NSG1_MOUSE
ID NSG1_MOUSE Reviewed; 185 AA.
AC Q62092; O54717; Q3UF63; Q922E5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Neuronal vesicle trafficking-associated protein 1 {ECO:0000250|UniProtKB:P42857};
DE AltName: Full=M234;
DE AltName: Full=Neuron-enriched endosomal protein of 21 kDa {ECO:0000303|PubMed:15187090};
DE AltName: Full=Neuron-specific protein family member 1 {ECO:0000250|UniProtKB:P42857};
DE AltName: Full=p21 {ECO:0000303|PubMed:9461575};
GN Name=Nsg1 {ECO:0000312|MGI:MGI:109149};
GN Synonyms=NEEP21 {ECO:0000303|PubMed:15187090};
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 [GENOMIC DNA].
RX PubMed=9013775; DOI=10.1016/s0169-328x(96)00115-5;
RA Carlock L., Vo T., Lorincz M., Walker P.D., Bessert D., Wisniewski D.,
RA Dunbar J.C.;
RT "Variable subcellular localization of a neuron-specific protein during
RT NTera 2 differentiation into post-mitotic human neurons.";
RL Brain Res. Mol. Brain Res. 42:202-212(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9461575; DOI=10.1074/jbc.273.7.3909;
RA Saberan-Djoneidi D., Picart R., Escalier D., Gelman M., Barret A.,
RA Tougard C., Glowinski J., Levi-Strauss M.;
RT "A 21-kDa polypeptide belonging to a new family of proteins is expressed in
RT the Golgi apparatus of neural and germ cells.";
RL J. Biol. Chem. 273:3909-3914(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Head, and Sympathetic ganglion;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP INTERACTION WITH STX12, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12070131; DOI=10.1083/jcb.200202022;
RA Steiner P., Sarria J.C., Glauser L., Magnin S., Catsicas S., Hirling H.;
RT "Modulation of receptor cycling by neuron-enriched endosomal protein of 21
RT kD.";
RL J. Cell Biol. 157:1197-1209(2002).
RN [6]
RP FUNCTION.
RX PubMed=15187090; DOI=10.1074/jbc.m402751200;
RA Debaigt C., Hirling H., Steiner P., Vincent J.P., Mazella J.;
RT "Crucial role of neuron-enriched endosomal protein of 21 kDa in sorting
RT between degradation and recycling of internalized G-protein-coupled
RT receptors.";
RL J. Biol. Chem. 279:35687-35691(2004).
RN [7]
RP FUNCTION.
RX PubMed=16037816; DOI=10.1038/sj.emboj.7600755;
RA Steiner P., Alberi S., Kulangara K., Yersin A., Sarria J.C., Regulier E.,
RA Kasas S., Dietler G., Muller D., Catsicas S., Hirling H.;
RT "Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and
RT recycling of the glutamate receptor subunit GluR2.";
RL EMBO J. 24:2873-2884(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [9]
RP INTERACTION WITH APP, AND FUNCTION.
RX PubMed=21084623; DOI=10.1523/jneurosci.4464-10.2010;
RA Norstrom E.M., Zhang C., Tanzi R., Sisodia S.S.;
RT "Identification of NEEP21 as a ss-amyloid precursor protein-interacting
RT protein in vivo that modulates amyloidogenic processing in vitro.";
RL J. Neurosci. 30:15677-15685(2010).
RN [10]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=28299779; DOI=10.1002/cne.24168;
RA Barford K., Yap C.C., Dwyer N.D., Winckler B.;
RT "The related neuronal endosomal proteins NEEP21 (Nsg1) and P19 (Nsg2) have
RT divergent expression profiles in vivo.";
RL J. Comp. Neurol. 525:1861-1878(2017).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=28874679; DOI=10.1038/s41598-017-07667-x;
RA Yap C.C., Digilio L., McMahon L., Winckler B.;
RT "The endosomal neuronal proteins Nsg1/NEEP21 and Nsg2/P19 are itinerant,
RT not resident proteins of dendritic endosomes.";
RL Sci. Rep. 7:10481-10481(2017).
CC -!- FUNCTION: Plays a role in the recycling mechanism in neurons of
CC multiple receptors, including AMPAR, APP and L1CAM and acts at the
CC level of early endosomes to promote sorting of receptors toward a
CC recycling pathway (PubMed:15187090, PubMed:12070131, PubMed:21084623,
CC PubMed:16037816). Regulates sorting and recycling of GRIA2 through
CC interaction with GRIP1 and then contributes to the regulation of
CC synaptic transmission and plasticity by affecting the recycling and
CC targeting of AMPA receptors to the synapse (PubMed:16037816). Is
CC required for faithful sorting of L1CAM to axons by facilitating
CC trafficking from somatodendritic early endosome or the recycling
CC endosome (By similarity). In an other hand, induces apoptosis via the
CC activation of CASP3 in response to DNA damage (By similarity).
CC {ECO:0000250|UniProtKB:P02683, ECO:0000250|UniProtKB:P42857,
CC ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:15187090,
CC ECO:0000269|PubMed:16037816, ECO:0000269|PubMed:21084623}.
CC -!- SUBUNIT: Forms a complex with GRIP1, GRIA2 and STX12 through direct
CC interaction with GRIP1; controls the intracellular fate of AMPAR and
CC the endosomal sorting of the GRIA2 subunit toward recycling and
CC membrane targeting. Interacts with STX12 (PubMed:12070131). Interacts
CC with APP; could regulate APP processing (PubMed:21084623). Interacts
CC with FAM171A1 (By similarity). {ECO:0000250|UniProtKB:P42857,
CC ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:21084623}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02683}; Single-
CC pass type II membrane protein {ECO:0000250|UniProtKB:P02683}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P02683}.
CC Endosome membrane {ECO:0000250|UniProtKB:P02683}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:P02683}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P02683}. Late endosome membrane
CC {ECO:0000269|PubMed:28874679}. Lysosome lumen
CC {ECO:0000250|UniProtKB:P02683}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P02683}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P02683}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P02683}. Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:P02683}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P42857}. Note=Endocytosed from the cell surface,
CC thus enters into early endosomes, trafficks to late endosomes and
CC degradates in lysosomes (By similarity). Endoplasmic reticulum
CC targeting is essential for apoptosis (By similarity). Found in both
CC stationary and motile endosomes (PubMed:28874679). A previous study
CC supports a type I membrane protein topology (PubMed:12070131).
CC {ECO:0000250|UniProtKB:P02683, ECO:0000250|UniProtKB:P42857,
CC ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:28874679}.
CC -!- TISSUE SPECIFICITY: Pituitary and less in adrenal gland and testis.
CC Expressed in the hippocampus throughout development. At P0, highly and
CC broadly expressed throughout the cortical plate, but is down-regulated
CC overall at P8 and P14, but remains relatively enriched in layer V. At
CC P0 is expressed ubiquitously in the developing cerebellum namely
CC Purkinje neurons as well as granule neurons. However, it becomes
CC restricted to Purkinje cells by P8. This exclusive expression in
CC Purkinje cells is maintained throughout adulthood.
CC {ECO:0000269|PubMed:28299779}.
CC -!- DEVELOPMENTAL STAGE: At 17.5 dpc, highly expressed in the cortical
CC plate and in the subplate (SP). {ECO:0000269|PubMed:28299779}.
CC -!- SIMILARITY: Belongs to the NSG family. {ECO:0000305}.
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DR EMBL; M98530; AAA39966.1; -; Genomic_DNA.
DR EMBL; AF035683; AAB88210.1; -; mRNA.
DR EMBL; AK076451; BAC36347.1; -; mRNA.
DR EMBL; AK144503; BAE25919.1; -; mRNA.
DR EMBL; AK148941; BAE28698.1; -; mRNA.
DR EMBL; BC008272; AAH08272.1; -; mRNA.
DR CCDS; CCDS19251.1; -.
DR RefSeq; NP_035072.2; NM_010942.3.
DR RefSeq; XP_006503836.1; XM_006503773.1.
DR AlphaFoldDB; Q62092; -.
DR SMR; Q62092; -.
DR STRING; 10090.ENSMUSP00000031009; -.
DR iPTMnet; Q62092; -.
DR PhosphoSitePlus; Q62092; -.
DR MaxQB; Q62092; -.
DR PaxDb; Q62092; -.
DR PeptideAtlas; Q62092; -.
DR PRIDE; Q62092; -.
DR ProteomicsDB; 293984; -.
DR Antibodypedia; 22570; 229 antibodies from 30 providers.
DR DNASU; 18196; -.
DR Ensembl; ENSMUST00000031009; ENSMUSP00000031009; ENSMUSG00000029126.
DR Ensembl; ENSMUST00000201363; ENSMUSP00000144396; ENSMUSG00000029126.
DR GeneID; 18196; -.
DR KEGG; mmu:18196; -.
DR UCSC; uc008xga.1; mouse.
DR CTD; 27065; -.
DR MGI; MGI:109149; Nsg1.
DR VEuPathDB; HostDB:ENSMUSG00000029126; -.
DR eggNOG; ENOG502QSAI; Eukaryota.
DR GeneTree; ENSGT00390000000483; -.
DR HOGENOM; CLU_112085_1_0_1; -.
DR InParanoid; Q62092; -.
DR OMA; MQGRCMP; -.
DR OrthoDB; 1315835at2759; -.
DR PhylomeDB; Q62092; -.
DR TreeFam; TF332232; -.
DR BioGRID-ORCS; 18196; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Nsg1; mouse.
DR PRO; PR:Q62092; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q62092; protein.
DR Bgee; ENSMUSG00000029126; Expressed in cortical plate and 229 other tissues.
DR ExpressionAtlas; Q62092; baseline and differential.
DR Genevisible; Q62092; MM.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0043202; C:lysosomal lumen; ISO:MGI.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098845; C:postsynaptic endosome; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:0099627; P:neurotransmitter receptor cycle; IDA:UniProtKB.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
DR GO; GO:0099630; P:postsynaptic neurotransmitter receptor cycle; ISS:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; IMP:UniProtKB.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0098814; P:spontaneous synaptic transmission; ISS:UniProtKB.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR InterPro; IPR009431; NSG.
DR PANTHER; PTHR28546; PTHR28546; 1.
DR Pfam; PF06387; Calcyon; 1.
DR PIRSF; PIRSF002383; Calcyon; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasmic vesicle; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Lysosome; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..185
FT /note="Neuronal vesicle trafficking-associated protein 1"
FT /id="PRO_0000164364"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02683"
FT TRANSMEM 83..103
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..185
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P02683"
FT REGION 129..164
FT /note="Required for GRIP1 interaction"
FT /evidence="ECO:0000250|UniProtKB:P02683"
FT CONFLICT 112
FT /note="C -> Y (in Ref. 1; AAA39966)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="A -> D (in Ref. 1; AAA39966)"
FT /evidence="ECO:0000305"
FT CONFLICT 151..152
FT /note="NV -> KL (in Ref. 1; AAA39966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 20929 MW; B184238A71710C1F CRC64;
MVKLGNNFAE KGTKQPLLED GFDTIPLMTP LDVNQLQFPP PDKVVVKTKT EYEPDRKKGK
ARPPKIAEFT VSITEGVTER FKVSVLVLFA LAFLTCVVFL VVYKVYKYDR ACPDGFVLKN
TQCIPEGLES YYTEQDSSAR EKFYTVINHY NVAKQSITRS VSPWMSVLSE EKLSEQETEA
AEKSA
