SPA5L_RAT
ID SPA5L_RAT Reviewed; 747 AA.
AC D4A2B7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 92.
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|RGD:1595990};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND 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:0000269|PubMed:34626583}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons; also expressed at lower level
CC in astrocytes, oligodendrocytes and microglia.
CC {ECO:0000269|PubMed:34626583}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. AFG2 subfamily.
CC {ECO:0000305}.
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DR EMBL; CH473949; EDL80042.1; -; Genomic_DNA.
DR RefSeq; NP_001103117.1; NM_001109647.1.
DR SMR; D4A2B7; -.
DR STRING; 10116.ENSRNOP00000040861; -.
DR Ensembl; ENSRNOT00000043414.4; ENSRNOP00000040861.3; ENSRNOG00000000169.6.
DR GeneID; 691729; -.
DR KEGG; rno:691729; -.
DR UCSC; RGD:1595990; rat.
DR CTD; 79029; -.
DR RGD; 1595990; Spata5l1.
DR eggNOG; KOG0730; Eukaryota.
DR GeneTree; ENSGT00940000160700; -.
DR HOGENOM; CLU_000688_12_2_1; -.
DR OMA; RAPDLCD; -.
DR OrthoDB; 194195at2759; -.
DR TreeFam; TF325792; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000000169; Expressed in thymus and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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; 2.
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_0000456284"
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; 80414 MW; C884DBA1BD0F14E2 CRC64;
MAPDSGPFPD GQFLKLLPVD PRDRGTQRCR LGPAAFRSLG VRLGSPMRIS LPAGGCCLCT
AWPRRDGADG FVQLDLQCAS PGAAAAAGRI SMDRLQPVSC PPLRRLEVWP VLRPQAGAPS
SDAVLEVSQE LLRNRPVSRG HVVATPPGIP GPVAALHVVS GTPDPEPAGR VTPHTRITLS
DKPPPQVEPP GEVTLGGLSE TADSLRELLR LPLCYPLALA ALGLAVPRGV LLAGPPGVGK
TQLVRAVARE AGAELLAVSA PALQGTRPGE TEENVRRVFQ RAQELASRGP SLLFLDEVDA
LCPRRGGPQR APESRVVAQV LTLLDGIHGD REVVVVGATN RPDELDPALR RPGRFDREVI
IGTPTLKQRE AILGVITSKM PISSHIDLGL LAEMTVGYVG ADLTALCREA ATCALLKNEK
NQNNPKIEET DFLEAFKKVQ PSSFRSSIGL TDIRPVGWEQ IGGLEDVKLK LKQCVEWPLK
FPQEFARMGL TQPKGLLLYG PPGCAKTTLV RALATSCHCS FVSVCGADLF SPFVGDSEKV
LSQVFRQARA NTPALVFLDE IDSVLGSRSV GSSGCDARER VLSVLLNELD GVGVRTVERR
GSKASQQECQ EILSRSVMIV VATNRPDVLD DALLRPGRLD KMVYVPPPDR EGRLSILKVC
TNNMPIGLNV SLENLAAETC YFSGADLRNL CKEAALFALQ ENGLEATTVE QEHFTEALKT
VKPSLTLKDL TFYENLFKKE LSNLEDH
