RTN2_RAT
ID RTN2_RAT Reviewed; 469 AA.
AC Q6WN19; F1LM00;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Reticulon-2 {ECO:0000312|RGD:1303245};
DE AltName: Full=Neuroendocrine-specific protein-like 1 {ECO:0000250|UniProtKB:O70622};
DE Short=NSP-like protein 1 {ECO:0000250|UniProtKB:O70622};
DE AltName: Full=Neuroendocrine-specific protein-like I {ECO:0000305};
DE Short=NSP-like protein I {ECO:0000305};
DE Short=NSPLI {ECO:0000305};
GN Name=Rtn2 {ECO:0000312|RGD:1303245};
GN Synonyms=Nspl1 {ECO:0000250|UniProtKB:O70622};
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 {ECO:0000312|EMBL:AAQ18231.1};
RN [1] {ECO:0000312|EMBL:AAQ18231.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Vidensky S.O., Ruggiero A.M., Rothstein J.D.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
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 [3] {ECO:0000312|EMBL:AAI29080.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI29080.1};
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] {ECO:0000312|EMBL:DAA01961.2}
RP IDENTIFICATION.
RX PubMed=12832288; DOI=10.1096/fj.02-1166hyp;
RA Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.;
RT "A reticular rhapsody: phylogenic evolution and nomenclature of the
RT RTN/Nogo gene family.";
RL FASEB J. 17:1238-1247(2003).
RN [5] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ARL6IP5 AND SLC1A1, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=18096700; DOI=10.1074/jbc.m708096200;
RA Liu Y., Vidensky S., Ruggiero A.M., Maier S., Sitte H.H., Rothstein J.D.;
RT "Reticulon RTN2B regulates trafficking and function of neuronal glutamate
RT transporter EAAC1.";
RL J. Biol. Chem. 283:6561-6571(2008).
CC -!- FUNCTION: Inhibits amyloid precursor protein processing, probably by
CC blocking BACE1 activity (By similarity). Enhances trafficking of the
CC glutamate transporter SLC1A1/EAAC1 from the endoplasmic reticulum to
CC the cell surface (PubMed:18096700). Plays a role in the translocation
CC of SLC2A4/GLUT4 from intracellular membranes to the cell membrane which
CC facilitates the uptake of glucose into the cell (By similarity).
CC {ECO:0000250|UniProtKB:O70622, ECO:0000250|UniProtKB:O75298,
CC ECO:0000269|PubMed:18096700}.
CC -!- SUBUNIT: Interacts with SPAST (By similarity). Interacts with BACE1 (By
CC similarity). Interacts (via first transmembrane domain) with
CC ARL6IP5/GTRAP3-18 (PubMed:18096700). Interacts (via N-terminus) with
CC SLC1A1/EAAC1; the interaction promotes cell surface expression of
CC SLC1A1 (PubMed:18096700). {ECO:0000250|UniProtKB:O75298,
CC ECO:0000269|PubMed:18096700}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|RuleBase:RU210713, ECO:0000269|PubMed:18096700}; Multi-
CC pass membrane protein {ECO:0000255|RuleBase:RU210713}. Sarcoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane
CC protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:18096700};
CC Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:O70622}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O70622}. Note=Localizes to intermediate
CC filaments in mononucleated myoblasts and to Z lines in mature myotubes.
CC {ECO:0000250|UniProtKB:O70622}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and spinal cord (at protein
CC level) (PubMed:18096700). In the embryonic brain cortex, expressed in
CC neurons but not in astrocytes (at protein level) (PubMed:18096700).
CC {ECO:0000269|PubMed:18096700}.
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DR EMBL; AY279211; AAQ18231.1; -; mRNA.
DR EMBL; AABR07002674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC129079; AAI29080.1; -; mRNA.
DR EMBL; BK001788; DAA01961.2; -; mRNA.
DR RefSeq; NP_963856.1; NM_201562.3.
DR AlphaFoldDB; Q6WN19; -.
DR SMR; Q6WN19; -.
DR STRING; 10116.ENSRNOP00000022528; -.
DR PhosphoSitePlus; Q6WN19; -.
DR PaxDb; Q6WN19; -.
DR Ensembl; ENSRNOT00000022528; ENSRNOP00000022528; ENSRNOG00000016603.
DR GeneID; 308410; -.
DR KEGG; rno:308410; -.
DR UCSC; RGD:1303245; rat.
DR CTD; 6253; -.
DR RGD; 1303245; Rtn2.
DR eggNOG; KOG1792; Eukaryota.
DR GeneTree; ENSGT00940000160599; -.
DR HOGENOM; CLU_508939_0_0_1; -.
DR InParanoid; Q6WN19; -.
DR OMA; WRAIGWV; -.
DR OrthoDB; 1011511at2759; -.
DR PhylomeDB; Q6WN19; -.
DR TreeFam; TF105431; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016603; Expressed in skeletal muscle tissue and 19 other tissues.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR GO; GO:0014802; C:terminal cisterna; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IDA:MGI.
DR GO; GO:0046324; P:regulation of glucose import; ISS:UniProtKB.
DR InterPro; IPR003388; Reticulon.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..469
FT /note="Reticulon-2"
FT /id="PRO_0000452174"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 270..469
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70622"
SQ SEQUENCE 469 AA; 50967 MW; 6C91D2DF0F0689F0 CRC64;
MGQVLPVFAH CKEAPSTASS TPDSTEGGND DSDFRELHTA REFSEDEEEE TTSQDWGTPR
ELTFSYIAFD GVVGSGGRRD SVVRRPRPQG RSVSEPRDPP PQPSLGDSLE SIPSLSQSPE
PGRRGDPDTV PPAERPLEEL RLRLDQLGWA VRSAGSGEDS ATSSSTPLEN EEPDGLEASE
AGETNLELRL AQPLHLQFEG LTPQLSPSSG IPQAHTPSPQ RSQDLNTGPD EPLPNGEGEH
WRLLEQEPIT AQCLNSTDQS EFTLEPLLLV ADLLYWKDTR TSGAIFTGLM ASLLCLLHFS
IVSVAAHLAL LGLCATISLR VYRKVLQAVH RGDGTNPFQA YLDMDLTLTR EQTERLSQQI
ASHVVSTATQ LRHFFLVEDL VDSLKLALLF YILTFVGAIF NGLTLVILGV VALFTVPLLY
RQHQAQIDQY VGLVTSQLSH IKAKIRAKIP GTGTLAPAAS VSGSKAKAE
