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Database: UniProt
Entry: A0A7M4FJH6_CROPO
LinkDB: A0A7M4FJH6_CROPO
Original site: A0A7M4FJH6_CROPO 
ID   A0A7M4FJH6_CROPO        Unreviewed;       720 AA.
AC   A0A7M4FJH6;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   RecName: Full=Reticulon {ECO:0000256|RuleBase:RU210713};
GN   Name=RTN1 {ECO:0000313|Ensembl:ENSCPRP00005025929.1};
OS   Crocodylus porosus (Saltwater crocodile) (Estuarine crocodile).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Longirostres; Crocodylidae;
OC   Crocodylus.
OX   NCBI_TaxID=8502 {ECO:0000313|Ensembl:ENSCPRP00005025929.1, ECO:0000313|Proteomes:UP000594220};
RN   [1] {ECO:0000313|Ensembl:ENSCPRP00005025929.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSCPRP00005025929.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- FUNCTION: Inhibits amyloid precursor protein processing, probably by
CC       blocking BACE1 activity. {ECO:0000256|ARBA:ARBA00037306}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU210713}.
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DR   AlphaFoldDB; A0A7M4FJH6; -.
DR   Ensembl; ENSCPRT00005030287.1; ENSCPRP00005025929.1; ENSCPRG00005017988.1.
DR   GeneTree; ENSGT00940000155077; -.
DR   OMA; DICYSSQ; -.
DR   Proteomes; UP000594220; Unplaced.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0014069; C:postsynaptic density; IEA:TreeGrafter.
DR   GO; GO:0007420; P:brain development; IEA:TreeGrafter.
DR   GO; GO:0071787; P:endoplasmic reticulum tubular network formation; IEA:TreeGrafter.
DR   GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IEA:TreeGrafter.
DR   FunFam; 1.20.5.2480:FF:000001; Reticulon; 1.
DR   Gene3D; 1.20.5.2480; -; 1.
DR   InterPro; IPR003388; Reticulon.
DR   InterPro; IPR046964; RTN1-4.
DR   PANTHER; PTHR45799:SF5; RETICULON-1; 1.
DR   PANTHER; PTHR45799; RETICULON-LIKE PROTEIN; 1.
DR   Pfam; PF02453; Reticulon; 1.
DR   PROSITE; PS50845; RETICULON; 1.
PE   4: Predicted;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU210713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000594220};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU210713};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU210713}.
FT   TRANSMEM        587..616
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU210713"
FT   DOMAIN          573..701
FT                   /note="Reticulon"
FT                   /evidence="ECO:0000259|PROSITE:PS50845"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..67
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..320
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   720 AA;  78503 MW;  C2998357288704F6 CRC64;
     MGLRRPQPYL VPDPPSWVLS PPDAAHTGAG VRTPQNTAPS QALGTPPLLG SSYEASSTPT
     ASPSDPASSH FFDYTSTKAP NGGDASFYTT LISDVHYTTP RDSSYFTGIL QPENSHVICS
     DSTEGFSMLG HAIQEVTGFE SHGLFSSDSG IELTPAESTD VNKTLADPMK VEAYKYIDIS
     RSEEIKYQEK CETSPEDKSA GFLDRSPDAS AKLKHGSISP KTAFEETKVT KGQNLLEEEM
     FGDRQSASLI TSPVKITLTE TESTGEPVSK ETTIHKQETG LKPSHEVVPV VTVSEPEDDS
     PGSITPPSSG TEPSGSESQG KCSLSEDELI SAIKEAKGFT FEATEAQRSQ GVYAEKPDQK
     TKPGRPAASA PPDNEASSAE SGDSEIELVS EDPLAAEEVL HSNYMTFSHI GGPPPSPASP
     SIQYSILREE REAELDSELI IESCDASSAS EESPKREQDS PLMKPIIMDI IQEENGSRAD
     ASDYEVSNTT ESRMNRENLA ESASYLKCSF VAPKVSVEPP ASAVSTEELK ERIILKKPIE
     ETVVNQSKLS SKDSEKRSPL ASHQLQFLNK QKAIDLLYWR DIKQTGIVFG SLLLLLFSLT
     QFSVVSVIAY LALAALSATI SFRIYKSVLQ AVQKTDEGHP FKAYLEMEMS LSQDQIQKYT
     DCLQLYVNST VKELRRLFLV QDLVDSLKFA VLMWLLTYVG AQIDQYLGLV RTHINTVMAK
//
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