VP26A_DANRE
ID VP26A_DANRE Reviewed; 327 AA.
AC Q6TNP8; Q7ZUB5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Vacuolar protein sorting-associated protein 26A;
DE AltName: Full=Vesicle protein sorting 26A;
GN Name=vps26a; ORFNames=zgc:56673;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-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; AY391469; AAQ91281.1; -; mRNA.
DR EMBL; BC049342; AAH49342.1; -; mRNA.
DR EMBL; BC071350; AAH71350.1; -; mRNA.
DR RefSeq; NP_957201.1; NM_200907.1.
DR PDB; 6MD5; X-ray; 1.70 A; A=9-327.
DR PDBsum; 6MD5; -.
DR AlphaFoldDB; Q6TNP8; -.
DR SMR; Q6TNP8; -.
DR STRING; 7955.ENSDARP00000072602; -.
DR PaxDb; Q6TNP8; -.
DR PRIDE; Q6TNP8; -.
DR DNASU; 393881; -.
DR Ensembl; ENSDART00000078140; ENSDARP00000072602; ENSDARG00000056549.
DR GeneID; 393881; -.
DR KEGG; dre:393881; -.
DR CTD; 9559; -.
DR ZFIN; ZDB-GENE-040426-1108; vps26a.
DR eggNOG; KOG3063; Eukaryota.
DR GeneTree; ENSGT00950000183064; -.
DR HOGENOM; CLU_031077_0_0_1; -.
DR InParanoid; Q6TNP8; -.
DR OMA; FKQHGKR; -.
DR OrthoDB; 987411at2759; -.
DR PhylomeDB; Q6TNP8; -.
DR TreeFam; TF300907; -.
DR Reactome; R-DRE-3238698; WNT ligand biogenesis and trafficking.
DR PRO; PR:Q6TNP8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000056549; Expressed in cleaving embryo and 28 other tissues.
DR ExpressionAtlas; Q6TNP8; baseline and differential.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..327
FT /note="Vacuolar protein sorting-associated protein 26A"
FT /id="PRO_0000247085"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 11
FT /note="V -> A (in Ref. 2; AAH49342)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="D -> E (in Ref. 2; AAH49342)"
FT /evidence="ECO:0000305"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:6MD5"
FT TURN 19..23
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:6MD5"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 84..96
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 124..136
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:6MD5"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 190..200
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 205..219
FT /evidence="ECO:0007829|PDB:6MD5"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:6MD5"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:6MD5"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 267..279
FT /evidence="ECO:0007829|PDB:6MD5"
FT STRAND 286..295
FT /evidence="ECO:0007829|PDB:6MD5"
SQ SEQUENCE 327 AA; 38178 MW; 636497E67FC4C928 CRC64;
MSFLGGLFGP VCEIDVILND AESRKTAELK TEEGKLEKHY LFYDGESVSG KVNINVKQTS
KRLEHQGIRI EFVGQIELFS DKSNTHEFVN LVKELALPGE LTQNRSYDFE FMQVEKPYES
YVGANVRLRY FLKVTIVRRL SDLVKEYDLI VHQLATYPDV NNSIKMEVGI EDCLHIEFEY
NKSKYHLKDV IVGKIYFLLV RIKIQHMELQ LIKKEMTGIG PSTTTETETV AKYEIMDGAP
VKGESIPIRL FLAGYDLTPT MRDVNKKFSV RYFLNLVLVD EEDRRYFKQQ EIVLWRKAPE
KMRKRNFHQR YESPEPRPSL SAEQPEM