SPAT5_MOUSE
ID SPAT5_MOUSE Reviewed; 893 AA.
AC Q3UMC0; A2ACU2; A3KG23; A3KG24; Q9CXZ7; Q9Z2K7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ribosome biogenesis protein SPATA5 {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P32794};
DE AltName: Full=Spermatogenesis-associated factor protein {ECO:0000303|PubMed:10734318};
DE AltName: Full=Spermatogenesis-associated protein 5;
GN Name=Spata5 {ECO:0000312|MGI:MGI:1927170};
GN Synonyms=Spaf {ECO:0000303|PubMed:10734318};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=10734318; DOI=10.1038/sj.onc.1203442;
RA Liu Y., Black J., Kisiel N., Kulesz-Martin M.F.;
RT "SPAF, a new AAA-protein specific to early spermatogenesis and malignant
RT conversion.";
RL Oncogene 19:1579-1588(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-271, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-271, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 SPATA5L1, C1orf109 ortholog and
CC CINP (By similarity). May be involved in morphological and functional
CC mitochondrial transformations during spermatogenesis (PubMed:10734318).
CC {ECO:0000250|UniProtKB:Q8NB90, ECO:0000269|PubMed:10734318}.
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:Q8NB90}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10734318}.
CC Mitochondrion {ECO:0000269|PubMed:10734318}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:Q8NB90}.
CC -!- TISSUE SPECIFICITY: Expressed in testis; with localization to
CC spermatogonia and early spermatocytes in the basal compartment of the
CC seminiferous tubules (at early stages of spermatogenesis). Very weak
CC signals observed in spleen and skin. {ECO:0000269|PubMed:10734318}.
CC -!- DOMAIN: The first ATP-binding region binds ATP with low affinity
CC whereas the second ATP-binding region binds ATP with high affinity.
CC {ECO:0000250|UniProtKB:P32794}.
CC -!- MISCELLANEOUS: Aberrantly expressed at the malignant conversion stage
CC in a clonal epidermal model of chemical carcinogenesis.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. AFG2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF049099; AAD02481.1; -; mRNA.
DR EMBL; AK011111; BAB27406.1; -; mRNA.
DR EMBL; AK144998; BAE26178.1; -; mRNA.
DR EMBL; AL669927; CAM21041.1; -; Genomic_DNA.
DR EMBL; AL627074; CAM21041.1; JOINED; Genomic_DNA.
DR EMBL; AL669927; CAM21042.1; -; Genomic_DNA.
DR EMBL; AL627074; CAM21042.1; JOINED; Genomic_DNA.
DR EMBL; AL627074; CAM25218.1; -; Genomic_DNA.
DR EMBL; AL669927; CAM25218.1; JOINED; Genomic_DNA.
DR EMBL; AL627074; CAM25219.1; -; Genomic_DNA.
DR EMBL; AL669927; CAM25219.1; JOINED; Genomic_DNA.
DR EMBL; AL645968; CAM46305.1; -; Genomic_DNA.
DR EMBL; AL645968; CAM46306.1; -; Genomic_DNA.
DR CCDS; CCDS50895.1; -.
DR RefSeq; NP_001156983.1; NM_001163511.2.
DR RefSeq; NP_001297402.1; NM_001310473.1.
DR RefSeq; NP_067318.2; NM_021343.3.
DR AlphaFoldDB; Q3UMC0; -.
DR SMR; Q3UMC0; -.
DR BioGRID; 208337; 3.
DR IntAct; Q3UMC0; 1.
DR STRING; 10090.ENSMUSP00000103747; -.
DR iPTMnet; Q3UMC0; -.
DR PhosphoSitePlus; Q3UMC0; -.
DR EPD; Q3UMC0; -.
DR jPOST; Q3UMC0; -.
DR MaxQB; Q3UMC0; -.
DR PaxDb; Q3UMC0; -.
DR PRIDE; Q3UMC0; -.
DR ProteomicsDB; 257336; -.
DR Antibodypedia; 26869; 53 antibodies from 18 providers.
DR DNASU; 57815; -.
DR Ensembl; ENSMUST00000108112; ENSMUSP00000103747; ENSMUSG00000027722.
DR GeneID; 57815; -.
DR KEGG; mmu:57815; -.
DR UCSC; uc008pav.2; mouse.
DR CTD; 166378; -.
DR MGI; MGI:1927170; Spata5.
DR VEuPathDB; HostDB:ENSMUSG00000027722; -.
DR eggNOG; KOG0730; Eukaryota.
DR GeneTree; ENSGT00940000157323; -.
DR InParanoid; Q3UMC0; -.
DR OMA; KIKLRAM; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; Q3UMC0; -.
DR TreeFam; TF314525; -.
DR BioGRID-ORCS; 57815; 22 hits in 75 CRISPR screens.
DR ChiTaRS; Spata5; mouse.
DR PRO; PR:Q3UMC0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3UMC0; protein.
DR Bgee; ENSMUSG00000027722; Expressed in spermatocyte and 261 other tissues.
DR ExpressionAtlas; Q3UMC0; baseline and differential.
DR Genevisible; Q3UMC0; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:1990275; F:preribosome binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Hydrolase; Isopeptide bond; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ribosome biogenesis; Spermatogenesis; Ubl conjugation.
FT CHAIN 1..893
FT /note="Ribosome biogenesis protein SPATA5"
FT /id="PRO_0000330584"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394..401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32794"
FT BINDING 668..675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32794"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NB90"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NB90"
FT CROSSLNK 859
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NB90"
FT CONFLICT 54
FT /note="Missing (in Ref. 1; AAD02481 and 3; CAM46306/
FT CAM21041)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="L -> P (in Ref. 1; AAD02481, 2; BAE26178 and 3;
FT CAM46305/CAM46306)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="S -> N (in Ref. 1; AAD02481 and 3; CAM46305/
FT CAM46306)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="Q -> E (in Ref. 1; AAD02481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 97256 MW; 1B5FF96EDC9B9596 CRC64;
MSSKKNRKRQ KEGAEGASPS LSAAPSRSGT STPFAQPSPA APGMLVVTNF LEKVDGKVPK
TFQNSLVHLG LNTMKSANIC IGRPVLLTSL DGKQEVYTAW PVAGFPGGKV GLSEMAQKNV
GVRAGETIQV QPLLGAVLQA QEMDLALSDK DKEINEEELT GCILRKLDGK IVLPGNFLYC
TFYGRLCKLQ VLQVKGTDGT TLGKLQSASG TDAQGMASEH SSMESSDVDL SFQLSQLDLK
EPQSPSSQST PCKPTNDRTV NKAGEVLLDV TQSPRDGSGL GLEESTGLKC SFDSSKEGNT
QPVSEEKLLK PASAGTKSNT DTFYFISSTT RINLRKICTN SKEQDSQFKV TYDMIGGLNS
QLKAIREIIE LPLKQPELFK SYGIPAPRGL LLYGPPGTGK TMIARAVANE VGAYVSVING
PEIISKFYGE TEARLRQIFA EATLRHPSII FIDELDALCP KREGAQSEVE KRVVASLLTL
MDGIGSEGSE GRVLVLGATN RPQALDAALR RPGRFDKEIE IGIPNAQDRL DILQKLLRRV
PHLLTKAELL RLANNAHGYV GADLKALCNE AGLHALRRVL RKQPNLPDSK VAGMVKITLN
DFLQGMNDIR PSAMREVAID VPNVSWSDIG GLENIKLKLK QAVEWPLKHP KSFNRMGIQP
PKGVLLYGPP GCSKTMIAKA LANESGLNFL AIKGPELMNK YVGESERAVR EIFRKARAVA
PSIIFFDELD ALAVERGSSS GAGNVADRVL AQLLTEMDGI EQLKNVTVLA ATNRPDRIDK
ALMRPGRIDR IIYVPLPDAA TRREILNLQF HSMPISNEVD LDELVLQTDT YSGAEIIAVC
KEAALLALEE NIKADCIMKR HFTQALSIVT PRIPESLRRF YEDYQEKSGL HTV
