VP26A_XENTR
ID VP26A_XENTR Reviewed; 326 AA.
AC Q28HT6; Q0VGY4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Vacuolar protein sorting-associated protein 26A;
DE AltName: Full=Vesicle protein sorting 26A;
GN Name=vps26a; ORFNames=TGas130e20.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-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. Retromer mediates retrograde transport of cargo
CC proteins from endosomes to the trans-Golgi network (TGN) (By
CC similarity). {ECO:0000250|UniProtKB:O75436}.
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). {ECO:0000250|UniProtKB:O75436}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40336}.
CC Endosome membrane {ECO:0000250|UniProtKB:P40336}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P40336}. Early endosome
CC {ECO:0000250|UniProtKB:O75436}. Note=Localizes to tubular profiles
CC adjacent to endosomes. {ECO:0000250|UniProtKB:O75436}.
CC -!- SIMILARITY: Belongs to the VPS26 family. {ECO:0000305}.
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DR EMBL; CR760746; CAJ83492.1; -; mRNA.
DR EMBL; BC080329; AAH80329.1; -; mRNA.
DR RefSeq; NP_001017171.1; NM_001017171.3.
DR AlphaFoldDB; Q28HT6; -.
DR SMR; Q28HT6; -.
DR PaxDb; Q28HT6; -.
DR DNASU; 549925; -.
DR Ensembl; ENSXETT00000019433; ENSXETP00000019433; ENSXETG00000008848.
DR GeneID; 549925; -.
DR KEGG; xtr:549925; -.
DR CTD; 9559; -.
DR Xenbase; XB-GENE-944860; vps26a.
DR eggNOG; KOG3063; Eukaryota.
DR HOGENOM; CLU_031077_0_0_1; -.
DR InParanoid; Q28HT6; -.
DR OMA; FKQHGKR; -.
DR OrthoDB; 987411at2759; -.
DR PhylomeDB; Q28HT6; -.
DR TreeFam; TF300907; -.
DR Reactome; R-XTR-3238698; WNT ligand biogenesis and trafficking.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000008848; Expressed in egg cell and 19 other tissues.
DR ExpressionAtlas; Q28HT6; baseline.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030904; C:retromer complex; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; 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 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; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..326
FT /note="Vacuolar protein sorting-associated protein 26A"
FT /id="PRO_0000247088"
SQ SEQUENCE 326 AA; 38123 MW; F13FB061A52763A3 CRC64;
MSFLSGFFGP ICEIEVVLND ADTRKVSEIK TEEGKVEKHF LFYDGESVAG KVNIVFRQPG
KRLEHQGIRI EFVGQIELFN DKSNTHEFVN LVKELALPGE LTQSRNYDFE FMQVEKPYES
YIGANVRLRY FLKVTIVRRL TDLVKEYDLI VHQLATYPDV NNSIKMEVGI EDCLHIEFEY
NKSKYHLKDV IVGKIYFLLV RIKIQHMELQ LIKKEITGIG PSTTTETETV AKYEIMDGAP
VKGESIPIRL FLAGYDPTPT MRDVNKKFSV RYFLNLVLVD EEDRRYFKQQ EIILWRKAPE
KIRKRTNFHQ RFEPQEPQAS AEEPEI