ID NGDN_MOUSE Reviewed; 315 AA.
AC Q9DB96; Q8CIJ2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Neuroguidin;
DE AltName: Full=EIF4E-binding protein;
GN Name=Ngdn; Synonyms=Ngd;
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=Cerebellum;
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 gland, and 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).
RN [3]
RP FUNCTION, INTERACTION WITH CPEB1 AND EIF4E, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=16705177; DOI=10.1128/mcb.02470-05;
RA Jung M.-Y., Lorenz L., Richter J.D.;
RT "Translational control by neuroguidin, a eukaryotic initiation factor 4E
RT and CPEB binding protein.";
RL Mol. Cell. Biol. 26:4277-4287(2006).
CC -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor
CC of the small eukaryotic ribosomal subunit. During the assembly of the
CC SSU processome in the nucleolus, many ribosome biogenesis factors, an
CC RNA chaperone and ribosomal proteins associate with the nascent pre-
CC rRNA and work in concert to generate RNA folding, modifications,
CC rearrangements and cleavage as well as targeted degradation of pre-
CC ribosomal RNA by the RNA exosome. Its dissociation from the complex
CC determines the transition from state pre-A1 to state pre-A1* (By
CC similarity). Inhibits mRNA translation in a cytoplasmic polyadenylation
CC element (CPE)-dependent manner (PubMed:16705177).
CC {ECO:0000250|UniProtKB:Q8NEJ9, ECO:0000269|PubMed:16705177}.
CC -!- SUBUNIT: Interacts with CPEB1 and EIF4E. {ECO:0000269|PubMed:16705177}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16705177}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q8NEJ9}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q8NEJ9}. Cytoplasm
CC {ECO:0000269|PubMed:16705177}. Cell projection, axon
CC {ECO:0000269|PubMed:16705177}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16705177}. Cell projection, filopodium
CC {ECO:0000269|PubMed:16705177}. Note=Translocated from nucleolus to
CC nuclear foci in response to UV damage (By similarity). Detected in
CC axons, dendrites and filopodia. Colocalized with EIF4E in neurites.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, ovary, spleen, kidney,
CC hippocampus and cerebellum (at protein level). Expressed in testis,
CC ovary, spleen, kidney, brain. {ECO:0000269|PubMed:16705177}.
CC -!- SIMILARITY: Belongs to the SAS10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23770.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK005098; BAB23816.1; -; mRNA.
DR EMBL; BC023770; AAH23770.1; ALT_INIT; mRNA.
DR EMBL; BC052790; AAH52790.1; -; mRNA.
DR CCDS; CCDS36928.1; -.
DR RefSeq; NP_081166.1; NM_026890.2.
DR AlphaFoldDB; Q9DB96; -.
DR SMR; Q9DB96; -.
DR BioGRID; 213145; 2.
DR STRING; 10090.ENSMUSP00000022815; -.
DR iPTMnet; Q9DB96; -.
DR PhosphoSitePlus; Q9DB96; -.
DR EPD; Q9DB96; -.
DR MaxQB; Q9DB96; -.
DR PaxDb; 10090-ENSMUSP00000022815; -.
DR PeptideAtlas; Q9DB96; -.
DR ProteomicsDB; 252960; -.
DR Pumba; Q9DB96; -.
DR Antibodypedia; 89; 193 antibodies from 26 providers.
DR Ensembl; ENSMUST00000022815.10; ENSMUSP00000022815.9; ENSMUSG00000022204.10.
DR GeneID; 68966; -.
DR KEGG; mmu:68966; -.
DR UCSC; uc007txx.2; mouse.
DR AGR; MGI:1916216; -.
DR CTD; 25983; -.
DR MGI; MGI:1916216; Ngdn.
DR VEuPathDB; HostDB:ENSMUSG00000022204; -.
DR eggNOG; KOG3117; Eukaryota.
DR GeneTree; ENSGT00500000044922; -.
DR HOGENOM; CLU_031901_0_0_1; -.
DR InParanoid; Q9DB96; -.
DR OMA; MALDYDC; -.
DR OrthoDB; 102916at2759; -.
DR PhylomeDB; Q9DB96; -.
DR TreeFam; TF313713; -.
DR BioGRID-ORCS; 68966; 26 hits in 80 CRISPR screens.
DR ChiTaRS; Ngdn; mouse.
DR PRO; PR:Q9DB96; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9DB96; Protein.
DR Bgee; ENSMUSG00000022204; Expressed in paneth cell and 263 other cell types or tissues.
DR Genevisible; Q9DB96; MM.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0140240; C:perforant pathway to dendrate granule cell synapse; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0140245; P:regulation of translation at postsynapse; ISO:MGI.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB.
DR InterPro; IPR007146; Sas10/Utp3/C1D.
DR PANTHER; PTHR13237:SF9; NEUROGUIDIN; 1.
DR PANTHER; PTHR13237; SOMETHING ABOUT SILENCING PROTEIN 10-RELATED; 1.
DR Pfam; PF04000; Sas10_Utp3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Centromere; Chromosome; Coiled coil;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT CHAIN 2..315
FT /note="Neuroguidin"
FT /id="PRO_0000114332"
FT REGION 41..174
FT /note="Necessary for interaction with EIF4E"
FT /evidence="ECO:0000269|PubMed:16705177"
FT REGION 123..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..41
FT /evidence="ECO:0000255"
FT COILED 181..203
FT /evidence="ECO:0000255"
FT COMPBIAS 298..315
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEJ9"
FT CONFLICT 154
FT /note="G -> D (in Ref. 2; AAH23770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 35659 MW; A5C59A3949A0F40C CRC64;
MAAPEVLESD VSSSITLLKN LQEQVMAVTA QIQALTTKVR AGTYSTEKGL SFLEVKDQLL
LMYLMDLSHL ILDKASGASL QGHPAVLRLV EIRTVLEKLR PLDQKLKYQI DKLVKTAVTG
SLSENDPLRF KPHPSNMVSK LSSEDEEESE AEEGQSEASG KKSAKGSAKK YVPPRLVPVH
YDETEAEREQ KRLEKAKRRA LSSSVIRELK EQYSDAPEEI RDARHPHVTR QSQEDQHRVN
YEESMMVRLS VSKREKGLRR RASAMSSQLH SLTHFSDISA LTGGTAHLDE DQNPVKKRKK
LPKKGRKKKG FRRRW
//
