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OXA12_SCHPO
ID   OXA12_SCHPO             Reviewed;         409 AA.
AC   O43092;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Mitochondrial inner membrane protein oxa1-2;
DE   AltName: Full=Cytochrome oxidase biogenesis protein 1-2;
DE            Short=Sp2;
DE   Flags: Precursor;
GN   Name=oxa102; Synonyms=oxa1-2; ORFNames=SPBC1346.02c, SPBP4H10.03;
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 [MRNA], AND FUNCTION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10712694; DOI=10.1046/j.1365-2958.2000.01781.x;
RA   Bonnefoy N., Kermorgant M., Groudinsky O., Dujardin G.;
RT   "The respiratory gene OXA1 has two fission yeast orthologues which together
RT   encode a function essential for cellular viability.";
RL   Mol. Microbiol. 35:1135-1145(2000).
RN   [2]
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: Required for the insertion of integral membrane proteins into
CC       the mitochondrial inner membrane. Essential for the activity and
CC       assembly of cytochrome c oxidase. It is essential for viability while
CC       oxa101 is not. When both are deleted the cell is non-viable, suggesting
CC       that oxa101 act as a back-up for oxa102. {ECO:0000269|PubMed:10712694}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. {ECO:0000305}.
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DR   EMBL; X94124; CAA63844.1; -; mRNA.
DR   EMBL; CU329671; CAB83161.1; -; Genomic_DNA.
DR   PIR; T43703; T43703.
DR   PIR; T50311; T50311.
DR   RefSeq; NP_596177.1; NM_001022096.2.
DR   AlphaFoldDB; O43092; -.
DR   BioGRID; 276361; 2.
DR   STRING; 4896.SPBP4H10.03.1; -.
DR   MaxQB; O43092; -.
DR   PaxDb; O43092; -.
DR   EnsemblFungi; SPBP4H10.03.1; SPBP4H10.03.1:pep; SPBP4H10.03.
DR   GeneID; 2539811; -.
DR   KEGG; spo:SPBP4H10.03; -.
DR   PomBase; SPBP4H10.03; oxa102.
DR   VEuPathDB; FungiDB:SPBP4H10.03; -.
DR   eggNOG; KOG1239; Eukaryota.
DR   HOGENOM; CLU_029282_3_2_1; -.
DR   InParanoid; O43092; -.
DR   OMA; TVVKTHM; -.
DR   PhylomeDB; O43092; -.
DR   PRO; PR:O43092; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0032977; F:membrane insertase activity; ISO:PomBase.
DR   GO; GO:0051205; P:protein insertion into membrane; IBA:GO_Central.
DR   GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; ISO:PomBase.
DR   InterPro; IPR001708; YidC/ALB3/OXA1/COX18.
DR   PANTHER; PTHR12428; PTHR12428; 1.
DR   Pfam; PF02096; 60KD_IMP; 1.
PE   2: Evidence at transcript level;
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           ?..409
FT                   /note="Mitochondrial inner membrane protein oxa1-2"
FT                   /id="PRO_0000020359"
FT   TOPO_DOM        ?..75
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..114
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..188
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..235
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..275
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..409
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          369..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        350
FT                   /note="E -> V (in Ref. 1; CAA63844)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   409 AA;  45361 MW;  2918903E51B9BEB7 CRC64;
     MFSVIGRGIK FSSKSHYSVS CFLIATQGAK IRQIHTHNTF FKNFSFAKLG RNQRTSSLIK
     IHNSSTSFPK SRSEKVVYTP SLPLSSSVLA SFSFLPHNIL QNGLNTLHIW SGLPWWASIA
     ACAVAMRIAV FPIMLKMMKT SAKLAIINPK VAEHMSVLSK AKAEGNSELM MQATTQIQNL
     YKVNNVNPLN LLSAPVFQGI LFISFFYALK TMAGVPVEGF TDGGFWWVND LSQPDPLHIF
     PVANGLLMLL NIELGSETGS NKVAMSPSMK KFFRFLCLAS PLFTMNFPMA IFMYWFPSNV
     FSVFQGAFLR SSTIRHKLGL PEVPSAMPVP NAQNESFVKS FTDIVHGVQE KGKYPQASEI
     LDATRFLKTD TNNEQKPTNN STITKATTLS DNSQNDKSSS VTKPTEKKD
 
 
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