NSG1_RAT
ID NSG1_RAT Reviewed; 185 AA.
AC P02683; P02684; Q6P9Y0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Neuronal vesicle trafficking-associated protein 1 {ECO:0000250|UniProtKB:P42857};
DE AltName: Full=Brain neuron cytoplasmic protein 1/2;
DE AltName: Full=Neuron-enriched endosomal protein of 21 kDa {ECO:0000250|UniProtKB:P42857};
DE AltName: Full=Neuron-specific protein family member 1 {ECO:0000250|UniProtKB:P42857};
GN Name=Nsg1 {ECO:0000312|RGD:2222}; Synonyms=Bsmrb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-185, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=6347394; DOI=10.1016/0092-8674(83)90010-7;
RA Sutcliffe J.G., Milner R.J., Shinnick T.M., Bloom F.E.;
RT "Identifying the protein products of brain-specific genes with antibodies
RT to chemically synthesized peptides.";
RL Cell 33:671-682(1983).
RN [3]
RP TISSUE SPECIFICITY.
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 [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [5]
RP INTERACTION WITH STX12, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 INTERACTION WITH GRIP1, COMPLEX FORMATION WITH GRIP1; GRIA2 AND STX12, AND
RP REGION.
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 [7]
RP FUNCTION.
RX PubMed=15911354; DOI=10.1016/j.mcn.2005.03.011;
RA Alberi S., Boda B., Steiner P., Nikonenko I., Hirling H., Muller D.;
RT "The endosomal protein NEEP21 regulates AMPA receptor-mediated synaptic
RT transmission and plasticity in the hippocampus.";
RL Mol. Cell. Neurosci. 29:313-319(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18299352; DOI=10.1083/jcb.200707143;
RA Yap C.C., Wisco D., Kujala P., Lasiecka Z.M., Cannon J.T., Chang M.C.,
RA Hirling H., Klumperman J., Winckler B.;
RT "The somatodendritic endosomal regulator NEEP21 facilitates axonal
RT targeting of L1/NgCAM.";
RL J. Cell Biol. 180:827-842(2008).
RN [9]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
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:18299352, PubMed:15911354). Regulates sorting
CC and recycling of GRIA2 through interaction with GRIP1 and then
CC contributes to the regulation of synaptic transmission and plasticity
CC by affecting the recycling and targeting of AMPA receptors to the
CC synapse (PubMed:15911354). Is required for faithful sorting of L1CAM to
CC axons by facilitating trafficking from somatodendritic early endosome
CC or the recycling endosome (PubMed:18299352). In an other hand, induces
CC apoptosis via the activation of CASP3 in response to DNA damage (By
CC similarity). {ECO:0000250|UniProtKB:P42857,
CC ECO:0000269|PubMed:15911354, ECO:0000269|PubMed:18299352}.
CC -!- SUBUNIT: Forms a complex with GRIP1, GRIA2 and STX12; controls the
CC intracellular fate of AMPAR and the endosomal sorting of the GRIA2
CC subunit toward recycling and membrane targeting. Interacts with GRIP1
CC (PubMed:16037816). Interacts with STX12 (PubMed:12070131). Interacts
CC with APP; could regulate APP processing (By similarity). Interacts with
CC FAM171A1 (By similarity). {ECO:0000250|UniProtKB:P42857,
CC ECO:0000250|UniProtKB:Q62092, ECO:0000269|PubMed:12070131,
CC ECO:0000269|PubMed:16037816}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:28874679}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:28874679}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:28874679}.
CC Endosome membrane {ECO:0000269|PubMed:18299352,
CC ECO:0000269|PubMed:28874679}. Cell projection, dendrite
CC {ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:28874679}. Early
CC endosome membrane {ECO:0000269|PubMed:12070131,
CC ECO:0000269|PubMed:28874679}. Late endosome membrane
CC {ECO:0000269|PubMed:28874679}. Lysosome lumen
CC {ECO:0000269|PubMed:28874679}. Recycling endosome membrane
CC {ECO:0000269|PubMed:12070131}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:9461575}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:9461575}. Endosome, multivesicular body membrane
CC {ECO:0000269|PubMed:9461575}. 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 (PubMed:28874679). Endoplasmic reticulum
CC targeting is essential for apoptosis (By similarity). Found in both
CC stationary and motile endosomes. A previous study supports a type I
CC membrane protein topology (By similarity).
CC {ECO:0000250|UniProtKB:P42857, ECO:0000250|UniProtKB:Q62092,
CC ECO:0000269|PubMed:28874679}.
CC -!- TISSUE SPECIFICITY: Widely expressed in brain and spinal cord
CC (PubMed:6347394, PubMed:9013775, PubMed:9461575). Expressed in neurons
CC during maturation and synapse formation (PubMed:12070131).
CC {ECO:0000269|PubMed:12070131, ECO:0000269|PubMed:6347394,
CC ECO:0000269|PubMed:9013775, ECO:0000269|PubMed:9461575}.
CC -!- SIMILARITY: Belongs to the NSG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24785.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; BC060538; AAH60538.1; -; mRNA.
DR EMBL; V01543; CAA24784.1; -; Genomic_DNA.
DR EMBL; V01543; CAA24785.1; ALT_SEQ; Genomic_DNA.
DR PIR; A03136; BNRT1.
DR PIR; A03137; BNRT2.
DR RefSeq; NP_077042.2; NM_024128.3.
DR AlphaFoldDB; P02683; -.
DR SMR; P02683; -.
DR BioGRID; 247287; 1.
DR CORUM; P02683; -.
DR STRING; 10116.ENSRNOP00000008030; -.
DR iPTMnet; P02683; -.
DR PhosphoSitePlus; P02683; -.
DR jPOST; P02683; -.
DR PaxDb; P02683; -.
DR PRIDE; P02683; -.
DR Ensembl; ENSRNOT00000118922; ENSRNOP00000097258; ENSRNOG00000005700.
DR GeneID; 25247; -.
DR KEGG; rno:25247; -.
DR CTD; 27065; -.
DR RGD; 2222; Nsg1.
DR eggNOG; ENOG502QSAI; Eukaryota.
DR GeneTree; ENSGT00390000000483; -.
DR HOGENOM; CLU_112085_1_0_1; -.
DR InParanoid; P02683; -.
DR OMA; MQGRCMP; -.
DR OrthoDB; 1315835at2759; -.
DR PhylomeDB; P02683; -.
DR TreeFam; TF332232; -.
DR PRO; PR:P02683; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000005700; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P02683; RN.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IDA: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:UniProtKB.
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; ISO:RGD.
DR GO; GO:0043202; C:lysosomal lumen; IDA:UniProtKB.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098845; C:postsynaptic endosome; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; ISS: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; IMP:RGD.
DR GO; GO:0099627; P:neurotransmitter receptor cycle; ISS:UniProtKB.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:RGD.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IMP:RGD.
DR GO; GO:0099630; P:postsynaptic neurotransmitter receptor cycle; IMP:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; ISS:UniProtKB.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0098814; P:spontaneous synaptic transmission; IMP:UniProtKB.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:RGD.
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_0000164365"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28874679"
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:0000269|PubMed:28874679"
FT REGION 129..164
FT /note="Required for GRIP1 interaction"
FT /evidence="ECO:0000269|PubMed:16037816"
SQ SEQUENCE 185 AA; 20943 MW; B1909CC191710C1F CRC64;
MVKLGNNFAE KGTKQPLLED GFDTIPLMTP LDVNQLQFPP PDKVVVKTKT EYEPDRKKGK
ARPPKIAEFT VSITEGVTER FKVSVLVLFA LAFLTCVVFL VVYKVYKYDR ACPDGFVLKN
TQCIPEGLES YYTEQDSSAR EKFYTVINHY NLAKQSITRS VSPWMSVLSE EKLSEQETEA
AEKSA
