Full text data of VPS29
VPS29
[Confidence: low (only semi-automatic identification from reviews)]
Vacuolar protein sorting-associated protein 29; hVPS29; 3.1.3.3 (PEP11 homolog; Vesicle protein sorting 29)
Vacuolar protein sorting-associated protein 29; hVPS29; 3.1.3.3 (PEP11 homolog; Vesicle protein sorting 29)
UniProt
Q9UBQ0
ID VPS29_HUMAN Reviewed; 182 AA.
AC Q9UBQ0; Q502Y5; Q6FIF8; Q6IAH3; Q9H0W0; Q9NRP1; Q9NRU7;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Vacuolar protein sorting-associated protein 29;
DE Short=hVPS29;
DE EC=3.1.3.3;
DE AltName: Full=PEP11 homolog;
DE AltName: Full=Vesicle protein sorting 29;
GN Name=VPS29; ORFNames=DC15, DC7, MDS007;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
RX PubMed=11062004; DOI=10.1006/bbrc.2000.3727;
RA Edgar A.J., Polak J.M.;
RT "Human homologues of yeast vacuolar protein sorting 29 and 35.";
RL Biochem. Biophys. Res. Commun. 277:622-630(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH VPS26A;
RP VPS35; SNX1 AND SNX2.
RC TISSUE=Parathyroid;
RX PubMed=11102511; DOI=10.1091/mbc.11.12.4105;
RA Renfrew Haft C., de la Luz Sierra M., Bafford R., Lesniak M.A.,
RA Barr V.A., Taylor S.I.;
RT "Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29,
RT and 35: assembly into multimeric complexes.";
RL Mol. Biol. Cell 11:4105-4116(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J.,
RA Gu J., Huang Q., Yu Y., Xu S., Ren S., Fu G., Li N.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Cervix;
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 [8]
RP IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS35
RP AND SFN.
RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT "Exportin 7 defines a novel general nuclear export pathway.";
RL EMBO J. 23:3227-3236(2004).
RN [9]
RP FUNCTION.
RX PubMed=15247922; DOI=10.1038/ncb1153;
RA Verges M., Luton F., Gruber C., Tiemann F., Reinders L.G., Huang L.,
RA Burlingame A.L., Haft C.R., Mostov K.E.;
RT "The mammalian retromer regulates transcytosis of the polymeric
RT immunoglobulin receptor.";
RL Nat. Cell Biol. 6:763-769(2004).
RN [10]
RP CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF ASP-8; ASN-39; ASP-62;
RP HIS-86 AND HIS-117, AND SUBUNIT.
RX PubMed=16737443; DOI=10.1042/BJ20060033;
RA Damen E., Krieger E., Nielsen J.E., Eygensteyn J., van Leeuwen J.E.M.;
RT "The human Vps29 retromer component is a metallo-phosphoesterase for a
RT cation-independent mannose 6-phosphate receptor substrate peptide.";
RL Biochem. J. 398:399-409(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND MASS 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 [12]
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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND METAL-BINDING.
RX PubMed=15788412; DOI=10.1074/jbc.M500464200;
RA Wang D., Guo M., Liang Z., Fan J., Zhu Z., Zang J., Zhu Z., Li X.,
RA Teng M., Niu L., Dong Y., Liu P.;
RT "Crystal structure of human vacuolar protein sorting protein 29
RT reveals a phosphodiesterase/nuclease-like fold and two protein-protein
RT interaction sites.";
RL J. Biol. Chem. 280:22962-22967(2005).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH VPS35, AND
RP ELECTRON MICROSCOPY OF THE RETROMER COMPLEX CONTAINING VPS29; VPS35
RP AND VPS26.
RX PubMed=17891154; DOI=10.1038/nature06216;
RA Hierro A., Rojas A.L., Rojas R., Murthy N., Effantin G., Kajava A.V.,
RA Steven A.C., Bonifacino J.S., Hurley J.H.;
RT "Functional architecture of the retromer cargo-recognition complex.";
RL Nature 449:1063-1067(2007).
CC -!- FUNCTION: Essential component of the retromer complex, a complex
CC required to retrieve lysosomal enzyme receptors (IGF2R and M6PR)
CC from endosomes to the trans-Golgi network. Also required to
CC regulate transcytosis of the polymeric immunoglobulin receptor
CC (pIgR-pIgA). Has low protein phosphatase activity towards a
CC serine-phosphorylated peptide derived from IGF2R (in vitro).
CC -!- CATALYTIC ACTIVITY: O-phospho-L(or D)-serine + H(2)O = L(or D)-
CC serine + phosphate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit (Probable).
CC -!- SUBUNIT: Component of the retromer complex composed of VPS26
CC (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Found in a
CC complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein. Endosome membrane; Peripheral membrane protein (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBQ0-2; Sequence=VSP_004073;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, lung,
CC placenta, spleen, peripheral blood leukocytes, thymus, colon
CC skeletal muscle, kidney and brain.
CC -!- SIMILARITY: Belongs to the VPS29 family.
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; AF193795; AAF04596.1; -; mRNA.
DR EMBL; AF175264; AAF89952.1; -; mRNA.
DR EMBL; AF168716; AAF87318.1; -; mRNA.
DR EMBL; AF201936; AAF86872.1; -; mRNA.
DR EMBL; AF201946; AAF17238.1; -; mRNA.
DR EMBL; AL136614; CAB66549.1; -; mRNA.
DR EMBL; CR457182; CAG33463.1; -; mRNA.
DR EMBL; CR533468; CAG38499.1; -; mRNA.
DR EMBL; BC000880; AAH00880.1; -; mRNA.
DR EMBL; BC095446; AAH95446.1; -; mRNA.
DR PIR; JC7515; JC7515.
DR RefSeq; NP_057310.1; NM_016226.4.
DR RefSeq; NP_476528.1; NM_057180.2.
DR UniGene; Hs.600114; -.
DR PDB; 1W24; X-ray; 2.10 A; A=1-182.
DR PDB; 2R17; X-ray; 2.80 A; A/B=1-182.
DR PDBsum; 1W24; -.
DR PDBsum; 2R17; -.
DR ProteinModelPortal; Q9UBQ0; -.
DR SMR; Q9UBQ0; 1-181.
DR DIP; DIP-29077N; -.
DR IntAct; Q9UBQ0; 3.
DR MINT; MINT-1422473; -.
DR STRING; 9606.ENSP00000380795; -.
DR PhosphoSite; Q9UBQ0; -.
DR DMDM; 25453325; -.
DR PaxDb; Q9UBQ0; -.
DR PRIDE; Q9UBQ0; -.
DR DNASU; 51699; -.
DR Ensembl; ENST00000360579; ENSP00000353786; ENSG00000111237.
DR Ensembl; ENST00000549578; ENSP00000447058; ENSG00000111237.
DR GeneID; 51699; -.
DR KEGG; hsa:51699; -.
DR UCSC; uc001tqy.3; human.
DR CTD; 51699; -.
DR GeneCards; GC12M110929; -.
DR HGNC; HGNC:14340; VPS29.
DR HPA; HPA039748; -.
DR MIM; 606932; gene.
DR neXtProt; NX_Q9UBQ0; -.
DR PharmGKB; PA37875; -.
DR eggNOG; COG0622; -.
DR HOVERGEN; HBG056165; -.
DR KO; K07095; -.
DR OrthoDB; EOG7JHM6S; -.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; Q9UBQ0; -.
DR GeneWiki; VPS29; -.
DR GenomeRNAi; 51699; -.
DR NextBio; 55714; -.
DR PRO; PR:Q9UBQ0; -.
DR ArrayExpress; Q9UBQ0; -.
DR Bgee; Q9UBQ0; -.
DR CleanEx; HS_VPS29; -.
DR Genevestigator; Q9UBQ0; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:LIFEdb.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004647; F:phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR024654; Calcineurin-like_PEstase_dom.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR PANTHER; PTHR11124; PTHR11124; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR TIGRFAMs; TIGR00040; yfcE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Endosome; Hydrolase; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1 182 Vacuolar protein sorting-associated
FT protein 29.
FT /FTId=PRO_0000065894.
FT METAL 8 8 Zinc 1 (By similarity).
FT METAL 10 10 Zinc 1 (By similarity).
FT METAL 39 39 Zinc 1 (By similarity).
FT METAL 39 39 Zinc 2 (By similarity).
FT METAL 62 62 Zinc 2 (By similarity).
FT METAL 86 86 Zinc 2 (By similarity).
FT METAL 115 115 Zinc 2 (By similarity).
FT METAL 117 117 Zinc 1 (By similarity).
FT MOD_RES 50 50 N6-acetyllysine.
FT VAR_SEQ 1 1 M -> MAGHR (in isoform 2).
FT /FTId=VSP_004073.
FT MUTAGEN 8 8 D->A: Loss of protein phosphatase
FT activity.
FT MUTAGEN 39 39 N->A: Loss of protein phosphatase
FT activity.
FT MUTAGEN 39 39 N->D: No effect on protein phosphatase
FT activity.
FT MUTAGEN 62 62 D->A,N: Loss of protein phosphatase
FT activity.
FT MUTAGEN 86 86 H->A: Loss of protein phosphatase
FT activity.
FT MUTAGEN 117 117 H->A: Loss of protein phosphatase
FT activity.
FT CONFLICT 1 2 ML -> MKIVLYPV (in Ref. 4; AAF86872).
FT CONFLICT 119 119 F -> S (in Ref. 5; CAB66549 and 6;
FT CAG38499).
FT STRAND 2 6
FT TURN 11 14
FT STRAND 16 18
FT HELIX 20 25
FT STRAND 32 36
FT HELIX 43 52
FT STRAND 54 58
FT STRAND 71 77
FT STRAND 80 85
FT STRAND 90 92
FT HELIX 96 106
FT STRAND 109 113
FT STRAND 115 118
FT STRAND 120 124
FT STRAND 127 131
FT STRAND 149 156
FT STRAND 159 168
FT STRAND 171 180
SQ SEQUENCE 182 AA; 20506 MW; 6E0CDE6B720C9BF8 CRC64;
MLVLVLGDLH IPHRCNSLPA KFKKLLVPGK IQHILCTGNL CTKESYDYLK TLAGDVHIVR
GDFDENLNYP EQKVVTVGQF KIGLIHGHQV IPWGDMASLA LLQRQFDVDI LISGHTHKFE
AFEHENKFYI NPGSATGAYN ALETNIIPSF VLMDIQASTV VTYVYQLIGD DVKVERIEYK
KP
//
ID VPS29_HUMAN Reviewed; 182 AA.
AC Q9UBQ0; Q502Y5; Q6FIF8; Q6IAH3; Q9H0W0; Q9NRP1; Q9NRU7;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Vacuolar protein sorting-associated protein 29;
DE Short=hVPS29;
DE EC=3.1.3.3;
DE AltName: Full=PEP11 homolog;
DE AltName: Full=Vesicle protein sorting 29;
GN Name=VPS29; ORFNames=DC15, DC7, MDS007;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
RX PubMed=11062004; DOI=10.1006/bbrc.2000.3727;
RA Edgar A.J., Polak J.M.;
RT "Human homologues of yeast vacuolar protein sorting 29 and 35.";
RL Biochem. Biophys. Res. Commun. 277:622-630(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH VPS26A;
RP VPS35; SNX1 AND SNX2.
RC TISSUE=Parathyroid;
RX PubMed=11102511; DOI=10.1091/mbc.11.12.4105;
RA Renfrew Haft C., de la Luz Sierra M., Bafford R., Lesniak M.A.,
RA Barr V.A., Taylor S.I.;
RT "Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29,
RT and 35: assembly into multimeric complexes.";
RL Mol. Biol. Cell 11:4105-4116(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J.,
RA Gu J., Huang Q., Yu Y., Xu S., Ren S., Fu G., Li N.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Cervix;
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 [8]
RP IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS35
RP AND SFN.
RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT "Exportin 7 defines a novel general nuclear export pathway.";
RL EMBO J. 23:3227-3236(2004).
RN [9]
RP FUNCTION.
RX PubMed=15247922; DOI=10.1038/ncb1153;
RA Verges M., Luton F., Gruber C., Tiemann F., Reinders L.G., Huang L.,
RA Burlingame A.L., Haft C.R., Mostov K.E.;
RT "The mammalian retromer regulates transcytosis of the polymeric
RT immunoglobulin receptor.";
RL Nat. Cell Biol. 6:763-769(2004).
RN [10]
RP CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF ASP-8; ASN-39; ASP-62;
RP HIS-86 AND HIS-117, AND SUBUNIT.
RX PubMed=16737443; DOI=10.1042/BJ20060033;
RA Damen E., Krieger E., Nielsen J.E., Eygensteyn J., van Leeuwen J.E.M.;
RT "The human Vps29 retromer component is a metallo-phosphoesterase for a
RT cation-independent mannose 6-phosphate receptor substrate peptide.";
RL Biochem. J. 398:399-409(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND MASS 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 [12]
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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND METAL-BINDING.
RX PubMed=15788412; DOI=10.1074/jbc.M500464200;
RA Wang D., Guo M., Liang Z., Fan J., Zhu Z., Zang J., Zhu Z., Li X.,
RA Teng M., Niu L., Dong Y., Liu P.;
RT "Crystal structure of human vacuolar protein sorting protein 29
RT reveals a phosphodiesterase/nuclease-like fold and two protein-protein
RT interaction sites.";
RL J. Biol. Chem. 280:22962-22967(2005).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH VPS35, AND
RP ELECTRON MICROSCOPY OF THE RETROMER COMPLEX CONTAINING VPS29; VPS35
RP AND VPS26.
RX PubMed=17891154; DOI=10.1038/nature06216;
RA Hierro A., Rojas A.L., Rojas R., Murthy N., Effantin G., Kajava A.V.,
RA Steven A.C., Bonifacino J.S., Hurley J.H.;
RT "Functional architecture of the retromer cargo-recognition complex.";
RL Nature 449:1063-1067(2007).
CC -!- FUNCTION: Essential component of the retromer complex, a complex
CC required to retrieve lysosomal enzyme receptors (IGF2R and M6PR)
CC from endosomes to the trans-Golgi network. Also required to
CC regulate transcytosis of the polymeric immunoglobulin receptor
CC (pIgR-pIgA). Has low protein phosphatase activity towards a
CC serine-phosphorylated peptide derived from IGF2R (in vitro).
CC -!- CATALYTIC ACTIVITY: O-phospho-L(or D)-serine + H(2)O = L(or D)-
CC serine + phosphate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit (Probable).
CC -!- SUBUNIT: Component of the retromer complex composed of VPS26
CC (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Found in a
CC complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein. Endosome membrane; Peripheral membrane protein (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBQ0-2; Sequence=VSP_004073;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, lung,
CC placenta, spleen, peripheral blood leukocytes, thymus, colon
CC skeletal muscle, kidney and brain.
CC -!- SIMILARITY: Belongs to the VPS29 family.
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; AF193795; AAF04596.1; -; mRNA.
DR EMBL; AF175264; AAF89952.1; -; mRNA.
DR EMBL; AF168716; AAF87318.1; -; mRNA.
DR EMBL; AF201936; AAF86872.1; -; mRNA.
DR EMBL; AF201946; AAF17238.1; -; mRNA.
DR EMBL; AL136614; CAB66549.1; -; mRNA.
DR EMBL; CR457182; CAG33463.1; -; mRNA.
DR EMBL; CR533468; CAG38499.1; -; mRNA.
DR EMBL; BC000880; AAH00880.1; -; mRNA.
DR EMBL; BC095446; AAH95446.1; -; mRNA.
DR PIR; JC7515; JC7515.
DR RefSeq; NP_057310.1; NM_016226.4.
DR RefSeq; NP_476528.1; NM_057180.2.
DR UniGene; Hs.600114; -.
DR PDB; 1W24; X-ray; 2.10 A; A=1-182.
DR PDB; 2R17; X-ray; 2.80 A; A/B=1-182.
DR PDBsum; 1W24; -.
DR PDBsum; 2R17; -.
DR ProteinModelPortal; Q9UBQ0; -.
DR SMR; Q9UBQ0; 1-181.
DR DIP; DIP-29077N; -.
DR IntAct; Q9UBQ0; 3.
DR MINT; MINT-1422473; -.
DR STRING; 9606.ENSP00000380795; -.
DR PhosphoSite; Q9UBQ0; -.
DR DMDM; 25453325; -.
DR PaxDb; Q9UBQ0; -.
DR PRIDE; Q9UBQ0; -.
DR DNASU; 51699; -.
DR Ensembl; ENST00000360579; ENSP00000353786; ENSG00000111237.
DR Ensembl; ENST00000549578; ENSP00000447058; ENSG00000111237.
DR GeneID; 51699; -.
DR KEGG; hsa:51699; -.
DR UCSC; uc001tqy.3; human.
DR CTD; 51699; -.
DR GeneCards; GC12M110929; -.
DR HGNC; HGNC:14340; VPS29.
DR HPA; HPA039748; -.
DR MIM; 606932; gene.
DR neXtProt; NX_Q9UBQ0; -.
DR PharmGKB; PA37875; -.
DR eggNOG; COG0622; -.
DR HOVERGEN; HBG056165; -.
DR KO; K07095; -.
DR OrthoDB; EOG7JHM6S; -.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; Q9UBQ0; -.
DR GeneWiki; VPS29; -.
DR GenomeRNAi; 51699; -.
DR NextBio; 55714; -.
DR PRO; PR:Q9UBQ0; -.
DR ArrayExpress; Q9UBQ0; -.
DR Bgee; Q9UBQ0; -.
DR CleanEx; HS_VPS29; -.
DR Genevestigator; Q9UBQ0; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:LIFEdb.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004647; F:phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR024654; Calcineurin-like_PEstase_dom.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR PANTHER; PTHR11124; PTHR11124; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR TIGRFAMs; TIGR00040; yfcE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Endosome; Hydrolase; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1 182 Vacuolar protein sorting-associated
FT protein 29.
FT /FTId=PRO_0000065894.
FT METAL 8 8 Zinc 1 (By similarity).
FT METAL 10 10 Zinc 1 (By similarity).
FT METAL 39 39 Zinc 1 (By similarity).
FT METAL 39 39 Zinc 2 (By similarity).
FT METAL 62 62 Zinc 2 (By similarity).
FT METAL 86 86 Zinc 2 (By similarity).
FT METAL 115 115 Zinc 2 (By similarity).
FT METAL 117 117 Zinc 1 (By similarity).
FT MOD_RES 50 50 N6-acetyllysine.
FT VAR_SEQ 1 1 M -> MAGHR (in isoform 2).
FT /FTId=VSP_004073.
FT MUTAGEN 8 8 D->A: Loss of protein phosphatase
FT activity.
FT MUTAGEN 39 39 N->A: Loss of protein phosphatase
FT activity.
FT MUTAGEN 39 39 N->D: No effect on protein phosphatase
FT activity.
FT MUTAGEN 62 62 D->A,N: Loss of protein phosphatase
FT activity.
FT MUTAGEN 86 86 H->A: Loss of protein phosphatase
FT activity.
FT MUTAGEN 117 117 H->A: Loss of protein phosphatase
FT activity.
FT CONFLICT 1 2 ML -> MKIVLYPV (in Ref. 4; AAF86872).
FT CONFLICT 119 119 F -> S (in Ref. 5; CAB66549 and 6;
FT CAG38499).
FT STRAND 2 6
FT TURN 11 14
FT STRAND 16 18
FT HELIX 20 25
FT STRAND 32 36
FT HELIX 43 52
FT STRAND 54 58
FT STRAND 71 77
FT STRAND 80 85
FT STRAND 90 92
FT HELIX 96 106
FT STRAND 109 113
FT STRAND 115 118
FT STRAND 120 124
FT STRAND 127 131
FT STRAND 149 156
FT STRAND 159 168
FT STRAND 171 180
SQ SEQUENCE 182 AA; 20506 MW; 6E0CDE6B720C9BF8 CRC64;
MLVLVLGDLH IPHRCNSLPA KFKKLLVPGK IQHILCTGNL CTKESYDYLK TLAGDVHIVR
GDFDENLNYP EQKVVTVGQF KIGLIHGHQV IPWGDMASLA LLQRQFDVDI LISGHTHKFE
AFEHENKFYI NPGSATGAYN ALETNIIPSF VLMDIQASTV VTYVYQLIGD DVKVERIEYK
KP
//
MIM
606932
*RECORD*
*FIELD* NO
606932
*FIELD* TI
*606932 VACUOLAR PROTEIN SORTING 29, YEAST, HOMOLOG OF; VPS29
;;RETROMER PROTEIN;;
read morePEP11;;
DC7;;
DC15
*FIELD* TX
DESCRIPTION
The maintenance of organelles in eukaryotic cells depends on sorting
proteins, which ensure the proper delivery of organelle-specific
proteins. VPS29 is one of several sorting proteins in the yeast S.
cerevisiae that is required for vacuolar/late endosome to Golgi
retrieval of the vacuolar hydrolase receptor, suggesting that human
VPS29 may have an analogous function in the maintenance of lysosomes.
CLONING
Edgar and Polak (2000) used sequences from S. cerevisiae to search an
EST database for homologous human sequences. Sequences obtained from
this search were used to develop primers to clone VPS29 by PCR from a
human lung cDNA library. The deduced 20.5-kD VPS29 protein is
hydrophilic and has a predicted mixed alpha-helix and beta-sheet
structure. It has 2 polyadenylation signals and a charged C terminus
containing the conserved NPGS amino acid motif. Northern blot analysis
detected 2 transcripts of 0.8 and 2 kb corresponding to the 2
polyadenylation signals. The longer transcript was more abundant,
showing highest expression in heart, skeletal muscle, and kidney,
intermediate expression in brain, colon, and liver, and lowest
expression in thymus, spleen, small intestine, placenta, lung, and
leukocytes. Edgar and Polak (2000) also cloned mouse Vps29 by PCR from a
mouse lung cDNA library. The mouse protein is identical to the human
protein except for a C-terminal serine.
GENE FUNCTION
Haft et al. (2000) used yeast 2-hybrid assays, mutation analysis, and
expression in mammalian cells to define the binding interactions among
VPS29 and other human orthologs of yeast vacuolar protein sorting
proteins, VPS26 (605506), SNX1 (601272), and VPS35 (601501). Their
results are consistent with a model in which VPS29 is bound to VPS35 in
a multimeric complex. Haft et al. (2000) identified a discrete domain
within VPS35 that interacts with VPS29. Gel filtration chromatography of
COS-7 cells showed that both recombinant and endogenous VPS proteins
coelute as a 220- to 240-kD complex, and in the absence of VPS35,
neither VPS26 nor VPS29 is found in the complex.
GENE STRUCTURE
Edgar and Polak (2000) determined that the VPS29 gene is present in the
human genome in single copy, contains 5 exons, and spans 10.5 kb. They
also identified an upstream CpG island and a potential TATA box.
BIOCHEMICAL FEATURES
- Crystal Structure
Hierro et al. (2007) reported the crystal structure of a VPS29-VPS35
subcomplex showing how the metallophosphoesterase-fold subunit VPS29
acts as a scaffold for the C-terminal half of VPS35. VPS35 forms a
horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face
of which completely covers the metal-binding site of VPS29, whereas the
convex face exposes a series of hydrophobic interhelical grooves.
Electron microscopy showed that the intact VPS26-VPS29-VPS35 complex is
a stick-shaped, flexible structure, approximately 21 nanometers long. A
hybrid structural model derived from crystal structures, electron
microscopy, interaction studies, and bioinformatics showed that the
alpha-solenoid fold extends the full length of VPS35, and that VPS26 is
bound at the opposite end from VPS29. This extended structure presents
multiple binding sites for the SNX complex and receptor cargo, and
appears capable of flexing to conform to curved vesicular membranes.
MAPPING
Edgar and Polak (2000) mapped the VPS29 gene to chromosome 12q24 based
on sequence similarity between the VPS29 gene and a genomic clone mapped
to 12q24.
*FIELD* RF
1. Edgar, A. J.; Polak, J. M.: Human homologues of yeast vacuolar
protein sorting 29 and 35. Biochem. Biophys. Res. Commun. 277: 622-630,
2000.
2. Haft, C. R.; de la Luz Sierra, M.; Bafford, R.; Lesniak, M. A.;
Barr, V. A.; Taylor, S. I.: Human orthologs of yeast vacuolar protein
sorting proteins Vps26, 29, and 35: assembly into multimeric complexes. Molec.
Biol. Cell 11: 4105-4116, 2000.
3. Hierro, A.; Rojas, A. L.; Rojas, R.; Murthy, N.; Effantin, G.;
Kajava, A. V.; Steven, A. C.; Bonifacino, J. S.; Hurley, J. H.: Functional
architecture of the retromer cargo-recognition complex. Nature 449:
1063-1067, 2007.
*FIELD* CN
Ada Hamosh - updated: 11/12/2007
*FIELD* CD
Patricia A. Hartz: 5/10/2002
*FIELD* ED
terry: 09/08/2010
alopez: 11/14/2007
terry: 11/12/2007
mgross: 3/25/2004
alopez: 5/14/2002
alopez: 5/13/2002
alopez: 5/10/2002
*RECORD*
*FIELD* NO
606932
*FIELD* TI
*606932 VACUOLAR PROTEIN SORTING 29, YEAST, HOMOLOG OF; VPS29
;;RETROMER PROTEIN;;
read morePEP11;;
DC7;;
DC15
*FIELD* TX
DESCRIPTION
The maintenance of organelles in eukaryotic cells depends on sorting
proteins, which ensure the proper delivery of organelle-specific
proteins. VPS29 is one of several sorting proteins in the yeast S.
cerevisiae that is required for vacuolar/late endosome to Golgi
retrieval of the vacuolar hydrolase receptor, suggesting that human
VPS29 may have an analogous function in the maintenance of lysosomes.
CLONING
Edgar and Polak (2000) used sequences from S. cerevisiae to search an
EST database for homologous human sequences. Sequences obtained from
this search were used to develop primers to clone VPS29 by PCR from a
human lung cDNA library. The deduced 20.5-kD VPS29 protein is
hydrophilic and has a predicted mixed alpha-helix and beta-sheet
structure. It has 2 polyadenylation signals and a charged C terminus
containing the conserved NPGS amino acid motif. Northern blot analysis
detected 2 transcripts of 0.8 and 2 kb corresponding to the 2
polyadenylation signals. The longer transcript was more abundant,
showing highest expression in heart, skeletal muscle, and kidney,
intermediate expression in brain, colon, and liver, and lowest
expression in thymus, spleen, small intestine, placenta, lung, and
leukocytes. Edgar and Polak (2000) also cloned mouse Vps29 by PCR from a
mouse lung cDNA library. The mouse protein is identical to the human
protein except for a C-terminal serine.
GENE FUNCTION
Haft et al. (2000) used yeast 2-hybrid assays, mutation analysis, and
expression in mammalian cells to define the binding interactions among
VPS29 and other human orthologs of yeast vacuolar protein sorting
proteins, VPS26 (605506), SNX1 (601272), and VPS35 (601501). Their
results are consistent with a model in which VPS29 is bound to VPS35 in
a multimeric complex. Haft et al. (2000) identified a discrete domain
within VPS35 that interacts with VPS29. Gel filtration chromatography of
COS-7 cells showed that both recombinant and endogenous VPS proteins
coelute as a 220- to 240-kD complex, and in the absence of VPS35,
neither VPS26 nor VPS29 is found in the complex.
GENE STRUCTURE
Edgar and Polak (2000) determined that the VPS29 gene is present in the
human genome in single copy, contains 5 exons, and spans 10.5 kb. They
also identified an upstream CpG island and a potential TATA box.
BIOCHEMICAL FEATURES
- Crystal Structure
Hierro et al. (2007) reported the crystal structure of a VPS29-VPS35
subcomplex showing how the metallophosphoesterase-fold subunit VPS29
acts as a scaffold for the C-terminal half of VPS35. VPS35 forms a
horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face
of which completely covers the metal-binding site of VPS29, whereas the
convex face exposes a series of hydrophobic interhelical grooves.
Electron microscopy showed that the intact VPS26-VPS29-VPS35 complex is
a stick-shaped, flexible structure, approximately 21 nanometers long. A
hybrid structural model derived from crystal structures, electron
microscopy, interaction studies, and bioinformatics showed that the
alpha-solenoid fold extends the full length of VPS35, and that VPS26 is
bound at the opposite end from VPS29. This extended structure presents
multiple binding sites for the SNX complex and receptor cargo, and
appears capable of flexing to conform to curved vesicular membranes.
MAPPING
Edgar and Polak (2000) mapped the VPS29 gene to chromosome 12q24 based
on sequence similarity between the VPS29 gene and a genomic clone mapped
to 12q24.
*FIELD* RF
1. Edgar, A. J.; Polak, J. M.: Human homologues of yeast vacuolar
protein sorting 29 and 35. Biochem. Biophys. Res. Commun. 277: 622-630,
2000.
2. Haft, C. R.; de la Luz Sierra, M.; Bafford, R.; Lesniak, M. A.;
Barr, V. A.; Taylor, S. I.: Human orthologs of yeast vacuolar protein
sorting proteins Vps26, 29, and 35: assembly into multimeric complexes. Molec.
Biol. Cell 11: 4105-4116, 2000.
3. Hierro, A.; Rojas, A. L.; Rojas, R.; Murthy, N.; Effantin, G.;
Kajava, A. V.; Steven, A. C.; Bonifacino, J. S.; Hurley, J. H.: Functional
architecture of the retromer cargo-recognition complex. Nature 449:
1063-1067, 2007.
*FIELD* CN
Ada Hamosh - updated: 11/12/2007
*FIELD* CD
Patricia A. Hartz: 5/10/2002
*FIELD* ED
terry: 09/08/2010
alopez: 11/14/2007
terry: 11/12/2007
mgross: 3/25/2004
alopez: 5/14/2002
alopez: 5/13/2002
alopez: 5/10/2002