NOB1_MOUSE
ID NOB1_MOUSE Reviewed; 403 AA.
AC Q8BW10; Q7TPR3; Q9CRD7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=RNA-binding protein NOB1;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q9FLL1};
GN Name=Nob1;
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; TISSUE=Embryonic stem cell, and Testis;
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 TISSUE=Colon, and Embryo;
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).
RN [3]
RP STRUCTURE BY NMR OF 251-316 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-035, a Zn-ribbon module in mouse cDNA.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: May play a role in mRNA degradation (By similarity).
CC Endonuclease required for processing of 20S pre-rRNA precursor and
CC biogenesis of 40S ribosomal subunits (By similarity).
CC {ECO:0000250|UniProtKB:Q9FLL1, ECO:0000250|UniProtKB:Q9ULX3}.
CC -!- SUBUNIT: May interact with UPF2 (Probable). Component of the small
CC ribosomal subunit, ribosomal RNA processing complex (SSU RRP complex)
CC (By similarity). {ECO:0000250|UniProtKB:Q9FLL1, ECO:0000305|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULX3}.
CC -!- SIMILARITY: Belongs to the NOB1 family. {ECO:0000305}.
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DR EMBL; AK075755; BAC35933.1; -; mRNA.
DR EMBL; AK021194; BAB32325.1; -; mRNA.
DR EMBL; BC054835; AAH54835.1; -; mRNA.
DR EMBL; BC103793; AAI03794.1; -; mRNA.
DR CCDS; CCDS22649.1; -.
DR RefSeq; NP_080553.1; NM_026277.3.
DR PDB; 2CON; NMR; -; A=251-316.
DR PDBsum; 2CON; -.
DR AlphaFoldDB; Q8BW10; -.
DR SMR; Q8BW10; -.
DR BioGRID; 212314; 4.
DR IntAct; Q8BW10; 2.
DR STRING; 10090.ENSMUSP00000003946; -.
DR iPTMnet; Q8BW10; -.
DR PhosphoSitePlus; Q8BW10; -.
DR EPD; Q8BW10; -.
DR MaxQB; Q8BW10; -.
DR PaxDb; Q8BW10; -.
DR PRIDE; Q8BW10; -.
DR ProteomicsDB; 252838; -.
DR Antibodypedia; 29888; 264 antibodies from 24 providers.
DR DNASU; 67619; -.
DR Ensembl; ENSMUST00000003946; ENSMUSP00000003946; ENSMUSG00000003848.
DR GeneID; 67619; -.
DR KEGG; mmu:67619; -.
DR UCSC; uc009nhr.1; mouse.
DR CTD; 28987; -.
DR MGI; MGI:1914869; Nob1.
DR VEuPathDB; HostDB:ENSMUSG00000003848; -.
DR eggNOG; KOG2463; Eukaryota.
DR GeneTree; ENSGT00390000015857; -.
DR HOGENOM; CLU_024666_0_0_1; -.
DR InParanoid; Q8BW10; -.
DR OMA; GYELECE; -.
DR OrthoDB; 765237at2759; -.
DR PhylomeDB; Q8BW10; -.
DR TreeFam; TF105838; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 67619; 25 hits in 77 CRISPR screens.
DR ChiTaRS; Nob1; mouse.
DR EvolutionaryTrace; Q8BW10; -.
DR PRO; PR:Q8BW10; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BW10; protein.
DR Bgee; ENSMUSG00000003848; Expressed in manus and 234 other tissues.
DR ExpressionAtlas; Q8BW10; baseline and differential.
DR Genevisible; Q8BW10; MM.
DR GO; GO:0005737; C:cytoplasm; ISA:MGI.
DR GO; GO:0005730; C:nucleolus; ISA:MGI.
DR GO; GO:0005634; C:nucleus; ISA:MGI.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IEA:InterPro.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISA:MGI.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISA:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd09876; PIN_Nob1-like; 1.
DR Gene3D; 6.20.210.10; -; 1.
DR InterPro; IPR039907; NOB1.
DR InterPro; IPR017117; Nob1_euk.
DR InterPro; IPR036283; NOB1_Zf-like_sf.
DR InterPro; IPR014881; NOB1_Zn-bd.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR033411; Ribonuclease_PIN.
DR InterPro; IPR033461; WRNPLPNID.
DR PANTHER; PTHR12814; PTHR12814; 1.
DR Pfam; PF08772; NOB1_Zn_bind; 1.
DR Pfam; PF17146; PIN_6; 1.
DR Pfam; PF15017; WRNPLPNID; 1.
DR PIRSF; PIRSF037125; D-site_20S_pre-rRNA_nuclease; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF144206; SSF144206; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..403
FT /note="RNA-binding protein NOB1"
FT /id="PRO_0000233267"
FT DOMAIN 5..108
FT /note="PINc"
FT /evidence="ECO:0000255"
FT ZN_FING 251..323
FT /note="NOB1"
FT /evidence="ECO:0000255"
FT REGION 180..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2CON"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2CON"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2CON"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2CON"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:2CON"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2CON"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:2CON"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2CON"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:2CON"
SQ SEQUENCE 403 AA; 45464 MW; 923A88BF2B2275FF CRC64;
MAPVEHVVAD AGAFLRDAPL QDIGKNIYTI REVVREIRDK ATRRRLAVLP YQLRFKEPLP
EYVRLVTEFS KKTGDYPSLS ATDIQVLALT YQLEAEFVGV SHLKKEPEKA KVSSSIQHPE
TALHISGFHL PSKSKPLQEA VDRGHAADGP ENLEFSSFMF WRTPLPNIDR ELQELLIDGR
EEEEEEEECE DSDDDGGGWI TPSNIKQIQQ ELEQCDTPED VQVGCVTTDF AMQNVLLQMG
LHVLAVNGML VREARSYILR CHGCFKTTSD MNRVFCGHCG NKTLKKVSVT INDDGTLHMH
FSRNPKVLNP RGLRYSLPTP KGGKYAINPH LTEDQRFPQL RLSQKARQKT DVFAPDYIAG
VSPFAENDIS SRSAILQVRD GMLGAGRRRL NPNASRKKFV KKR
