Full text data of REEP5
REEP5
(C5orf18, DP1, TB2)
[Confidence: high (present in two of the MS resources)]
Receptor expression-enhancing protein 5 (Polyposis locus protein 1; Protein TB2)
Receptor expression-enhancing protein 5 (Polyposis locus protein 1; Protein TB2)
hRBCD
IPI00024670
IPI00024670 Polyposis locus protein 1 Polyposis locus protein 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 2 2 2 1 n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00024670 Polyposis locus protein 1 Polyposis locus protein 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 2 2 2 1 n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
Q00765
ID REEP5_HUMAN Reviewed; 189 AA.
AC Q00765; D3DT04; Q04198; Q5QGT0; Q9BWH9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-NOV-2005, sequence version 3.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Receptor expression-enhancing protein 5;
DE AltName: Full=Polyposis locus protein 1;
DE AltName: Full=Protein TB2;
GN Name=REEP5; Synonyms=C5orf18, DP1, TB2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1678319; DOI=10.1016/0092-8674(81)90022-2;
RA Joslyn G., Carlson M., Thliveris A., Albertsen H., Gelbert L.,
RA Samowitz W., Groden J., Stevens J., Spirio L., Robertson M.,
RA Sargeant L., Krapcho K., Wolff E., Burt R., Hughes J.P.,
RA Warrington J., McPherson J.D., Wasmuth J.J., le Paslier D.,
RA Abderrahim H., Cohen D., Leppert M., White R.;
RT "Identification of deletion mutations and three new genes at the
RT familial polyposis locus.";
RL Cell 66:601-613(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1651562; DOI=10.1126/science.1651562;
RA Kinzler K.W., Nilbert M.C., Su L.-K., Vogelstein B., Bryan T.M.,
RA Levy D.B., Smith K.J., Preisinger A.C., Hedge P., McKechnie D.,
RA Finniear R., Markham A., Groffen J., Boguski M.S., Altschul S.F.,
RA Horii A.K., Ando H., Miyoshi Y., Miki Y., Nishisho I., Nakamura Y.;
RT "Identification of FAP locus genes from chromosome 5q21.";
RL Science 253:661-665(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT "RTP family members induce functional expression of mammalian odorant
RT receptors.";
RL Cell 119:679-691(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH ATL2.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the
RT tubular ER network.";
RL Cell 138:549-561(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-162 AND LYS-164, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May promote functional cell surface expression of
CC olfactory receptors.
CC -!- SUBUNIT: Interacts with ATL1 (By similarity). Interacts with ATL2.
CC -!- INTERACTION:
CC Q6P1Q0:LETMD1; NbExp=3; IntAct=EBI-1549827, EBI-1549822;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- SIMILARITY: Belongs to the DP1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60136.1; Type=Erroneous initiation;
CC Sequence=AAA66351.1; Type=Erroneous initiation;
CC Sequence=AAH65926.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M73547; AAA60136.1; ALT_INIT; mRNA.
DR EMBL; M74090; AAA66351.1; ALT_INIT; mRNA.
DR EMBL; AY562243; AAT70688.1; -; mRNA.
DR EMBL; CH471086; EAW48994.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW48995.1; -; Genomic_DNA.
DR EMBL; BC000232; AAH00232.2; -; mRNA.
DR EMBL; BC065926; AAH65926.1; ALT_INIT; mRNA.
DR PIR; A39658; A39658.
DR RefSeq; NP_005660.4; NM_005669.4.
DR UniGene; Hs.429608; -.
DR ProteinModelPortal; Q00765; -.
DR IntAct; Q00765; 7.
DR MINT; MINT-237079; -.
DR STRING; 9606.ENSP00000368959; -.
DR PhosphoSite; Q00765; -.
DR DMDM; 82654932; -.
DR PaxDb; Q00765; -.
DR PRIDE; Q00765; -.
DR DNASU; 7905; -.
DR Ensembl; ENST00000379638; ENSP00000368959; ENSG00000129625.
DR GeneID; 7905; -.
DR KEGG; hsa:7905; -.
DR UCSC; uc003kqe.1; human.
DR CTD; 7905; -.
DR GeneCards; GC05M112212; -.
DR HGNC; HGNC:30077; REEP5.
DR HPA; HPA003895; -.
DR MIM; 125265; gene.
DR neXtProt; NX_Q00765; -.
DR PharmGKB; PA134882361; -.
DR eggNOG; COG5052; -.
DR HOGENOM; HOG000172351; -.
DR HOVERGEN; HBG000796; -.
DR InParanoid; Q00765; -.
DR KO; K17279; -.
DR OMA; VPKSYAF; -.
DR OrthoDB; EOG747PKP; -.
DR GeneWiki; REEP5; -.
DR GenomeRNAi; 7905; -.
DR NextBio; 30368; -.
DR PRO; PR:Q00765; -.
DR ArrayExpress; Q00765; -.
DR Bgee; Q00765; -.
DR CleanEx; HS_REEP5; -.
DR Genevestigator; Q00765; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR PANTHER; PTHR12300; PTHR12300; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 189 Receptor expression-enhancing protein 5.
FT /FTId=PRO_0000101815.
FT TRANSMEM 35 55 Helical; (Potential).
FT TRANSMEM 90 110 Helical; (Potential).
FT MOD_RES 162 162 N6-acetyllysine.
FT MOD_RES 164 164 N6-acetyllysine.
FT CONFLICT 115 115 M -> I (in Ref. 2; AAA66351).
FT CONFLICT 163 163 A -> S (in Ref. 1; AAA60136).
SQ SEQUENCE 189 AA; 21493 MW; F4E57E500CB7C831 CRC64;
MSAAMRERFD RFLHEKNCMT DLLAKLEAKT GVNRSFIALG VIGLVALYLV FGYGASLLCN
LIGFGYPAYI SIKAIESPNK EDDTQWLTYW VVYGVFSIAE FFSDIFLSWF PFYYMLKCGF
LLWCMAPSPS NGAELLYKRI IRPFFLKHES QMDSVVKDLK DKAKETADAI TKEAKKATVN
LLGEEKKST
//
ID REEP5_HUMAN Reviewed; 189 AA.
AC Q00765; D3DT04; Q04198; Q5QGT0; Q9BWH9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-NOV-2005, sequence version 3.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Receptor expression-enhancing protein 5;
DE AltName: Full=Polyposis locus protein 1;
DE AltName: Full=Protein TB2;
GN Name=REEP5; Synonyms=C5orf18, DP1, TB2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1678319; DOI=10.1016/0092-8674(81)90022-2;
RA Joslyn G., Carlson M., Thliveris A., Albertsen H., Gelbert L.,
RA Samowitz W., Groden J., Stevens J., Spirio L., Robertson M.,
RA Sargeant L., Krapcho K., Wolff E., Burt R., Hughes J.P.,
RA Warrington J., McPherson J.D., Wasmuth J.J., le Paslier D.,
RA Abderrahim H., Cohen D., Leppert M., White R.;
RT "Identification of deletion mutations and three new genes at the
RT familial polyposis locus.";
RL Cell 66:601-613(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1651562; DOI=10.1126/science.1651562;
RA Kinzler K.W., Nilbert M.C., Su L.-K., Vogelstein B., Bryan T.M.,
RA Levy D.B., Smith K.J., Preisinger A.C., Hedge P., McKechnie D.,
RA Finniear R., Markham A., Groffen J., Boguski M.S., Altschul S.F.,
RA Horii A.K., Ando H., Miyoshi Y., Miki Y., Nishisho I., Nakamura Y.;
RT "Identification of FAP locus genes from chromosome 5q21.";
RL Science 253:661-665(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT "RTP family members induce functional expression of mammalian odorant
RT receptors.";
RL Cell 119:679-691(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH ATL2.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the
RT tubular ER network.";
RL Cell 138:549-561(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-162 AND LYS-164, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May promote functional cell surface expression of
CC olfactory receptors.
CC -!- SUBUNIT: Interacts with ATL1 (By similarity). Interacts with ATL2.
CC -!- INTERACTION:
CC Q6P1Q0:LETMD1; NbExp=3; IntAct=EBI-1549827, EBI-1549822;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- SIMILARITY: Belongs to the DP1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60136.1; Type=Erroneous initiation;
CC Sequence=AAA66351.1; Type=Erroneous initiation;
CC Sequence=AAH65926.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M73547; AAA60136.1; ALT_INIT; mRNA.
DR EMBL; M74090; AAA66351.1; ALT_INIT; mRNA.
DR EMBL; AY562243; AAT70688.1; -; mRNA.
DR EMBL; CH471086; EAW48994.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW48995.1; -; Genomic_DNA.
DR EMBL; BC000232; AAH00232.2; -; mRNA.
DR EMBL; BC065926; AAH65926.1; ALT_INIT; mRNA.
DR PIR; A39658; A39658.
DR RefSeq; NP_005660.4; NM_005669.4.
DR UniGene; Hs.429608; -.
DR ProteinModelPortal; Q00765; -.
DR IntAct; Q00765; 7.
DR MINT; MINT-237079; -.
DR STRING; 9606.ENSP00000368959; -.
DR PhosphoSite; Q00765; -.
DR DMDM; 82654932; -.
DR PaxDb; Q00765; -.
DR PRIDE; Q00765; -.
DR DNASU; 7905; -.
DR Ensembl; ENST00000379638; ENSP00000368959; ENSG00000129625.
DR GeneID; 7905; -.
DR KEGG; hsa:7905; -.
DR UCSC; uc003kqe.1; human.
DR CTD; 7905; -.
DR GeneCards; GC05M112212; -.
DR HGNC; HGNC:30077; REEP5.
DR HPA; HPA003895; -.
DR MIM; 125265; gene.
DR neXtProt; NX_Q00765; -.
DR PharmGKB; PA134882361; -.
DR eggNOG; COG5052; -.
DR HOGENOM; HOG000172351; -.
DR HOVERGEN; HBG000796; -.
DR InParanoid; Q00765; -.
DR KO; K17279; -.
DR OMA; VPKSYAF; -.
DR OrthoDB; EOG747PKP; -.
DR GeneWiki; REEP5; -.
DR GenomeRNAi; 7905; -.
DR NextBio; 30368; -.
DR PRO; PR:Q00765; -.
DR ArrayExpress; Q00765; -.
DR Bgee; Q00765; -.
DR CleanEx; HS_REEP5; -.
DR Genevestigator; Q00765; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR PANTHER; PTHR12300; PTHR12300; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 189 Receptor expression-enhancing protein 5.
FT /FTId=PRO_0000101815.
FT TRANSMEM 35 55 Helical; (Potential).
FT TRANSMEM 90 110 Helical; (Potential).
FT MOD_RES 162 162 N6-acetyllysine.
FT MOD_RES 164 164 N6-acetyllysine.
FT CONFLICT 115 115 M -> I (in Ref. 2; AAA66351).
FT CONFLICT 163 163 A -> S (in Ref. 1; AAA60136).
SQ SEQUENCE 189 AA; 21493 MW; F4E57E500CB7C831 CRC64;
MSAAMRERFD RFLHEKNCMT DLLAKLEAKT GVNRSFIALG VIGLVALYLV FGYGASLLCN
LIGFGYPAYI SIKAIESPNK EDDTQWLTYW VVYGVFSIAE FFSDIFLSWF PFYYMLKCGF
LLWCMAPSPS NGAELLYKRI IRPFFLKHES QMDSVVKDLK DKAKETADAI TKEAKKATVN
LLGEEKKST
//
MIM
125265
*RECORD*
*FIELD* NO
125265
*FIELD* TI
*125265 RECEPTOR EXPRESSION-ENHANCING PROTEIN 5; REEP5
;;DELETED IN POLYPOSIS 1; DP1;;
read moreTB2;;
D5S346;;
YOP1, S. CEREVISIAE, HOMOLOG OF; YOP1;;
CHROMOSOME 5 OPEN READING FRAME 18; C5ORF18
*FIELD* TX
CLONING
Through study of submicroscopic deletions in 2 unrelated patients with
familial adenomatous polyposis coli (FAP; 175100), Joslyn et al. (1991)
found 3 genes in a 100-kb deleted segment on chromosome 5. MCC (159350),
a previous candidate gene, was shown to be located outside the deleted
region. One of the new genes contained a sequence identical to SRP19
(182175). The second gene, provisionally designated DP1, was transcribed
in the same orientation as MCC. Two other cDNAs, DP2 and DP3, were found
to overlap, forming a single gene, DP2.5, which was transcribed in the
same orientation as SRP19. The DP2.5 gene was shown by Groden et al.
(1991) to be the polyposis gene, as indicated in 611731.
Transport of G protein-coupled receptors (GPCRs) to the cell surface
membrane is critical for receptor-ligand recognition. However, mammalian
GPCR odorant receptors (ORs), when heterologously expressed in cells,
are poorly expressed on the cell surface. By screening for genes that
induced cell surface expression of ORs expressed in human embryonic
kidney cells, Saito et al. (2004) identified mouse and human REEP1
(609139). They searched databases for homologs of REEP1 and identified
several other REEP genes, including DP1, which they called REEP5. In
situ hybridization of mouse olfactory epithelium revealed that, unlike
Reep1, Reep5 was not expressed in olfactory neurons.
GENE FUNCTION
Using an in vitro system to identify Xenopus membrane proteins involved
in endoplasmic reticulum (ER) network formation, followed by
localization, overexpression, and deletion experiments in mammalian and
yeast cells, Voeltz et al. (2006) identified the reticulons,
particularly Rtn4a/NogoA (604475), and the reticulon-interacting protein
DP1/Yop1 as the major components shaping the tubular ER.
MAPPING
Joslyn et al. (1991) identified the DP1 gene in a 100-kb segment on
chromosome 5 deleted in 2 patients with APC.
*FIELD* RF
1. Groden, J.; Thliveris, A.; Samowitz, W.; Carlson, M.; Gelbert,
L.; Albertsen, H.; Joslyn, G.; Stevens, J.; Spirio, L.; Robertson,
M.; Sargeant, L.; Krapcho, K.; Wolff, E.; Burt, R.; Hughes, J. P.;
Warrington, J.; McPherson, J.; Wasmuth, J.; Le Paslier, D.; Abderrahim,
H.; Cohen, D.; Leppert, M.; White, R.: Identification and characterization
of the familial adenomatous polyposis coli gene. Cell 66: 589-600,
1991.
2. Joslyn, G.; Carlson, M.; Thliveris, A.; Albertsen, H.; Gelbert,
L.; Samowitz, W.; Groden, J.; Stevens, J.; Spirio, L.; Robertson,
M.; Sargeant, L.; Krapcho, K.; Wolff, E.; Burt, R.; Hughes, J. P.;
Warrington, J.; McPherson, J.; Wasmuth, J.; Le Paslier, D.; Abderrahim,
H.; Cohen, D.; Leppert, M.; White, R.: Identification of deletion
mutations and three new genes at the familial polyposis locus. Cell 66:
601-613, 1991.
3. Saito, H.; Kubota, M.; Roberts, R. W.; Chi, Q.; Matsunami, H.:
RTP family members induce functional expression of mammalian odorant
receptors. Cell 119: 679-691, 2004.
4. Voeltz, G. K.; Prinz, W. A.; Shibata, Y.; Rist, J. M.; Rapoport,
T. A.: A class of membrane proteins shaping the tubular endoplasmic
reticulum. Cell 573-586, 2006.
*FIELD* CN
Matthew B. Gross - updated: 5/21/2009
Matthew B. Gross - updated: 4/29/2005
*FIELD* CD
Victor A. McKusick: 9/30/1991
*FIELD* ED
alopez: 12/02/2010
wwang: 5/28/2009
mgross: 5/21/2009
mgross: 2/4/2009
ckniffin: 2/5/2008
alopez: 2/16/2006
mgross: 4/29/2005
carol: 3/14/2000
mimadm: 6/25/1994
supermim: 3/16/1992
carol: 2/27/1992
carol: 9/30/1991
*RECORD*
*FIELD* NO
125265
*FIELD* TI
*125265 RECEPTOR EXPRESSION-ENHANCING PROTEIN 5; REEP5
;;DELETED IN POLYPOSIS 1; DP1;;
read moreTB2;;
D5S346;;
YOP1, S. CEREVISIAE, HOMOLOG OF; YOP1;;
CHROMOSOME 5 OPEN READING FRAME 18; C5ORF18
*FIELD* TX
CLONING
Through study of submicroscopic deletions in 2 unrelated patients with
familial adenomatous polyposis coli (FAP; 175100), Joslyn et al. (1991)
found 3 genes in a 100-kb deleted segment on chromosome 5. MCC (159350),
a previous candidate gene, was shown to be located outside the deleted
region. One of the new genes contained a sequence identical to SRP19
(182175). The second gene, provisionally designated DP1, was transcribed
in the same orientation as MCC. Two other cDNAs, DP2 and DP3, were found
to overlap, forming a single gene, DP2.5, which was transcribed in the
same orientation as SRP19. The DP2.5 gene was shown by Groden et al.
(1991) to be the polyposis gene, as indicated in 611731.
Transport of G protein-coupled receptors (GPCRs) to the cell surface
membrane is critical for receptor-ligand recognition. However, mammalian
GPCR odorant receptors (ORs), when heterologously expressed in cells,
are poorly expressed on the cell surface. By screening for genes that
induced cell surface expression of ORs expressed in human embryonic
kidney cells, Saito et al. (2004) identified mouse and human REEP1
(609139). They searched databases for homologs of REEP1 and identified
several other REEP genes, including DP1, which they called REEP5. In
situ hybridization of mouse olfactory epithelium revealed that, unlike
Reep1, Reep5 was not expressed in olfactory neurons.
GENE FUNCTION
Using an in vitro system to identify Xenopus membrane proteins involved
in endoplasmic reticulum (ER) network formation, followed by
localization, overexpression, and deletion experiments in mammalian and
yeast cells, Voeltz et al. (2006) identified the reticulons,
particularly Rtn4a/NogoA (604475), and the reticulon-interacting protein
DP1/Yop1 as the major components shaping the tubular ER.
MAPPING
Joslyn et al. (1991) identified the DP1 gene in a 100-kb segment on
chromosome 5 deleted in 2 patients with APC.
*FIELD* RF
1. Groden, J.; Thliveris, A.; Samowitz, W.; Carlson, M.; Gelbert,
L.; Albertsen, H.; Joslyn, G.; Stevens, J.; Spirio, L.; Robertson,
M.; Sargeant, L.; Krapcho, K.; Wolff, E.; Burt, R.; Hughes, J. P.;
Warrington, J.; McPherson, J.; Wasmuth, J.; Le Paslier, D.; Abderrahim,
H.; Cohen, D.; Leppert, M.; White, R.: Identification and characterization
of the familial adenomatous polyposis coli gene. Cell 66: 589-600,
1991.
2. Joslyn, G.; Carlson, M.; Thliveris, A.; Albertsen, H.; Gelbert,
L.; Samowitz, W.; Groden, J.; Stevens, J.; Spirio, L.; Robertson,
M.; Sargeant, L.; Krapcho, K.; Wolff, E.; Burt, R.; Hughes, J. P.;
Warrington, J.; McPherson, J.; Wasmuth, J.; Le Paslier, D.; Abderrahim,
H.; Cohen, D.; Leppert, M.; White, R.: Identification of deletion
mutations and three new genes at the familial polyposis locus. Cell 66:
601-613, 1991.
3. Saito, H.; Kubota, M.; Roberts, R. W.; Chi, Q.; Matsunami, H.:
RTP family members induce functional expression of mammalian odorant
receptors. Cell 119: 679-691, 2004.
4. Voeltz, G. K.; Prinz, W. A.; Shibata, Y.; Rist, J. M.; Rapoport,
T. A.: A class of membrane proteins shaping the tubular endoplasmic
reticulum. Cell 573-586, 2006.
*FIELD* CN
Matthew B. Gross - updated: 5/21/2009
Matthew B. Gross - updated: 4/29/2005
*FIELD* CD
Victor A. McKusick: 9/30/1991
*FIELD* ED
alopez: 12/02/2010
wwang: 5/28/2009
mgross: 5/21/2009
mgross: 2/4/2009
ckniffin: 2/5/2008
alopez: 2/16/2006
mgross: 4/29/2005
carol: 3/14/2000
mimadm: 6/25/1994
supermim: 3/16/1992
carol: 2/27/1992
carol: 9/30/1991