RETREG1
entrez
54463
canonical
uniprot
Q9H6L5
canonical
ensembl
ENSG00000154153
resolver
ensp
ENSP00000304642
resolver
ensp
ENSP00000382691
resolver
ensp
ENSP00000506804
resolver
ensp
ENSP00000671303
resolver
enst
ENST00000682142
resolver
genesymbol
RETREG1
resolver
genesymbol_syn
FAM134B
resolver
genesymbol_syn
JK1
resolver
hgnc
HGNC:25964
resolver
uniprot
A0A804HHX5
resolver
uniprot
Q69YN8
resolver
uniprot
Q9H6K6
resolver
uniprot
Q9H764
resolver
uniprot
Q9NXM8
resolver
uniprot_entry
A0A804HHX5_HUMAN
resolver
uniprot_entry
RETR1_HUMAN
resolver
uniprot_sec
Q69YN8
resolver
uniprot_sec
Q9H6K6
resolver
uniprot_sec
Q9H764
resolver
uniprot_sec
Q9NXM8
resolver
amino_acid_sequence
MASPAPPEHAEEGCPAPAAEEQAPPSPPPPQASPAERQQQEEEAQEAGAAEGAGLQVEEAAGRAAAAVTWLLGEPVLWLGCRADELLSWKRPLRSLLGFVAANLLFWFLALTPWRVYHLISVMILGRVIMQIIKDMVLSRTRGAQLWRSLSESWEVINSKPDERPRLSHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLLCAFLCPLFKCNDIGQKIYSKIKSVLLKLDFGIGEYINQKKRERSEADKEKSHKDDSELDFSALCPKISLTVAAKELSVSDTDVSEVSWTDNGTFNLSEGYTPQTDTSDDLDRPSEEVFSRDLSDFPSLENGMGTNDEDELSLGLPTELKRKKEQLDSGHRPSKETQSAAGLTLPLNSDQTFHLMSNLAGDVITAAVTAAIKDQLEGVQQALSQAAPIPEEDTDTEEGDDFELLDQSELDQIESELGLTQDQEAEAQQNKKSSGFLSNLLGGH
uniprot
proteins
disease_involvement
DISEASE: Neuropathy, hereditary sensory and autonomic, 2B (HSAN2B) [MIM:613115]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by sensory and/or autonomic abnormalities. HSAN2B is an autosomal recessive disorder characterized by impairment of pain, temperature and touch sensation. Onset occurs in the first or second decade, with impaired nociception and progressive mutilating ulceration of the hands and feet with osteomyelitis and acroosteolysis. Amputations of the hands and feet are common. Autonomic dysfunction includes hyperhidrosis, urinary incontinence, and slow pupillary light response. {ECO:0000269|PubMed:19838196}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Endoplasmic reticulum (ER)-anchored autophagy regulator which mediates ER delivery into lysosomes through sequestration into autophagosomes (PubMed:26040720, PubMed:31930741, PubMed:34338405). Promotes membrane remodeling and ER scission via its membrane bending capacity and targets the fragments into autophagosomes via interaction with ATG8 family proteins (PubMed:26040720, PubMed:31930741, PubMed:34338405). Active under basal conditions (PubMed:34338405). Required for collagen quality control in a LIR motif-dependent manner (By similarity). Required for long-term survival of nociceptive and autonomic ganglion neurons (PubMed:19838196, PubMed:26040720). {ECO:0000250|UniProtKB:Q8VE91, ECO:0000269|PubMed:19838196, ECO:0000269|PubMed:26040720, ECO:0000269|PubMed:34338405}.; FUNCTION: (Microbial infection) During SARS-CoV-2 infection, RETREG1-mediated reticulophagy is promoted by SARS-CoV-2 ORF3A protein (PubMed:35239449). This induces endoplasmic reticulum stress and inflammatory responses and facilitates viral infection (PubMed:35239449). {ECO:0000269|PubMed:35239449}.
uniprot
proteins
mass_dalton
54681
uniprot
proteins
mutagenesis
MUTAGEN 149; /note="S->A: Reduces self-association."; /evidence="ECO:0000269|PubMed:31930741"; MUTAGEN 149; /note="S->D: Phosphomimetic mutant which enhances self-association. Enhanced membrane scission activity; when associated with D-151 and D-153."; /evidence="ECO:0000269|PubMed:31930741"; MUTAGEN 151; /note="S->A: Abolishes phosphorylation and reduces self-association."; /evidence="ECO:0000269|PubMed:31930741"; MUTAGEN 151; /note="S->D: Phosphomimetic mutant which enhances self-association. Enhanced membrane scission activity; when associated with D-149 and D-153."; /evidence="ECO:0000269|PubMed:31930741"; MUTAGEN 153; /note="S->A: Reduces self-association."; /evidence="ECO:0000269|PubMed:31930741"; MUTAGEN 153; /note="S->D: Phosphomimetic mutant which enhances self-association. Enhanced membrane scission activity; when associated with D-149 and D-151."; /evidence="ECO:0000269|PubMed:31930741"; MUTAGEN 453..458; /note="DDFELL->AAAAAA: Abolishes interaction with ATG8 family proteins."; /evidence="ECO:0000269|PubMed:26040720"; MUTAGEN 455..458; /note="FELL->AELA: Abolishes interaction with ATG8 family proteins and reduces endoplasmic reticulum branching."; /evidence="ECO:0000269|PubMed:34338405"; MUTAGEN 456; /note="E->R: Severely impaired binding to GABARAP."; /evidence="ECO:0000269|PubMed:34854256"; MUTAGEN 462; /note="E->R: Severely impaired binding to GABARAP."; /evidence="ECO:0000269|PubMed:34854256"; MUTAGEN 463; /note="L->Q: Mildly weakened binding to GABARAP."; /evidence="ECO:0000269|PubMed:34854256"; MUTAGEN 466; /note="I->Q: Mildly weakened binding to GABARAP."; /evidence="ECO:0000269|PubMed:34854256
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-151 by CAMK2B enhances oligomerization and membrane scission and reticulophagy activity. {ECO:0000269|PubMed:31930741}.
uniprot
proteins
protein_family
RETREG family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17487424
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19838196
uniprot
proteins
pubmed
22302274
uniprot
proteins
pubmed
26040720
uniprot
proteins
pubmed
31930741
uniprot
proteins
pubmed
32620754
uniprot
proteins
pubmed
34338405
uniprot
proteins
pubmed
34854256
uniprot
proteins
pubmed
35239449
uniprot
proteins
sequence_length
497
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q8VE91}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:26040720}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:35239449}; Multi-pass membrane protein {ECO:0000255}. Note=(Microbial infection) Following SARS-CoV-2 infection, colocalizes with SARS-CoV-2 ORF3A protein at the endoplasmic reticulum. {ECO:0000269|PubMed:35239449}.
uniprot
proteins
transmembrane_region
TRANSMEM 60..80; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 96..116; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 119..139; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 209..229; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins