RETR1_RAT
ID RETR1_RAT Reviewed; 480 AA.
AC Q5FVM3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Reticulophagy regulator 1;
DE AltName: Full=Reticulophagy receptor 1 {ECO:0000305};
GN Name=Retreg1 {ECO:0000312|RGD:1565003}; Synonyms=Fam134b;
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 MRNA].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: Endoplasmic reticulum-anchored autophagy receptor that
CC mediates ER delivery into lysosomes through sequestration into
CC autophagosomes. Promotes membrane remodeling and ER scission via its
CC membrane bending capacity and targets the fragments into autophagosomes
CC via interaction with ATG8 family proteins. Required for long-term
CC survival of nociceptive and autonomic ganglion neurons.
CC {ECO:0000250|UniProtKB:Q9H6L5}.
CC -!- SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A,
CC MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2.
CC {ECO:0000250|UniProtKB:Q9H6L5}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q8VE91}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9H6L5}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The LIR motif interacts with ATG8 family proteins and is
CC necessary to target the ER fragments to autophagosomes for lysosomal
CC degradation. {ECO:0000250|UniProtKB:Q9H6L5}.
CC -!- DOMAIN: The reticulon homology domain provides capacity to bend the
CC membrane and promotes ER scission (By similarity). This domain does not
CC show relevant similarities with reticulon domains, preventing any
CC domain predictions within the protein sequence.
CC {ECO:0000250|UniProtKB:Q9H6L5, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RETREG family. {ECO:0000305}.
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DR EMBL; BC089887; AAH89887.1; -; mRNA.
DR RefSeq; NP_001030084.1; NM_001034912.1.
DR RefSeq; XP_008759043.1; XM_008760821.2.
DR RefSeq; XP_008773314.1; XM_008775092.1.
DR AlphaFoldDB; Q5FVM3; -.
DR STRING; 10116.ENSRNOP00000062258; -.
DR iPTMnet; Q5FVM3; -.
DR PhosphoSitePlus; Q5FVM3; -.
DR jPOST; Q5FVM3; -.
DR PaxDb; Q5FVM3; -.
DR PRIDE; Q5FVM3; -.
DR Ensembl; ENSRNOT00000063951; ENSRNOP00000062258; ENSRNOG00000010589.
DR GeneID; 619558; -.
DR KEGG; rno:619558; -.
DR UCSC; RGD:1565003; rat.
DR CTD; 54463; -.
DR RGD; 1565003; Retreg1.
DR eggNOG; ENOG502QPW8; Eukaryota.
DR GeneTree; ENSGT00390000018047; -.
DR InParanoid; Q5FVM3; -.
DR OMA; WPLISSQ; -.
DR OrthoDB; 901531at2759; -.
DR PhylomeDB; Q5FVM3; -.
DR PRO; PR:Q5FVM3; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010589; Expressed in stomach and 18 other tissues.
DR ExpressionAtlas; Q5FVM3; baseline and differential.
DR Genevisible; Q5FVM3; RN.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:GO_Central.
DR GO; GO:0140506; F:endoplasmic reticulum-autophagosome adaptor activity; ISO:RGD.
DR GO; GO:0006914; P:autophagy; ISO:RGD.
DR GO; GO:0030574; P:collagen catabolic process; ISO:RGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR GO; GO:0000423; P:mitophagy; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:GO_Central.
DR GO; GO:0061709; P:reticulophagy; ISS:GO_Central.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0050872; P:white fat cell differentiation; ISO:RGD.
DR InterPro; IPR033358; RETREG1.
DR InterPro; IPR043384; RETREG1/3.
DR PANTHER; PTHR28659; PTHR28659; 1.
DR PANTHER; PTHR28659:SF3; PTHR28659:SF3; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..480
FT /note="Reticulophagy regulator 1"
FT /id="PRO_0000288468"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..78
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..191
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..216
FT /note="Reticulon homology domain"
FT /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT REGION 302..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 436..441
FT /note="LIR motif"
FT /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT COMPBIAS 450..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 52782 MW; CA226070D013E00E CRC64;
MASPAPEEHA TQGCPATEEQ EPRPGVPGEE AGPEGAGPQV EEAAGRVAAA LTWLLGEPVL
WLGWRADELL SWKRPLRSLL AFLGANLLFW FLALTPWRVY HLISVMILGR VIMQIIKDMV
LSRARGAQLW RSLSESWEVI NSKPDERPRL SHCIAESWMN FSIFLQEMSL FKQQSPGKFC
LLVCSVCTFF TILGSYIPGV ILSYLLLLFA FLCPLFKCND IGQKIYSKVK SILLKLDFGI
GEYINQKKRE RSEADKEKSH KDDSEIDFSA LCPKISLTVA AKELSVSDTD VSEVSWTDNG
TFNLSEGYTP QTDTSDDLDR PSEEVFSRDL SDFPSLENGA GTNDEDELSL GLPTELKTKK
QQLNSAHRPS KDRQSAAGLS LPLKSDQALH LMSNLAGDVI TAAMTAAIKD QLEGARQALA
QAAPTPGDDT DTEEGDDFEL LDQAELDQIE SELGLTQDQG AEAQQSKKSS GFLSNLLGGH
