NSG2_RAT
ID NSG2_RAT Reviewed; 171 AA.
AC Q3KR51;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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};
GN Name=Nsg2 {ECO:0000312|RGD:1563944};
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 -!- 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. Cell projection, dendrite
CC {ECO:0000269|PubMed:28874679}. Endosome membrane
CC {ECO:0000269|PubMed:28874679}. Early endosome membrane
CC {ECO:0000269|PubMed:28874679}. Late endosome membrane
CC {ECO:0000269|PubMed:28874679}. Lysosome lumen
CC {ECO:0000269|PubMed:28874679}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P47759}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P47759}. Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:P47759}. Note=Endocytosed from the cell surface,
CC thus entered into early endosomes, trafficks to late endosomes and
CC degradates in lysosomes (PubMed:28874679). Mainly Golgi stack, but also
CC found in small vacuolar organelles and multivesicular bodies. Found in
CC both stationary and motile endosomes (By similarity).
CC {ECO:0000250|UniProtKB:P47759, ECO:0000269|PubMed:28874679}.
CC -!- SIMILARITY: Belongs to the NSG family. {ECO:0000305}.
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DR EMBL; AABR07029218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473948; EDM04026.1; -; Genomic_DNA.
DR EMBL; CH473948; EDM04027.1; -; Genomic_DNA.
DR EMBL; CH473948; EDM04028.1; -; Genomic_DNA.
DR EMBL; CH473948; EDM04029.1; -; Genomic_DNA.
DR EMBL; BC105916; AAI05917.1; -; mRNA.
DR RefSeq; NP_001029324.1; NM_001034152.1.
DR AlphaFoldDB; Q3KR51; -.
DR SMR; Q3KR51; -.
DR STRING; 10116.ENSRNOP00000028069; -.
DR iPTMnet; Q3KR51; -.
DR PhosphoSitePlus; Q3KR51; -.
DR PaxDb; Q3KR51; -.
DR Ensembl; ENSRNOT00000028069; ENSRNOP00000028069; ENSRNOG00000020644.
DR GeneID; 497878; -.
DR KEGG; rno:497878; -.
DR UCSC; RGD:1563944; rat.
DR CTD; 51617; -.
DR RGD; 1563944; Nsg2.
DR eggNOG; ENOG502QRFC; Eukaryota.
DR GeneTree; ENSGT00390000000483; -.
DR HOGENOM; CLU_112085_1_0_1; -.
DR InParanoid; Q3KR51; -.
DR OMA; QHDAKPP; -.
DR OrthoDB; 1315835at2759; -.
DR PhylomeDB; Q3KR51; -.
DR TreeFam; TF332232; -.
DR PRO; PR:Q3KR51; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000020644; Expressed in frontal cortex and 19 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:1990674; C:Golgi cis cisterna membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; IDA:UniProtKB.
DR GO; GO:0032585; C:multivesicular body membrane; ISS: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: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_0000442707"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28874679"
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:0000269|PubMed:28874679"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 171 AA; 18986 MW; D9E50283840E3891 CRC64;
MVKLNGNPGE KGAKPPSVED GFQTVPLITP LEVNHLQLSA PEKVIVKTRT EYQPEQRNKG
KFRVPKIAEF TVTILVSLAL AFLACIVFLV VYKAFTYDHS CPEGFVYKHK RCIPASLDAY
YSSQDPSSRS RFYTVISHYS VAKQSTARAI GPWLSAAAVI HEPKPPKTQG H