ID   VPS29_XENLA             Reviewed;         182 AA.
AC   Q6GP62;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Vacuolar protein sorting-associated protein 29;
DE   AltName: Full=Vesicle protein sorting 29;
GN   Name=vps29;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary, and Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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. Retromer mediates retrograde transport of cargo
CC       proteins from endosomes to the trans-Golgi network (TGN) (By
CC       similarity). Acts also as component of the retriever complex. The
CC       retriever complex is an heterotrimeric complex related to retromer
CC       cargo-selective complex (CSC) and essential for retromer-independent
CC       retrieval and recycling of numerous cargos such as integrins. In the
CC       endosomes, retriever complex drives the retrieval and recycling of
CC       NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo
CC       essential for the homeostatic maintenance of numerous cell surface
CC       proteins associated with processes that include cell migration, cell
CC       adhesion, nutrient supply and cell signaling (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UBQ0}.
CC   -!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective
CC       complex (CSC) which is believed to associate with variable sorting
CC       nexins to form functionally distinct retromer complex variants (By
CC       similarity). Component of the heterotrimeric retriever complex (By
CC       similarity). {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}.
CC   -!- SIMILARITY: Belongs to the VPS29 family. {ECO:0000305}.
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DR   EMBL; BC073281; AAH73281.1; -; mRNA.
DR   EMBL; BC097520; AAH97520.1; -; mRNA.
DR   RefSeq; NP_001085746.1; NM_001092277.1.
DR   RefSeq; XP_018118894.1; XM_018263405.1.
DR   AlphaFoldDB; Q6GP62; -.
DR   SMR; Q6GP62; -.
DR   MaxQB; Q6GP62; -.
DR   DNASU; 444173; -.
DR   GeneID; 108716875; -.
DR   GeneID; 444173; -.
DR   KEGG; xla:108716875; -.
DR   CTD; 444173; -.
DR   Xenbase; XB-GENE-967958; vps29.S.
DR   OrthoDB; 1233814at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 108716875; Expressed in brain and 20 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030904; C:retromer complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Endosome; Membrane; Metal-binding; Protein transport;
KW   Reference proteome; Transport; Zinc.
FT   CHAIN           1..182
FT                   /note="Vacuolar protein sorting-associated protein 29"
FT                   /id="PRO_0000339652"
SQ   SEQUENCE   182 AA;  20450 MW;  E1DB51F86D8105EC CRC64;
     MLVLVLGDLH IPHRCNSLPA KFKKLLVPGK IQHILCTGNL CTKESFDYLK TLAGDVHIVR
     GDFDENLNYP EQKVVTVGQF KIGLIHGHQV IPWGDMASLA LLQRQLDVDI LISGHTQKFE
     AFEHENKFYI NPGSATGAYN ALENNIIPSF VLMDIQASTV VTYVYQLIGD DVKVERIEYK
     KS