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OSB1_ARATH
ID   OSB1_ARATH              Reviewed;         261 AA.
AC   Q9SX99; Q9FZE9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Protein OSB1, mitochondrial;
DE   AltName: Full=Organellar single-stranded DNA-binding protein 1;
DE   Flags: Precursor;
GN   Name=OSB1; OrderedLocusNames=At1g47720; ORFNames=F16N3.2, T2E6.21;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   FUNCTION, MUTAGENESIS OF 199-TRP--ASP-201; 213-ASP-PHE-214 AND
RP   223-LEU-TRP-224, DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17189341; DOI=10.1105/tpc.106.042028;
RA   Zaegel V., Guermann B., Le Ret M., Andres C., Meyer D., Erhardt M.,
RA   Canaday J., Gualberto J.M., Imbault P.;
RT   "The plant-specific ssDNA binding protein OSB1 is involved in the
RT   stoichiometric transmission of mitochondrial DNA in Arabidopsis.";
RL   Plant Cell 18:3548-3563(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   PHE-28.
RX   PubMed=25732537; DOI=10.1093/jxb/erv064;
RA   Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT   "Identification of cleavage sites and substrate proteins for two
RT   mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL   J. Exp. Bot. 66:2691-2708(2015).
CC   -!- FUNCTION: Regulates mitochondrial DNA recombination. Represses
CC       homologous recombination, preventing mitochondrial genome instability
CC       and unbalanced transmission of alternative mtDNA configurations. Binds
CC       preferentially single-stranded DNA. Does not bind to RNA.
CC       {ECO:0000269|PubMed:17189341}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17189341,
CC       ECO:0000305|PubMed:25732537}.
CC   -!- TISSUE SPECIFICITY: Expressed in root elongation zone and in
CC       gametophytic cells. {ECO:0000269|PubMed:17189341}.
CC   -!- DOMAIN: The PDF region is required for protein-DNA interaction while
CC       the SSB domain is not required for ssDNA binding.
CC   -!- DISRUPTION PHENOTYPE: Severe leaf variegation, distortion and partial
CC       sterility. {ECO:0000269|PubMed:17189341}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF99794.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007519; AAD46017.1; -; Genomic_DNA.
DR   EMBL; AC012463; AAF99794.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32204.1; -; Genomic_DNA.
DR   EMBL; BT005269; AAO63333.1; -; mRNA.
DR   EMBL; AK119114; BAC43686.1; -; mRNA.
DR   RefSeq; NP_175203.2; NM_103665.3.
DR   AlphaFoldDB; Q9SX99; -.
DR   SMR; Q9SX99; -.
DR   STRING; 3702.AT1G47720.1; -.
DR   PaxDb; Q9SX99; -.
DR   PRIDE; Q9SX99; -.
DR   ProteomicsDB; 248910; -.
DR   EnsemblPlants; AT1G47720.1; AT1G47720.1; AT1G47720.
DR   GeneID; 841183; -.
DR   Gramene; AT1G47720.1; AT1G47720.1; AT1G47720.
DR   KEGG; ath:AT1G47720; -.
DR   Araport; AT1G47720; -.
DR   TAIR; locus:2015353; AT1G47720.
DR   eggNOG; ENOG502S048; Eukaryota.
DR   HOGENOM; CLU_049248_0_0_1; -.
DR   InParanoid; Q9SX99; -.
DR   OMA; DWWDNRR; -.
DR   OrthoDB; 1476527at2759; -.
DR   PhylomeDB; Q9SX99; -.
DR   PRO; PR:Q9SX99; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SX99; baseline and differential.
DR   Genevisible; Q9SX99; AT.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IBA:GO_Central.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IMP:TAIR.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IMP:TAIR.
DR   GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000424; Primosome_PriB/ssb.
DR   InterPro; IPR011344; ssDNA-bd.
DR   PANTHER; PTHR10302; PTHR10302; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:25732537"
FT   CHAIN           29..261
FT                   /note="Protein OSB1, mitochondrial"
FT                   /id="PRO_0000383608"
FT   DOMAIN          55..155
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00252"
FT   REGION          189..238
FT                   /note="PDF region"
FT   MUTAGEN         199..201
FT                   /note="WWD->GWG: Reduced ssDNA-binding."
FT                   /evidence="ECO:0000269|PubMed:17189341"
FT   MUTAGEN         213..214
FT                   /note="DF->GG: Reduced ssDNA-binding."
FT                   /evidence="ECO:0000269|PubMed:17189341"
FT   MUTAGEN         223..224
FT                   /note="LW->RG: Reduced ssDNA-binding."
FT                   /evidence="ECO:0000269|PubMed:17189341"
SQ   SEQUENCE   261 AA;  30564 MW;  E5FA365CC5844E97 CRC64;
     MNTFFKLGSL IQRTASQISS SFPKSRFFSD GESAVYHHAR LFKKPLSTKL KFNLVNSVSL
     MGFVDRSIQV MNTGPDRFGV FTILRVKDPL NPNRSFRISL RMWDAMARTC IAHLKLNDHI
     LVSGRLESYS KSSSDVYSGL NLDYQVKVAE VNYVAAPPSH VLDSQISKNP KTKTEDDIEE
     SKKDEIYLWQ VFFSNPYDWW DNRRNKKNPK QPDFKHKDTG EALWLCSDLP DWITRRLELF
     DQKNRFYDEE KTRRDRLSDY I
 
 
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