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RTN1_MOUSE
ID   RTN1_MOUSE              Reviewed;         780 AA.
AC   Q8K0T0; Q8K4S4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Reticulon-1;
DE   AltName: Full=Neuroendocrine-specific protein;
GN   Name=Rtn1; Synonyms=Nsp;
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], DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=12036513; DOI=10.1016/s0165-3806(02)00304-8;
RA   Hirata T., Nomura T., Takagi Y., Sato Y., Tomioka N., Fujisawa H.,
RA   Osumi N.;
RT   "Mosaic development of the olfactory cortex with Pax6-dependent and
RT   -independent components.";
RL   Brain Res. Dev. Brain Res. 136:17-26(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Olfactory epithelium;
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   PROTEIN SEQUENCE OF 181-190; 238-248; 647-654 AND 759-767, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-352 AND SER-487, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Lung, Spleen, and Testis;
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).
CC   -!- FUNCTION: Inhibits amyloid precursor protein processing, probably by
CC       blocking BACE1 activity. {ECO:0000250|UniProtKB:Q16799}.
CC   -!- SUBUNIT: Interacts with NDRG1. Interacts with BACE1. Interacts with
CC       TMEM33. {ECO:0000250|UniProtKB:Q16799}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12036513}; Multi-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q16799};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: At 12.5 dpc-14.5 dpc, strongly expressed in radial
CC       glial fibers, which are a scaffold for migrating neurons (at protein
CC       level). {ECO:0000269|PubMed:12036513}.
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DR   EMBL; AB074899; BAB96551.1; -; mRNA.
DR   EMBL; BC030455; AAH30455.1; -; mRNA.
DR   EMBL; BC053926; AAH53926.1; -; mRNA.
DR   EMBL; BC058579; AAH58579.1; -; mRNA.
DR   EMBL; BK001694; DAA01939.1; -; mRNA.
DR   CCDS; CCDS25968.1; -.
DR   RefSeq; NP_001273377.1; NM_001286448.1.
DR   RefSeq; NP_703187.2; NM_153457.7.
DR   AlphaFoldDB; Q8K0T0; -.
DR   SMR; Q8K0T0; -.
DR   BioGRID; 222271; 12.
DR   CORUM; Q8K0T0; -.
DR   IntAct; Q8K0T0; 3.
DR   STRING; 10090.ENSMUSP00000077594; -.
DR   iPTMnet; Q8K0T0; -.
DR   PhosphoSitePlus; Q8K0T0; -.
DR   SwissPalm; Q8K0T0; -.
DR   jPOST; Q8K0T0; -.
DR   MaxQB; Q8K0T0; -.
DR   PaxDb; Q8K0T0; -.
DR   PRIDE; Q8K0T0; -.
DR   ProteomicsDB; 262724; -.
DR   Antibodypedia; 3447; 509 antibodies from 26 providers.
DR   DNASU; 104001; -.
DR   Ensembl; ENSMUST00000078505; ENSMUSP00000077594; ENSMUSG00000021087.
DR   GeneID; 104001; -.
DR   KEGG; mmu:104001; -.
DR   UCSC; uc007nvk.2; mouse.
DR   CTD; 6252; -.
DR   MGI; MGI:1933947; Rtn1.
DR   VEuPathDB; HostDB:ENSMUSG00000021087; -.
DR   eggNOG; KOG1792; Eukaryota.
DR   GeneTree; ENSGT00940000155077; -.
DR   HOGENOM; CLU_018293_0_0_1; -.
DR   InParanoid; Q8K0T0; -.
DR   OrthoDB; 244299at2759; -.
DR   PhylomeDB; Q8K0T0; -.
DR   TreeFam; TF105431; -.
DR   BioGRID-ORCS; 104001; 2 hits in 70 CRISPR screens.
DR   ChiTaRS; Rtn1; mouse.
DR   PRO; PR:Q8K0T0; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8K0T0; protein.
DR   Bgee; ENSMUSG00000021087; Expressed in dentate gyrus of hippocampal formation granule cell and 187 other tissues.
DR   ExpressionAtlas; Q8K0T0; baseline and differential.
DR   Genevisible; Q8K0T0; MM.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR   GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:UniProtKB.
DR   InterPro; IPR003388; Reticulon.
DR   Pfam; PF02453; Reticulon; 1.
DR   PROSITE; PS50845; RETICULON; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..780
FT                   /note="Reticulon-1"
FT                   /id="PRO_0000168159"
FT   TRANSMEM        607..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        709..729
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          593..780
FT                   /note="Reticulon"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64548"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64548"
FT   MOD_RES         327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64548"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         487
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        71
FT                   /note="P -> S (in Ref. 1; BAB96551)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="D -> G (in Ref. 1; BAB96551)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   780 AA;  83572 MW;  29B47A58FC2F2027 CRC64;
     MAAPPDLQDE PLSLGSPGSQ WFGGRGDGED EATAVMGARP AQQDGEPAWG SGAGAGVTSS
     RELCSGPARS PPVAMETAST GMAAVPDALD HSPSSTLKDG EGACYTSLIS DVCYPPREDS
     AYFTGILQKE NGHITTSESP EEPETPGPSL PEVPGMEPQG LLSSDSGIEM TPAESTEVNK
     ILADPLDQMK AEAYKYIDIT RPQEAKGQEE QHPGLEDKDL DFKDKDTEVS TKAEGVRAPN
     QPAPVEGKLI KDHLFEESTF APYIDELSDE QHRVSLVTAP VKITLTEIEP PLMTATQETI
     PEKQDLCLKP SPDTVPTVTV SEPEDDSPGS VTPPSSGTEP SAAESQGKGS VSEDELIAAI
     KEAKGLSYET TESPRPVGQV ADKPKTKTRS GLPTIPSPLD QEASSAESGD SEIELVSEDP
     MASEDALPSG YVSFGHVSGP PPSPASPSIQ YSILREEREA ELDSELIIES CDASSASEES
     PKREQDSPPM KPGALDAIRE ETGSRATEER APSHQGPVEP DPMLSFAPAA ALQSRPEPSS
     GDGASVPEPP RSQQQKPEEE AVSSSQSPTA TEIPGPLGSG LMPPLPFFNK QKAIDLLYWR
     DIKQTGIVFG SFLLLLFSLT QFSVVSVVAY LALAALSATI SFRIYKSVLQ AVQKTDEGHP
     FKAYLELEIT LSQEQIQKYT DCLQLYVNST LKELRRLFLV QDLVDSLKFA VLMWLLTYVG
     ALFNGLTLLL MAVVSMFTLP VVYVKHQAQV DQYLGLVRTH INTVVAKIQA KIPGAKRHAE
 
 
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