ID   VPS29_PONAB             Reviewed;         182 AA.
AC   Q5R9Z1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Vacuolar protein sorting-associated protein 29;
DE   AltName: Full=Vesicle protein sorting 29;
GN   Name=VPS29;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. 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   -!- SIMILARITY: Belongs to the VPS29 family. {ECO:0000305}.
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DR   EMBL; CR859239; CAH91419.1; -; mRNA.
DR   RefSeq; NP_001129021.1; NM_001135549.1.
DR   AlphaFoldDB; Q5R9Z1; -.
DR   SMR; Q5R9Z1; -.
DR   STRING; 9601.ENSPPYP00000005648; -.
DR   GeneID; 100190862; -.
DR   KEGG; pon:100190862; -.
DR   CTD; 51699; -.
DR   eggNOG; KOG3325; Eukaryota.
DR   InParanoid; Q5R9Z1; -.
DR   OrthoDB; 1233814at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
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: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   Acetylation; Cytoplasm; Endosome; Membrane; Metal-binding;
KW   Protein transport; Reference proteome; Transport; Zinc.
FT   CHAIN           1..182
FT                   /note="Vacuolar protein sorting-associated protein 29"
FT                   /id="PRO_0000339649"
FT   MOD_RES         50
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBQ0"
SQ   SEQUENCE   182 AA;  20466 MW;  CCCDDE6B720C864E CRC64;
     MLVLVLGDLH IPHRCNSLPA KFKKLLVPGK IQHILCTGNL CTKESYDYLK TLAGDVHIVR
     GDFDENLNYP EQKVVTVGQF KIGLIHGHQV IPWGDMASLA LLQRQFDVDI LISGHTHKFE
     AFEHENKFYI NPGSATGAYN ALEANIIPSF VLMDIQASTV VTYVYQLIGD DVKVERIEYK
     KS