ID   VP35L_DANRE             Reviewed;         963 AA.
AC   A4VCH4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=VPS35 endosomal protein-sorting factor-like {ECO:0000305};
GN   Name=vps35l; ORFNames=zgc:163107;
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=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts 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 integrins. The recruitment of the
CC       retriever complex to the endosomal membrane involves CCC and WASH
CC       complexes. In the endosomes, drives the retrieval and recycling of
CC       NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo
CC       essential for the homeostatic maintenance of numerous cell surface
CC       proteins associated with processes that include cell migration, cell
CC       adhesion, nutrient supply and cell signaling. May be involved in
CC       copper-dependent atp7a trafficking between the trans-Golgi network and
CC       vesicles in the cell periphery. {ECO:0000250|UniProtKB:Q7Z3J2}.
CC   -!- SUBUNIT: Component of the heterotrimeric retriever complex.
CC       {ECO:0000250|UniProtKB:Q7Z3J2}.
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q7Z3J2}.
CC   -!- SIMILARITY: Belongs to the VPS35L family. {ECO:0000305}.
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DR   EMBL; BC139716; AAI39717.1; -; mRNA.
DR   RefSeq; NP_001091651.1; NM_001098181.1.
DR   AlphaFoldDB; A4VCH4; -.
DR   STRING; 7955.ENSDARP00000052536; -.
DR   PaxDb; A4VCH4; -.
DR   PeptideAtlas; A4VCH4; -.
DR   PRIDE; A4VCH4; -.
DR   Ensembl; ENSDART00000052537; ENSDARP00000052536; ENSDARG00000020041.
DR   GeneID; 563454; -.
DR   KEGG; dre:563454; -.
DR   CTD; 57020; -.
DR   ZFIN; ZDB-GENE-070521-7; vps35l.
DR   eggNOG; KOG3682; Eukaryota.
DR   GeneTree; ENSGT00390000011343; -.
DR   HOGENOM; CLU_012270_0_0_1; -.
DR   InParanoid; A4VCH4; -.
DR   OMA; MANLEWV; -.
DR   OrthoDB; 247677at2759; -.
DR   PhylomeDB; A4VCH4; -.
DR   TreeFam; TF324367; -.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   PRO; PR:A4VCH4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 12.
DR   Bgee; ENSDARG00000020041; Expressed in testis and 23 other tissues.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR029705; VPS35L.
DR   PANTHER; PTHR13673; PTHR13673; 1.
PE   2: Evidence at transcript level;
KW   Endosome; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..963
FT                   /note="VPS35 endosomal protein-sorting factor-like"
FT                   /id="PRO_0000311356"
FT   REGION          38..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  108645 MW;  75A99A5CDF651A86 CRC64;
     MASVQWHSRS RKYDSEWQAS RLEVSAVEFS DYHPLKAITV TDSKSRRGGR KGSTSSSSSS
     SSSVAPDPLS SMLDGTDPLS LFAAASETPT LPHSVSAGEL GRKRKEKEEE VGLDFEPWSS
     KRGEILSRFT TTEKLSINLF MGSDTSKASS PSSAVSEKVR TRLEELDDLE EGSQRELLNL
     SQQDYVNRIE ELNQSLKEAW GSDQKVKALK IVIQCSKLLS DTSVIQFYPS KFVLITDILD
     TFGGLVYDRI WSMCADPHPL PESFSADDVN DTAKETCLNW FFKIASIREL VPRLYVEAAL
     LKCNRFLTKC GIQETLQRLT AMIRGIGDPL VAVYARAYLC RVGMEVAPHL KDSLNKNFFD
     LLASFRQIHG DSVQNQLVLQ RVEIPVYLTL YSPAINWILQ CVAYRAPEVL LTEMMDRCKK
     LGNNALLLNS VMWAFRAEFV ATRATDFIGM IKDCDEAGFP KHLLFASLGR SLSCADPPES
     ERLSILNEAW KVITKVRSPR DYINCAEIWV EFTCRHFTKR EVNTVLADII KHMTPDRAFE
     DAYPQLQSVI KKILTYFHDF SMLFSMEKFL PFLDMFQKDS VRVEVCKSIM EVFIKHQQEP
     TRDPVILNAL LHICKTMHDS VNALTLDDEK RSLALLINGF IRMVSFGRDF EQQLSFCVEA
     RATFCNLEPV IIHLIHTVNQ LAMETGRVMK GNHSRKTAAF VRACAAYSFI TIPSLTNIFS
     RLNLYLLSGQ VALANQCLSQ ADAFLKAAVS ILPEVPRSIS IEGKQRSSES FLLDFINNFL
     STLLVVPDHP EQGVLYLVRG LLNMVQDYTW EDNSDAKVRV YISALPLLAA MSQESYLYTI
     PKVDSNETLY GGDPKFIAEI NKLCETLIGQ VLDHLKSLGR DEEVRRQGSL AFSLFGCLLA
     HGDLRNNKLN QLAVNLWNLS HKHGICDTRT SVRTLEHIKH QAQQTDMSHF SDMTARLSLQ
     SRA