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NSG2_MOUSE
ID   NSG2_MOUSE              Reviewed;         171 AA.
AC   P47759;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Neuronal vesicle trafficking-associated protein 2 {ECO:0000250|UniProtKB:Q9Y328};
DE   AltName: Full=Neuron-specific protein family member 2 {ECO:0000250|UniProtKB:Q9Y328};
DE   AltName: Full=Protein 8.5;
DE   AltName: Full=Protein p19;
GN   Name=Nsg2 {ECO:0000312|MGI:MGI:1202070};
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 [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=7829526; DOI=10.1074/jbc.270.4.1888;
RA   Saberan-Djoneidi D., Marey-Semper I., Picart R., Studler J.-M., Tougard C.,
RA   Glowinski J., Levi-Strauss M.;
RT   "A 19-kDa protein belonging to a new family is expressed in the Golgi
RT   apparatus of neural cells.";
RL   J. Biol. Chem. 270:1888-1893(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [4]
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   [5]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
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   [6]
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q3KR51}; Single-
CC       pass type II membrane protein {ECO:0000250|UniProtKB:Q3KR51}. Golgi
CC       apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q3KR51}.
CC       Cell projection, dendrite {ECO:0000250|UniProtKB:Q3KR51}. Endosome
CC       membrane {ECO:0000250|UniProtKB:Q3KR51}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q3KR51}. Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q3KR51}. Lysosome lumen
CC       {ECO:0000250|UniProtKB:Q3KR51}. Cytoplasmic vesicle membrane
CC       {ECO:0000269|PubMed:7829526}. Golgi apparatus, Golgi stack membrane
CC       {ECO:0000269|PubMed:7829526}. Endosome, multivesicular body membrane
CC       {ECO:0000269|PubMed:7829526}. Note=Endocytosed from the cell surface,
CC       thus entered into early endosomes, trafficks to late endosomes and
CC       degradates in lysosomes (By similarity). Mainly Golgi stack, but also
CC       found in small vacuolar organelles and multivesicular bodies
CC       (PubMed:7829526). Found in both stationary and motile endosomes
CC       (PubMed:28874679). {ECO:0000250|UniProtKB:Q3KR51,
CC       ECO:0000269|PubMed:28874679, ECO:0000269|PubMed:7829526}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in neural and neuroendocrine
CC       tissues. Pituitary and less in adrenal gland and testis. Expressed in
CC       the hippocampus throughout development. Remains enriched in layer V
CC       cortical neurons during development. At P0, broadly expressed in the
CC       neocortex. Is down-regulated overall at P8 and P14, but remains
CC       relatively enriched in layer V. At P0 is lower expressed in the
CC       cerebellum. Expression remains low throughout development, and is
CC       undetectable by adulthood (PubMed:28299779).
CC       {ECO:0000269|PubMed:28299779}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed at 20 dpc. At 17.5 dpc, highly
CC       expressed in the cortical plate and basal subventricular zone.
CC       {ECO:0000269|PubMed:28299779}.
CC   -!- SIMILARITY: Belongs to the NSG family. {ECO:0000305}.
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DR   EMBL; U17259; AAA67764.1; -; mRNA.
DR   EMBL; AK011563; BAB27700.1; -; mRNA.
DR   EMBL; AK075612; BAC35857.1; -; mRNA.
DR   EMBL; BC018224; AAH18224.1; -; mRNA.
DR   CCDS; CCDS24516.1; -.
DR   PIR; A55629; A55629.
DR   RefSeq; NP_001277609.1; NM_001290680.1.
DR   RefSeq; NP_001277610.1; NM_001290681.1.
DR   RefSeq; NP_032767.1; NM_008741.4.
DR   AlphaFoldDB; P47759; -.
DR   SMR; P47759; -.
DR   STRING; 10090.ENSMUSP00000020537; -.
DR   iPTMnet; P47759; -.
DR   PhosphoSitePlus; P47759; -.
DR   PaxDb; P47759; -.
DR   PeptideAtlas; P47759; -.
DR   PRIDE; P47759; -.
DR   ProteomicsDB; 293751; -.
DR   Antibodypedia; 45952; 80 antibodies from 20 providers.
DR   DNASU; 18197; -.
DR   Ensembl; ENSMUST00000020537; ENSMUSP00000020537; ENSMUSG00000020297.
DR   GeneID; 18197; -.
DR   KEGG; mmu:18197; -.
DR   UCSC; uc007iiw.2; mouse.
DR   CTD; 51617; -.
DR   MGI; MGI:1202070; Nsg2.
DR   VEuPathDB; HostDB:ENSMUSG00000020297; -.
DR   eggNOG; ENOG502QRFC; Eukaryota.
DR   GeneTree; ENSGT00390000000483; -.
DR   HOGENOM; CLU_112085_1_0_1; -.
DR   InParanoid; P47759; -.
DR   OMA; QHDAKPP; -.
DR   OrthoDB; 1315835at2759; -.
DR   PhylomeDB; P47759; -.
DR   TreeFam; TF332232; -.
DR   BioGRID-ORCS; 18197; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Nsg2; mouse.
DR   PRO; PR:P47759; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P47759; protein.
DR   Bgee; ENSMUSG00000020297; Expressed in cortical plate and 176 other tissues.
DR   ExpressionAtlas; P47759; baseline and differential.
DR   Genevisible; P47759; MM.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:1990674; C:Golgi cis cisterna membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0043202; C:lysosomal lumen; ISO:MGI.
DR   GO; GO:0032585; C:multivesicular body membrane; IDA: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: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; IBA:GO_Central.
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; Endosome; Golgi apparatus; Lysosome;
KW   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..171
FT                   /note="Neuronal vesicle trafficking-associated protein 2"
FT                   /id="PRO_0000164367"
FT   TOPO_DOM        1..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..171
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   171 AA;  19000 MW;  7A601049DBFD6869 CRC64;
     MVKLNSNPGE KGAKPPSVED GFQTVPLITP LEVNHLQLAA PEKVIVKTRT EYQPEQRNKG
     KFRVPKIAEF TVTILVSLAL AFLACIVFLV VYKAFTYDHS CPEGFVYKHK RCIPASLDAY
     YSSQDPSSRS RFYTVISHYS VAKQSTARAI GPWLSAAAVI HEPKPPKTQG H
 
 
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