SPA5L_MOUSE
ID SPA5L_MOUSE Reviewed; 747 AA.
AC A0A7N9VSG0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Ribosome biogenesis protein SPATA5L1 {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P32794};
DE AltName: Full=Spermatogenesis-associated protein 5-like protein 1;
GN Name=Spata5l1 {ECO:0000303|PubMed:34626583, ECO:0000312|MGI:MGI:3036261};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=34626583; DOI=10.1016/j.ajhg.2021.08.003;
RA Richard E.M., Bakhtiari S., Marsh A.P.L., Kaiyrzhanov R., Wagner M.,
RA Shetty S., Pagnozzi A., Nordlie S.M., Guida B.S., Cornejo P., Magee H.,
RA Liu J., Norton B.Y., Webster R.I., Worgan L., Hakonarson H., Li J., Guo Y.,
RA Jain M., Blesson A., Rodan L.H., Abbott M.A., Comi A., Cohen J.S.,
RA Alhaddad B., Meitinger T., Lenz D., Ziegler A., Kotzaeridou U., Brunet T.,
RA Chassevent A., Smith-Hicks C., Ekstein J., Weiden T., Hahn A.,
RA Zharkinbekova N., Turnpenny P., Tucci A., Yelton M., Horvath R., Gungor S.,
RA Hiz S., Oktay Y., Lochmuller H., Zollino M., Morleo M., Marangi G.,
RA Nigro V., Torella A., Pinelli M., Amenta S., Husain R.A., Grossmann B.,
RA Rapp M., Steen C., Marquardt I., Grimmel M., Grasshoff U., Korenke G.C.,
RA Owczarek-Lipska M., Neidhardt J., Radio F.C., Mancini C.,
RA Claps Sepulveda D.J., McWalter K., Begtrup A., Crunk A.,
RA Guillen Sacoto M.J., Person R., Schnur R.E., Mancardi M.M., Kreuder F.,
RA Striano P., Zara F., Chung W.K., Marks W.A., van Eyk C.L., Webber D.L.,
RA Corbett M.A., Harper K., Berry J.G., MacLennan A.H., Gecz J., Tartaglia M.,
RA Salpietro V., Christodoulou J., Kaslin J., Padilla-Lopez S., Bilguvar K.,
RA Munchau A., Ahmed Z.M., Hufnagel R.B., Fahey M.C., Maroofian R.,
RA Houlden H., Sticht H., Mane S.M., Rad A., Vona B., Jin S.C., Haack T.B.,
RA Makowski C., Hirsch Y., Riazuddin S., Kruer M.C.;
RT "Bi-allelic variants in SPATA5L1 lead to intellectual disability, spastic-
RT dystonic cerebral palsy, epilepsy, and hearing loss.";
RL Am. J. Hum. Genet. 108:2006-2016(2021).
CC -!- FUNCTION: ATP-dependent chaperone, which plays an essential role in the
CC cytoplasmic maturation steps of pre-60S ribosomal particles by
CC promoting the release of shuttling protein RSL24D1/RLP24 from the pre-
CC ribosomal particles. Acts together with SPATA5, C1orf109 ortholog and
CC CINP. {ECO:0000250|UniProtKB:Q9BVQ7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:P32794};
CC -!- SUBUNIT: Associates with pre-60S ribosomal particles. Interacts with
CC C1orf109 ortholog. {ECO:0000250|UniProtKB:Q9BVQ7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BVQ7}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BVQ7}.
CC Nucleus {ECO:0000250|UniProtKB:D4A2B7}.
CC -!- TISSUE SPECIFICITY: In adult ear, expressed at low levels in
CC neurosensory hair cells (inner and outer) and supporting cells (pillar
CC and Deiter cells). {ECO:0000269|PubMed:34626583}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. AFG2 subfamily.
CC {ECO:0000305}.
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DR RefSeq; NP_001028428.2; NM_001033256.4.
DR SMR; A0A7N9VSG0; -.
DR Ensembl; ENSMUST00000239506.1; ENSMUSP00000159384.2; ENSMUSG00000118663.1.
DR GeneID; 214616; -.
DR KEGG; mmu:214616; -.
DR CTD; 79029; -.
DR MGI; MGI:3036261; Spata5l1.
DR GeneTree; ENSGT00940000160700; -.
DR OMA; RAPDLCD; -.
DR Proteomes; UP000000589; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:1990275; F:preribosome binding; ISS:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat;
KW Ribosome biogenesis.
FT CHAIN 1..747
FT /note="Ribosome biogenesis protein SPATA5L1"
FT /id="PRO_0000456283"
FT BINDING 234..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 500..507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVQ7"
SQ SEQUENCE 747 AA; 80742 MW; 529F13F6F6066D6D CRC64;
MAPDSGPFPD GQLLKLLPVD PRDRDTQRCR LGPAAFRSLG ARLGSPLRIS LPAGGCCLCT
AWPRRDRVDG FVQLDPQCAS PGARVATGRI GMDCLQPVPC PPLRRLEVWP VLRPQAGAPS
SAAVLEVVHE LLRNRPVSRG HVVTTPPGVP GPVAALHVMG GTPDPEPGGW VTPHTRITLS
DKPPPQVEPP GEVTLGGLSE TADSLRELLR LPLRYPLALA ALGLAVPRGV LLAGPPGVGK
TQLVRAVARE TGAELLAVSA PALQGSRPGE TEENVRRIFQ RAQELASRGP SLLFLDEVDA
LCPRRGGPHR APESRVVAQV LTLLDGIHRD REFVVVGATN RPDELDPALR RPGRFDREVV
IGTPTLKQRE AILQVITSKM PISSHIDLGL LAEMTVGYVG ADLTALCREA AMCALLKNEK
NQDSPKIEET DFLEAFKKIQ PSSFRSSTGL MDIKPVGWEQ IGGLEDVKLK LKQCVEWPLK
FPQEFARMGL TQPKGLLLYG PPGCAKTTLV RALATGCHCS FVSVCGADLF SPFVGDSEKV
LSQVFRQARA NTPALVFLDE IDSVLGSRSV GTSGCDARER VLSVLLNELD GVGVRTVERR
GSKASQQECQ EILSRSVMIV VATNRPDVLD DALLRPGRLD KIIYVPPPDQ EGRLSILKVC
TNNMPVGPDV SLENLAAETC FFSGADLRNL CKEAALFALQ ENGLEATTVR QEHFTEALKT
VKPSLTLKEL TFYENLFKKG LSNLEDD
