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Reticulophagy regulator 1 (Reticulophagy receptor 1)

 RETR1_HUMAN             Reviewed;         497 AA.
Q9H6L5; Q69YN8; Q9H6K6; Q9H764; Q9NXM8;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 118.
RecName: Full=Reticulophagy regulator 1 {ECO:0000312|HGNC:HGNC:25964};
AltName: Full=Reticulophagy receptor 1 {ECO:0000305};
Name=RETREG1 {ECO:0000312|HGNC:HGNC:25964};
Synonyms=FAM134B, JK1 {ECO:0000303|PubMed:17487424};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-497.
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
TISSUE SPECIFICITY.
PubMed=17487424;
Tang W.K., Chui C.H., Fatima S., Kok S.H., Pak K.C., Ou T.M.,
Hui K.S., Wong M.M., Wong J., Law S., Tsao S.W., Lam K.Y., Beh P.S.,
Srivastava G., Chan A.S., Ho K.P., Tang J.C.;
"Oncogenic properties of a novel gene JK-1 located in chromosome 5p
and its overexpression in human esophageal squamous cell carcinoma.";
Int. J. Mol. Med. 19:915-923(2007).
[5]
FUNCTION, AND INVOLVEMENT IN HSAN2B.
PubMed=19838196; DOI=10.1038/ng.464;
Kurth I., Pamminger T., Hennings J.C., Soehendra D., Huebner A.K.,
Rotthier A., Baets J., Senderek J., Topaloglu H., Farrell S.A.,
Nuernberg G., Nurnberg P., De Jonghe P., Gal A., Kaether C.,
Timmerman V., Huebner C.A.;
"Mutations in FAM134B, encoding a newly identified Golgi protein,
cause severe sensory and autonomic neuropathy.";
Nat. Genet. 41:1179-1181(2009).
[6]
FUNCTION, INTERACTION WITH MAP1LC3A; MAP1LC3B; GABARAP; GABARAPL1 AND
GABARAPL2, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF
453-ASP--LEU-458.
PubMed=26040720; DOI=10.1038/nature14498;
Khaminets A., Heinrich T., Mari M., Grumati P., Huebner A.K.,
Akutsu M., Liebmann L., Stolz A., Nietzsche S., Koch N., Mauthe M.,
Katona I., Qualmann B., Weis J., Reggiori F., Kurth I., Huebner C.A.,
Dikic I.;
"Regulation of endoplasmic reticulum turnover by selective
autophagy.";
Nature 522:354-358(2015).
[7]
VARIANT ARG-216.
PubMed=22302274; DOI=10.1007/s00415-011-6397-y;
Davidson G.L., Murphy S.M., Polke J.M., Laura M., Salih M.A.,
Muntoni F., Blake J., Brandner S., Davies N., Horvath R., Price S.,
Donaghy M., Roberts M., Foulds N., Ramdharry G., Soler D., Lunn M.P.,
Manji H., Davis M.B., Houlden H., Reilly M.M.;
"Frequency of mutations in the genes associated with hereditary
sensory and autonomic neuropathy in a UK cohort.";
J. Neurol. 259:1673-1685(2012).
-!- FUNCTION: Endoplasmic reticulum-anchored autophagy receptor that
mediates ER delivery into lysosomes through sequestration into
autophagosomes (PubMed:26040720). 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). Required for long-term survival of
nociceptive and autonomic ganglion neurons (PubMed:19838196,
PubMed:26040720). {ECO:0000269|PubMed:19838196,
ECO:0000269|PubMed:26040720}.
-!- SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A,
MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2.
{ECO:0000269|PubMed:26040720}.
-!- INTERACTION:
P60520:GABARAPL2; NbExp=2; IntAct=EBI-16159046, EBI-720116;
Q9H492-1:MAP1LC3A; NbExp=2; IntAct=EBI-16159046, EBI-16082793;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H6L5-1; Sequence=Displayed;
Name=2;
IsoId=Q9H6L5-2; Sequence=VSP_025685, VSP_025686;
-!- TISSUE SPECIFICITY: Overexpressed in esophageal squamous cell
carcinoma (PubMed:17487424). {ECO:0000269|PubMed:17487424}.
-!- DOMAIN: The LIR motif interacts with ATG8 family proteins and is
necessary to target the ER fragments to autophagosomes for
subsequent lysosomal degradation. {ECO:0000269|PubMed:26040720}.
-!- DOMAIN: The reticulon homology domain provides capacity to bend
the membrane and promotes ER scission (PubMed:26040720). This
domain does not show relevant similarities with reticulon domains,
preventing any domain predictions within the protein sequence.
{ECO:0000269|PubMed:26040720, ECO:0000305}.
-!- 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 mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the RETREG family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH30517.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA90982.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15252.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AK000159; BAA90982.1; ALT_INIT; mRNA.
EMBL; AK024920; BAB15034.1; -; mRNA.
EMBL; AK025808; BAB15241.1; -; mRNA.
EMBL; AK025832; BAB15252.1; ALT_INIT; mRNA.
EMBL; BC030517; AAH30517.1; ALT_INIT; mRNA.
EMBL; BC053326; AAH53326.1; -; mRNA.
EMBL; BC073132; AAH73132.1; -; mRNA.
EMBL; AL832438; CAH10610.1; -; mRNA.
CCDS; CCDS43304.1; -. [Q9H6L5-1]
CCDS; CCDS43305.1; -. [Q9H6L5-2]
RefSeq; NP_001030022.1; NM_001034850.2. [Q9H6L5-1]
RefSeq; NP_061873.2; NM_019000.4. [Q9H6L5-2]
UniGene; Hs.481704; -.
ProteinModelPortal; Q9H6L5; -.
BioGrid; 119969; 4.
DIP; DIP-61577N; -.
IntAct; Q9H6L5; 15.
STRING; 9606.ENSP00000304642; -.
iPTMnet; Q9H6L5; -.
PhosphoSitePlus; Q9H6L5; -.
BioMuta; FAM134B; -.
DMDM; 74733613; -.
MaxQB; Q9H6L5; -.
PaxDb; Q9H6L5; -.
PeptideAtlas; Q9H6L5; -.
PRIDE; Q9H6L5; -.
DNASU; 54463; -.
Ensembl; ENST00000306320; ENSP00000304642; ENSG00000154153. [Q9H6L5-1]
Ensembl; ENST00000399793; ENSP00000382691; ENSG00000154153. [Q9H6L5-2]
GeneID; 54463; -.
KEGG; hsa:54463; -.
UCSC; uc003jfr.4; human. [Q9H6L5-1]
CTD; 54463; -.
DisGeNET; 54463; -.
EuPathDB; HostDB:ENSG00000154153.13; -.
GeneCards; RETREG1; -.
GeneReviews; FAM134B; -.
H-InvDB; HIX0004766; -.
HGNC; HGNC:25964; RETREG1.
HPA; HPA012077; -.
MalaCards; RETREG1; -.
MIM; 613114; gene.
MIM; 613115; phenotype.
neXtProt; NX_Q9H6L5; -.
OpenTargets; ENSG00000154153; -.
Orphanet; 970; Hereditary sensory and autonomic neuropathy type 2.
PharmGKB; PA162386188; -.
eggNOG; ENOG410IFP1; Eukaryota.
eggNOG; ENOG410XPQB; LUCA.
GeneTree; ENSGT00530000063240; -.
HOGENOM; HOG000050246; -.
HOVERGEN; HBG071073; -.
InParanoid; Q9H6L5; -.
OMA; LSESWEV; -.
OrthoDB; EOG091G08S3; -.
PhylomeDB; Q9H6L5; -.
TreeFam; TF329111; -.
ChiTaRS; FAM134B; human.
GenomeRNAi; 54463; -.
PRO; PR:Q9H6L5; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000154153; -.
CleanEx; HS_FAM134B; -.
ExpressionAtlas; Q9H6L5; baseline and differential.
Genevisible; Q9H6L5; HS.
GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:GO_Central.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:GO_Central.
GO; GO:0061709; P:reticulophagy; IMP:GO_Central.
GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
InterPro; IPR033358; RETREG1.
PANTHER; PTHR28659:SF3; PTHR28659:SF3; 1.
1: Evidence at protein level;
Alternative splicing; Autophagy; Complete proteome;
Endoplasmic reticulum; Golgi apparatus; Membrane; Neurodegeneration;
Neuropathy; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 497 Reticulophagy regulator 1.
/FTId=PRO_0000288466.
TOPO_DOM 1 59 Cytoplasmic.
{ECO:0000269|PubMed:26040720}.
TRANSMEM 60 80 Helical. {ECO:0000255}.
TOPO_DOM 81 95 Lumenal. {ECO:0000305}.
TRANSMEM 96 116 Helical. {ECO:0000255}.
TOPO_DOM 117 118 Cytoplasmic. {ECO:0000305}.
TRANSMEM 119 139 Helical. {ECO:0000255}.
TOPO_DOM 140 208 Lumenal. {ECO:0000305}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TOPO_DOM 230 497 Cytoplasmic.
{ECO:0000269|PubMed:26040720}.
REGION 84 233 Reticulon homology domain.
{ECO:0000305|PubMed:26040720}.
MOTIF 453 458 LIR motif. {ECO:0000305|PubMed:26040720}.
VAR_SEQ 1 141 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_025685.
VAR_SEQ 142 152 RGAQLWRSLSE -> MPEGEDFGPGK (in isoform
2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_025686.
VARIANT 216 216 G -> R (found in a patient with HSAN2B;
uncertain pathological significance).
{ECO:0000269|PubMed:22302274}.
/FTId=VAR_068477.
VARIANT 379 379 Q -> E (in dbSNP:rs34432513).
/FTId=VAR_032422.
MUTAGEN 453 458 DDFELL->AAAAAA: Abolishes interaction
with ATG8 family proteins.
{ECO:0000269|PubMed:26040720}.
CONFLICT 382 382 S -> G (in Ref. 1; BAB15252).
{ECO:0000305}.
SEQUENCE 497 AA; 54681 MW; 4EEB84B941DBFCE5 CRC64;
MASPAPPEHA EEGCPAPAAE EQAPPSPPPP QASPAERQQQ EEEAQEAGAA EGAGLQVEEA
AGRAAAAVTW LLGEPVLWLG CRADELLSWK RPLRSLLGFV AANLLFWFLA LTPWRVYHLI
SVMILGRVIM QIIKDMVLSR TRGAQLWRSL SESWEVINSK PDERPRLSHC IAESWMNFSI
FLQEMSLFKQ QSPGKFCLLV CSVCTFFTIL GSYIPGVILS YLLLLCAFLC PLFKCNDIGQ
KIYSKIKSVL LKLDFGIGEY INQKKRERSE ADKEKSHKDD SELDFSALCP KISLTVAAKE
LSVSDTDVSE VSWTDNGTFN LSEGYTPQTD TSDDLDRPSE EVFSRDLSDF PSLENGMGTN
DEDELSLGLP TELKRKKEQL DSGHRPSKET QSAAGLTLPL NSDQTFHLMS NLAGDVITAA
VTAAIKDQLE GVQQALSQAA PIPEEDTDTE EGDDFELLDQ SELDQIESEL GLTQDQEAEA
QQNKKSSGFL SNLLGGH


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