ID   RRP7A_MOUSE             Reviewed;         280 AA.
AC   Q9D1C9; Q3TWT8; Q8CCK8;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Ribosomal RNA-processing protein 7 homolog A;
DE   AltName: Full=Gastric cancer antigen Zg14 homolog;
GN   Name=Rrp7a;
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 MRNA].
RC   STRAIN=C57BL/6J, DBA/2J, and NOD;
RC   TISSUE=Amnion, Cerebellum, Heart, Olfactory bulb, and Thymus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Nucleolar protein that is involved in ribosomal RNA (rRNA)
CC       processing. Also plays a role in primary cilia resorption, and cell
CC       cycle progression in neurogenesis and neocortex development. Part of
CC       the small subunit (SSU) processome, first precursor of the small
CC       eukaryotic ribosomal subunit. During the assembly of the SSU processome
CC       in the nucleolus, many ribosome biogenesis factors, an RNA chaperone
CC       and ribosomal proteins associate with the nascent pre-rRNA and work in
CC       concert to generate RNA folding, modifications, rearrangements and
CC       cleavage as well as targeted degradation of pre-ribosomal RNA by the
CC       RNA exosome. {ECO:0000250|UniProtKB:Q9Y3A4}.
CC   -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more
CC       than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
CC       Interacts with NOL6; required for NOL6 localization to nucleolus.
CC       {ECO:0000250|UniProtKB:Q9Y3A4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9Y3A4}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q9Y3A4}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y3A4}.
CC   -!- SIMILARITY: Belongs to the RRP7 family. {ECO:0000305}.
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DR   EMBL; AK003698; BAB22944.1; -; mRNA.
DR   EMBL; AK032596; BAC27942.1; -; mRNA.
DR   EMBL; AK036247; BAC29360.1; -; mRNA.
DR   EMBL; AK088456; BAC40363.1; -; mRNA.
DR   EMBL; AK146821; BAE27459.1; -; mRNA.
DR   EMBL; AK159553; BAE35178.1; -; mRNA.
DR   EMBL; AK168189; BAE40149.1; -; mRNA.
DR   EMBL; AK168850; BAE40672.1; -; mRNA.
DR   EMBL; BC012523; AAH12523.1; -; mRNA.
DR   CCDS; CCDS27696.1; -.
DR   RefSeq; NP_083377.3; NM_029101.4.
DR   AlphaFoldDB; Q9D1C9; -.
DR   SMR; Q9D1C9; -.
DR   BioGRID; 217014; 4.
DR   STRING; 10090.ENSMUSP00000018184; -.
DR   iPTMnet; Q9D1C9; -.
DR   PhosphoSitePlus; Q9D1C9; -.
DR   EPD; Q9D1C9; -.
DR   MaxQB; Q9D1C9; -.
DR   PaxDb; 10090-ENSMUSP00000018184; -.
DR   ProteomicsDB; 299899; -.
DR   Pumba; Q9D1C9; -.
DR   Antibodypedia; 277; 155 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000018184.10; ENSMUSP00000018184.4; ENSMUSG00000018040.10.
DR   GeneID; 74778; -.
DR   KEGG; mmu:74778; -.
DR   UCSC; uc007wzy.3; mouse.
DR   AGR; MGI:1922028; -.
DR   CTD; 27341; -.
DR   MGI; MGI:1922028; Rrp7a.
DR   VEuPathDB; HostDB:ENSMUSG00000018040; -.
DR   eggNOG; KOG4008; Eukaryota.
DR   GeneTree; ENSGT00390000018482; -.
DR   HOGENOM; CLU_036234_2_1_1; -.
DR   InParanoid; Q9D1C9; -.
DR   OMA; VPPYCSE; -.
DR   OrthoDB; 5394928at2759; -.
DR   PhylomeDB; Q9D1C9; -.
DR   TreeFam; TF313949; -.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 74778; 27 hits in 78 CRISPR screens.
DR   ChiTaRS; Rrp7a; mouse.
DR   PRO; PR:Q9D1C9; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9D1C9; Protein.
DR   Bgee; ENSMUSG00000018040; Expressed in dentate gyrus of hippocampal formation granule cell and 75 other cell types or tissues.
DR   ExpressionAtlas; Q9D1C9; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0032545; C:CURI complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR   GO; GO:0034456; C:UTP-C complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR   GO; GO:0061523; P:cilium disassembly; ISS:UniProtKB.
DR   GO; GO:1902570; P:protein localization to nucleolus; IEA:Ensembl.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB.
DR   GO; GO:0042254; P:ribosome biogenesis; ISS:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR   CDD; cd12294; RRM_Rrp7A; 1.
DR   CDD; cd12951; RRP7_Rrp7A; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 6.10.250.1770; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR040447; RRM_Rrp7.
DR   InterPro; IPR040446; RRP7.
DR   InterPro; IPR024326; RRP7_C.
DR   InterPro; IPR034890; Rrp7A_RRM.
DR   PANTHER; PTHR13191; RIBOSOMAL RNA PROCESSING PROTEIN 7-RELATED; 1.
DR   PANTHER; PTHR13191:SF0; RIBOSOMAL RNA-PROCESSING PROTEIN 7 HOMOLOG A; 1.
DR   Pfam; PF17799; RRM_Rrp7; 1.
DR   Pfam; PF12923; RRP7; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   Genevisible; Q9D1C9; MM.
PE   2: Evidence at transcript level;
KW   Cell projection; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..280
FT                   /note="Ribosomal RNA-processing protein 7 homolog A"
FT                   /id="PRO_0000082009"
FT   DOMAIN          59..159
FT                   /note="RRM"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3A4"
FT   CONFLICT        103
FT                   /note="P -> Q (in Ref. 1; BAC27942)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   280 AA;  32399 MW;  4F2D324221B2AA3F CRC64;
     MVSRRKKRKA GGHEESIPSP PGYSAVPVKF SAKQQAPHYL YMRQHRVRQG TQSTWPPDRT
     LFILNVPPYC TQESLSRCLS CCGTIKTVEL QEKPDLAESP TEPKSQFFHP KPVPGFQVAY
     VVFQKPSGVS AALNLKGPLL VSTESHLVKS GIHKWISDYE DSVLDPEALR MEVDAFMEAY
     DKKIAEEEAK AKEEEGVPDE EGWVKVTRRG RRPVLPRTEA ASLRVLEKEK RKRARKELLN
     FYAWQHRETK MEHLAQLRKK FEEDKQRIEL MRAQRKFRPY
//