MSS51 family. {ECO:0000305}.
CC   -!- CAUTION: Although no clear MSS51 ortholog is encoded in mammalian
CC       genomes, the mammalian MSS51/ZMYND17 protein of unknown function is
CC       significantly similar. {ECO:0000305}.
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DR   EMBL; CU329670; CAB61770.1; -; Genomic_DNA.
DR   PIR; T50191; T50191.
DR   RefSeq; NP_594464.1; NM_001019893.2.
DR   AlphaFoldDB; Q9UTB4; -.
DR   BioGRID; 278090; 14.
DR   STRING; 284812.Q9UTB4; -.
DR   iPTMnet; Q9UTB4; -.
DR   MaxQB; Q9UTB4; -.
DR   PaxDb; 4896-SPAC25B8-04c-1; -.
DR   EnsemblFungi; SPAC25B8.04c.1; SPAC25B8.04c.1:pep; SPAC25B8.04c.
DR   GeneID; 2541593; -.
DR   KEGG; spo:SPAC25B8.04c; -.
DR   PomBase; SPAC25B8.04c; mss51.
DR   VEuPathDB; FungiDB:SPAC25B8.04c; -.
DR   eggNOG; ENOG502QQBW; Eukaryota.
DR   HOGENOM; CLU_033072_0_0_1; -.
DR   InParanoid; Q9UTB4; -.
DR   OMA; VAVKANW; -.
DR   PhylomeDB; Q9UTB4; -.
DR   PRO; PR:Q9UTB4; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:PomBase.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:PomBase.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR046824; Mss51-like_C.
DR   InterPro; IPR032717; Mss51_Znf.
DR   PANTHER; PTHR28069; GH20023P; 1.
DR   PANTHER; PTHR28069:SF1; PROTEIN MSS51, MITOCHONDRIAL; 1.
DR   Pfam; PF20179; MSS51_C; 1.
DR   Pfam; PF13824; zf-Mss51; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; mRNA processing;
KW   mRNA splicing; Reference proteome.
FT   CHAIN           1..378
FT                   /note="Protein mss51"
FT                   /id="PRO_0000352654"
SQ   SEQUENCE   378 AA;  43600 MW;  0D4B8BFCB18623A7 CRC64;
     MSFLKNLFKK KSPTHELFHP LSRSPLTALR RRSEHIKQVY RCPISGKSVE YECPESGFPT
     HCNRTHWEQD KIHQSLIPKL RQINEDYHDL ARPNPLPELL KLPGPMEEDE VVSLLSWDSF
     FYTRDFPKFQ SSRTARHITS LLTYPMSIGA ILHKNSPYNL KNGLTPQGLQ SLTALRYMLH
     RPLSAQSTDP RPTRIFVLGA TKECSLPPSI WLQGLNFLFP GRLFQLHFIG PEVVVPSKQP
     NLPSPLSLHF HQDYYHNLHR VGAFEPFDPY YDTFFLPMPL ISHPLYSSSW IPTLHDLVST
     RCSVWLTSPS SQRTTKDLEV LNNVLKDSIE PLLLPTVNKF ASLGWSVDDS NLHEVYHANQ
     EVFGFRALYY NVQNVSKE
//
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