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COX20_SCHPO
ID   COX20_SCHPO             Reviewed;         120 AA.
AC   G2TRP9;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Cytochrome c oxidase assembly protein cox20, mitochondrial;
DE   Flags: Precursor;
GN   Name=cox20; ORFNames=SPBC25H2.18;
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.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- FUNCTION: Involved in the assembly of the cytochrome oxidase complex.
CC       Required for the maturation and subsequent assembly of the
CC       mitochondrially encoded cox2, the precursor of subunit 2 of cytochrome
CC       oxidase (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the COX20 family. {ECO:0000305}.
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DR   EMBL; CU329671; CCD31378.1; -; Genomic_DNA.
DR   RefSeq; XP_004001726.1; XM_004001677.1.
DR   AlphaFoldDB; G2TRP9; -.
DR   STRING; 4896.SPBC25H2.18.1; -.
DR   MaxQB; G2TRP9; -.
DR   PaxDb; G2TRP9; -.
DR   EnsemblFungi; SPBC25H2.18.1; SPBC25H2.18.1:pep; SPBC25H2.18.
DR   PomBase; SPBC25H2.18; cox20.
DR   VEuPathDB; FungiDB:SPBC25H2.18; -.
DR   eggNOG; ENOG502S3BD; Eukaryota.
DR   HOGENOM; CLU_2051005_0_0_1; -.
DR   InParanoid; G2TRP9; -.
DR   OMA; SFELCQM; -.
DR   PRO; PR:G2TRP9; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISO:PomBase.
DR   InterPro; IPR022533; Cox20.
DR   PANTHER; PTHR31586; PTHR31586; 1.
DR   Pfam; PF12597; DUF3767; 1.
DR   PIRSF; PIRSF007871; Cox20; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..120
FT                   /note="Cytochrome c oxidase assembly protein cox20,
FT                   mitochondrial"
FT                   /id="PRO_0000416667"
FT   TOPO_DOM        ?..36
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        37..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..120
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   REGION          98..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   120 AA;  13437 MW;  9665DF7C5480A985 CRC64;
     MSTPNEPEKP GIIDAFKSLK MSDFAHMVHH PCFKESLITS VVCGLGVGCI HLFLRAPISR
     AANWGFGTYF GMSIVSWEGC NYRKQLETNN FNIKITEAAE KTPKHRSSRS AQEIDEGFNE
 
 
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