ID   RTN1_PANTR              Reviewed;         776 AA.
AC   Q5IS59;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Reticulon-1;
GN   Name=RTN1;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
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:0000250|UniProtKB:Q16799}; Multi-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q16799};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
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DR   EMBL; AY665269; AAV74307.1; -; mRNA.
DR   RefSeq; NP_001029293.1; NM_001034121.1.
DR   AlphaFoldDB; Q5IS59; -.
DR   SMR; Q5IS59; -.
DR   STRING; 9598.ENSPTRP00000056915; -.
DR   PaxDb; Q5IS59; -.
DR   GeneID; 452945; -.
DR   KEGG; ptr:452945; -.
DR   CTD; 6252; -.
DR   eggNOG; KOG1792; Eukaryota.
DR   InParanoid; Q5IS59; -.
DR   OrthoDB; 244299at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Golgi apparatus; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..776
FT                   /note="Reticulon-1"
FT                   /id="PRO_0000168160"
FT   TRANSMEM        603..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        705..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          589..776
FT                   /note="Reticulon"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64548"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K0T0"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K0T0"
FT   MOD_RES         487
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16799"
SQ   SEQUENCE   776 AA;  83526 MW;  4ABD323931268BC4 CRC64;
     MAAPGDPQDE LLPLAGPGSQ WLRDRGEGED EAVTPKGATP APQAGEPSPG LGARAREAAS
     REAGSGPARQ SPVAMETAST GVAGVSSAMD HTFSTTSKDG EGSCYTSLIS DICYPPQEDS
     TYFTGILQRE NGHVTISESP EELGTPGSSL PDVPGIESRG LFSSDSGIEM TPAESTEVNK
     ILADPLDQMK AEAYKYIDIT RPEEVKHQEQ NHPELEDKDL DFKNKDTDIS IKPEGVREPD
     EPAPVEGKII KDHLLEESTF APYIDDLSEE QRRAPQITTP VKITLTEIEP SVETTTQEKT
     PEKQDICLKP SPDTVPTVTV SEPEDDSPGS ITPPSSGTEP SAAESQGKGS ISEDELITAI
     KEAKGLSYET AESPRPVGQL ADRPEVKARS GPPTIPSPLD HEASSAESGD SEIELVSEDP
     MAAEDALPSG YVSFGHVGGP PPSPASPSIQ YSILREEREA ELDSELIIES CDASSASEES
     PKREQDSPPM KPGALDAIRE ETGVRAEERA PSRRGLAEPA SFLDYPSTEP QPGPELPPGD
     GALEPETPTL PRKPEEDASS HQSPAATKGP GPLGPGAPPP LLFLNKQKAI DLLYWRDIKQ
     TGIVFGSFLL LLFSLTQFSV VSVVAYLALA ALSATISFRI YKSVLQAVQK TDEGHPFKAY
     LELEITLSQE QIQKYTDCLQ FYVNSTLKEL RRLFLVQDLV DSLKFAVLMW LLTYVGALFN
     GLTLLLMAVV SMFTLPVVYV KHQAQIDQYL GLVRTHINAV VAKIQAKIPG AKRHAE