VPS29_RAT
ID VPS29_RAT Reviewed; 182 AA.
AC B2RZ78; A6J1A4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Vacuolar protein sorting-associated protein 29 {ECO:0000250|UniProtKB:Q9UBQ0};
DE AltName: Full=Vesicle protein sorting 29 {ECO:0000250|UniProtKB:Q9UBQ0};
GN Name=Vps29 {ECO:0000312|EMBL:AAI67055.1, ECO:0000312|RGD:1308332};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI67055.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary {ECO:0000312|EMBL:AAI67055.1};
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).
RN [3] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 1).
RA Maurya D.K., Bhargava P.;
RL Submitted (DEC-2008) to UniProtKB.
CC -!- FUNCTION: Acts as component of the retromer cargo-selective complex
CC (CSC). The CSC is believed to be the core functional component of
CC retromer or respective retromer complex variants acting to prevent
CC missorting of selected transmembrane cargo proteins into the lysosomal
CC degradation pathway. The recruitment of the CSC to the endosomal
CC membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates
CC retrograde transport of cargo proteins from endosomes to the trans-
CC Golgi network (TGN) and is involved in endosome-to-plasma membrane
CC transport for cargo protein recycling. The SNX3-retromer mediates the
CC retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR
CC retromer pathway. The SNX27-retromer is believed to be involved in
CC endosome-to-plasma membrane trafficking and recycling of a broad
CC spectrum of cargo proteins. The CSC seems to act as recruitment hub for
CC other proteins, such as the WASH complex and TBC1D5. Required to
CC regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-
CC pIgA). Acts also as component of the retriever complex. The retriever
CC complex is a heterotrimeric complex related to retromer cargo-selective
CC complex (CSC) and essential for retromer-independent retrieval and
CC recycling of numerous cargos such as integrin alpha-5/beta-1
CC (ITGA5:ITGB1). In the endosomes, retriever complex drives the retrieval
CC and recycling of NxxY-motif-containing cargo proteins by coupling to
CC SNX17, a cargo essential for the homeostatic maintenance of numerous
CC cell surface proteins associated with processes that include cell
CC migration, cell adhesion, nutrient supply and cell signaling. The
CC recruitment of the retriever complex to the endosomal membrane involves
CC CCC and WASH complexes. Involved in GLUT1 endosome-to-plasma membrane
CC trafficking; the function is dependent of association with ANKRD27.
CC {ECO:0000250|UniProtKB:Q9QZ88, ECO:0000250|UniProtKB:Q9UBQ0}.
CC -!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective
CC complex (CSC), also described as vacuolar protein sorting subcomplex
CC (VPS), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35 (By
CC similarity). The CSC has a highly elongated structure with VPS26 and
CC VPS29 binding independently at opposite distal ends of VPS35 as central
CC platform (By similarity). The CSC is believed to associate with
CC variable sorting nexins to form functionally distinct retromer complex
CC variants. The originally described retromer complex (also called SNX-
CC BAR retromer) is a pentamer containing the CSC and a heterodimeric
CC membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or
CC SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR
CC subcomplexes associate with low affinity. The CSC associates with SNX3
CC to form a SNX3-retromer complex. The CSC associates with SNX27, the
CC WASH complex and the SNX-BAR subcomplex to form the SNX27-retromer
CC complex. Component of the heterotrimeric retriever complex formed by
CC VPS26C, VPS29 and VPS35L. Interacts with VPS35L (By similarity).
CC Interacts with VPS26A, VPS35, SNX1, SNX2, SNX27, WASHC5, TBC1D5 (By
CC similarity). Interacts with VPS26B and ANKRD27 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QZ88, ECO:0000250|UniProtKB:Q9UBQ0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Endosome membrane {ECO:0000250|UniProtKB:Q9QZ88}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9QZ88}. Early endosome {ECO:0000305}.
CC Late endosome {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B2RZ78-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=B2RZ78-2; Sequence=VSP_053030;
CC -!- SIMILARITY: Belongs to the VPS29 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH473973; EDM13693.1; -; Genomic_DNA.
DR EMBL; BC167055; AAI67055.1; -; mRNA.
DR RefSeq; NP_001099402.1; NM_001105932.1. [B2RZ78-1]
DR RefSeq; XP_006249424.1; XM_006249362.3. [B2RZ78-2]
DR AlphaFoldDB; B2RZ78; -.
DR SMR; B2RZ78; -.
DR BioGRID; 252647; 1.
DR IntAct; B2RZ78; 1.
DR STRING; 10116.ENSRNOP00000001717; -.
DR iPTMnet; B2RZ78; -.
DR PhosphoSitePlus; B2RZ78; -.
DR jPOST; B2RZ78; -.
DR PaxDb; B2RZ78; -.
DR PeptideAtlas; B2RZ78; -.
DR PRIDE; B2RZ78; -.
DR Ensembl; ENSRNOT00000088905; ENSRNOP00000074640; ENSRNOG00000001274. [B2RZ78-2]
DR GeneID; 288666; -.
DR KEGG; rno:288666; -.
DR UCSC; RGD:1308332; rat. [B2RZ78-1]
DR CTD; 51699; -.
DR RGD; 1308332; Vps29.
DR VEuPathDB; HostDB:ENSRNOG00000001274; -.
DR eggNOG; KOG3325; Eukaryota.
DR GeneTree; ENSGT00390000012669; -.
DR InParanoid; B2RZ78; -.
DR OrthoDB; 1233814at2759; -.
DR PhylomeDB; B2RZ78; -.
DR Reactome; R-RNO-3238698; WNT ligand biogenesis and trafficking.
DR PRO; PR:B2RZ78; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000001274; Expressed in Ammon's horn and 20 other tissues.
DR ExpressionAtlas; B2RZ78; baseline and differential.
DR Genevisible; B2RZ78; RN.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030904; C:retromer complex; ISS:UniProtKB.
DR GO; GO:0030906; C:retromer, cargo-selective complex; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR CDD; cd07394; MPP_Vps29; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR InterPro; IPR028661; Vps29.
DR PANTHER; PTHR11124; PTHR11124; 1.
DR PANTHER; PTHR11124:SF12; PTHR11124:SF12; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00040; yfcE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Endosome; Membrane;
KW Metal-binding; Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..182
FT /note="Vacuolar protein sorting-associated protein 29"
FT /id="PRO_0000365104"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ88"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ88"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ88"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ88"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ88"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ88"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ88"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ88"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ0"
FT VAR_SEQ 1
FT /note="M -> MAGHR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053030"
SQ SEQUENCE 182 AA; 20469 MW; CCDCC36B7B9EC64E CRC64;
MLVLVLGDLH IPHRCNSLPA KFKKLLVPGK IQHILCTGNL CTKESYDYLK TLAGDVHIVR
GDFDESLNYP EQKVVTVGQF KIGLIHGHQV IPWGDMASLA LLQRQFDVDI LISGHTHKFE
AFEHENKFYI NPGSATGAYN ALETNIIPSF VLMDIQASTV VTYVYQLIGD DVKVERIEYK
KS
