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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
 
 
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