ID   VP26B_PONAB             Reviewed;         336 AA.
AC   Q5R436;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Vacuolar protein sorting-associated protein 26B;
DE   AltName: Full=Vesicle protein sorting 26B;
GN   Name=VPS26B;
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 transport of WLS distinct from the SNX-BAR retromer pathway.
CC       The SNX27-retromer is believed to be involved in endosome-to-plasma
CC       membrane trafficking and recycling of a broad spectrum of cargo
CC       proteins. The CSC seems to act as recruitment hub for other proteins,
CC       such as the WASH complex and TBC1D5. May be involved in retrograde
CC       transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in
CC       SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (By similarity).
CC       {ECO:0000250}.
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. The CSC has
CC       a highly elongated structure with VPS26 and VPS29 binding independently
CC       at opposite distal ends of VPS35 as central platform. The CSC is
CC       believed to associate with variable sorting nexins to form functionally
CC       distinct retromer complex variants. The originally described SNX-BAR
CC       retromer is a pentamer containing the CSC and a heterodimeric membrane-
CC       deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also
CC       called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes
CC       associate with low affinity. The CSC associates with SNX3 to form a
CC       SNX3-retromer complex. The CSC associates with SNX27, the WASH complex
CC       and the SNX-BAR subcomplex to form the SNX27-retromer complex.
CC       Interacts with VPS29, VPS35, TBC1D5, GOLPH3, SNX27 (By similarity).
CC       {ECO:0000250|UniProtKB:O75436, ECO:0000250|UniProtKB:Q8C0E2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8C0E2}.
CC       Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8C0E2}.
CC       Early endosome {ECO:0000250|UniProtKB:Q8C0E2}. Late endosome
CC       {ECO:0000250|UniProtKB:Q8C0E2}.
CC   -!- SIMILARITY: Belongs to the VPS26 family. {ECO:0000305}.
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DR   EMBL; CR861424; CAH93480.1; -; mRNA.
DR   AlphaFoldDB; Q5R436; -.
DR   SMR; Q5R436; -.
DR   STRING; 9601.ENSPPYP00000004656; -.
DR   eggNOG; KOG3063; Eukaryota.
DR   InParanoid; Q5R436; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   Gene3D; 2.60.40.640; -; 2.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR028934; Vps26-related.
DR   PANTHER; PTHR12233; PTHR12233; 1.
DR   Pfam; PF03643; Vps26; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endosome; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..336
FT                   /note="Vacuolar protein sorting-associated protein 26B"
FT                   /id="PRO_0000247091"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4G0F5"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4G0F5"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4G0F5"
SQ   SEQUENCE   336 AA;  39109 MW;  4ACB9C2F7C839DA2 CRC64;
     MSFFGFGQSV EVEILLNDAE SRKRAEHKTE DGKKEKYFLF YDGETVSGKV GLALKNPNKR
     LEHQGIKIEF IGQIELYYDR GNHHEFVSLV KDLARPGEIT QSQAFDFEFT HVEKPYESYT
     GQNVKLRYFL RATISRRLND VVKEMDIVVH TLSTYPELNS SIKMEVGIED CLHIEFEYNK
     SKYHLKDVIV GKIYFLLVRI KIKHMEIDII KRETTGTGPN VYHENVTIAK YEIMDGAPVR
     GESIPIRLFL AGYELTPTMR DINKKFSVRY YLNLVLIDEE ERRYFKQQEV VLWRKGDIVR
     KSMSHQAAIA SQRFEGTTSL GEVRTPSQLS DNNCRQ