SSBP_DANRE
ID SSBP_DANRE Reviewed; 146 AA.
AC B8A5I7; Q568F8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Single-stranded DNA-binding protein, mitochondrial {ECO:0000305};
DE Short=Mt-SSB {ECO:0000305};
DE Short=MtSSB {ECO:0000305};
DE Flags: Precursor;
GN Name=ssbp1 {ECO:0000312|ZFIN:ZDB-GENE-050417-340};
GN ORFNames=zgc:110325 {ECO:0000312|EMBL:AAH92875.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000312|EMBL:AAH92875.1, ECO:0000312|EMBL:AAI64281.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium {ECO:0000312|EMBL:AAH92875.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-37; ARG-106 AND
RP SER-140.
RX PubMed=31298765; DOI=10.1002/ana.25550;
RA Jurkute N., Leu C., Pogoda H.M., Arno G., Robson A.G., Nuernberg G.,
RA Altmueller J., Thiele H., Motameny S., Toliat M.R., Powell K., Hoehne W.,
RA Michaelides M., Webster A.R., Moore A.T., Hammerschmidt M., Nuernberg P.,
RA Yu-Wai-Man P., Votruba M.;
RT "SSBP1 mutations in dominant optic atrophy with variable retinal
RT degeneration.";
RL Ann. Neurol. 86:368-383(2019).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31550240; DOI=10.1172/jci128514;
RA Del Dotto V., Ullah F., Di Meo I., Magini P., Gusic M., Maresca A.,
RA Caporali L., Palombo F., Tagliavini F., Baugh E.H., Macao B., Szilagyi Z.,
RA Peron C., Gustafson M.A., Khan K., La Morgia C., Barboni P., Carbonelli M.,
RA Valentino M.L., Liguori R., Shashi V., Sullivan J., Nagaraj S.,
RA El-Dairi M., Iannaccone A., Cutcutache I., Bertini E., Carrozzo R.,
RA Emma F., Diomedi-Camassei F., Zanna C., Armstrong M., Page M., Stong N.,
RA Boesch S., Kopajtich R., Wortmann S., Sperl W., Davis E.E., Copeland W.C.,
RA Seri M., Falkenberg M., Prokisch H., Katsanis N., Tiranti V., Pippucci T.,
RA Carelli V.;
RT "SSBP1 mutations cause mtDNA depletion underlying a complex optic atrophy
RT disorder.";
RL J. Clin. Invest. 130:108-125(2020).
CC -!- FUNCTION: Binds preferentially and cooperatively to pyrimidine rich
CC single-stranded DNA (ss-DNA) (By similarity). May be required to
CC maintain the copy number of mitochondrial DNA (mtDNA) and play a
CC crucial role during mtDNA replication (PubMed:31550240). Required for
CC retinal ganglion cell differentiation and retinal integrity
CC (PubMed:31298765). {ECO:0000250|UniProtKB:Q04837,
CC ECO:0000269|PubMed:31298765, ECO:0000269|PubMed:31550240}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q04837}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250|UniProtKB:Q04837}.
CC -!- DISRUPTION PHENOTYPE: Morpholino-induced knockdown results in reduction
CC in optic nerve size and mitochondrial depletion (PubMed:31550240,
CC PubMed:31298765). Strongly reduced expression of the developmental
CC regulator genes isl1 and atoh7 in retinal ganglion cell (RGC)
CC precursors (PubMed:31298765). Nonphotoreceptor cells, both in the
CC ganglion cell layer and in the inner nuclear layer, display compromised
CC neuronal specification, whereas cell numbers in both layers are
CC unaltered (PubMed:31298765). {ECO:0000269|PubMed:31298765,
CC ECO:0000269|PubMed:31550240}.
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DR EMBL; BX546489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092875; AAH92875.1; -; mRNA.
DR EMBL; BC164281; AAI64281.1; -; mRNA.
DR RefSeq; NP_001017806.1; NM_001017806.1.
DR AlphaFoldDB; B8A5I7; -.
DR SMR; B8A5I7; -.
DR STRING; 7955.ENSDARP00000057506; -.
DR PaxDb; B8A5I7; -.
DR PeptideAtlas; B8A5I7; -.
DR PRIDE; B8A5I7; -.
DR Ensembl; ENSDART00000057507; ENSDARP00000057506; ENSDARG00000039350.
DR Ensembl; ENSDART00000193929; ENSDARP00000157021; ENSDARG00000039350.
DR GeneID; 550504; -.
DR KEGG; dre:550504; -.
DR CTD; 6742; -.
DR ZFIN; ZDB-GENE-050417-340; ssbp1.
DR eggNOG; KOG1653; Eukaryota.
DR GeneTree; ENSGT00390000002796; -.
DR HOGENOM; CLU_078758_2_1_1; -.
DR InParanoid; B8A5I7; -.
DR OMA; GNCIGRF; -.
DR OrthoDB; 1304218at2759; -.
DR PhylomeDB; B8A5I7; -.
DR TreeFam; TF314629; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000039350; Expressed in somite and 27 other tissues.
DR GO; GO:0042645; C:mitochondrial nucleoid; IBA:GO_Central.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006264; P:mitochondrial DNA replication; IBA:GO_Central.
DR GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
DR CDD; cd04496; SSB_OBF; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00984; SSB; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR011344; ssDNA-bd.
DR PANTHER; PTHR10302; PTHR10302; 1.
DR Pfam; PF00436; SSB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00621; ssb; 1.
DR PROSITE; PS50935; SSB; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-binding; Mitochondrion; Mitochondrion nucleoid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..146
FT /note="Single-stranded DNA-binding protein, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000453180"
FT DOMAIN 29..140
FT /note="SSB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00252"
FT MUTAGEN 37
FT /note="R->Q: Reduction in retinal atoh7 expression."
FT /evidence="ECO:0000269|PubMed:31298765"
FT MUTAGEN 106
FT /note="R->Q: Reduction in retinal atoh7 expression."
FT /evidence="ECO:0000269|PubMed:31298765"
FT MUTAGEN 140
FT /note="S->N: Reduction in retinal atoh7 expression."
FT /evidence="ECO:0000269|PubMed:31298765"
FT CONFLICT 4
FT /note="N -> Y (in Ref. 2; AAH92875/AAI64281)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="H -> Q (in Ref. 2; AAH92875/AAI64281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 146 AA; 16598 MW; A171D3A8CDA9F273 CRC64;
MLRNASAQIL KQFVRHRTTD ASLTLEKSIN KVQILGRVGQ DPVMRQVEGR NPVTIFSMAT
NEMWRSGEGE PVGAGDVTQK TTWHRISVFK PGLRDVAYQY VKKGSRIFVE GKLDYGEYVD
KNNVRRQATT IIADNIVFLS ENLRDQ
