ID   VP35L_PONAB             Reviewed;         963 AA.
AC   Q5R8N4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=VPS35 endosomal protein-sorting factor-like {ECO:0000305};
GN   Name=VPS35L {ECO:0000250|UniProtKB:Q7Z3J2};
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 integrin alpha-5/beta-1
CC       (ITGA5:ITGB1). The recruitment of the retriever complex to the
CC       endosomal membrane involves CCC and WASH complexes. In the endosomes,
CC       drives the retrieval and recycling of NxxY-motif-containing cargo
CC       proteins by coupling to SNX17, a cargo essential for the homeostatic
CC       maintenance of numerous cell surface proteins associated with processes
CC       that include cell migration, cell adhesion, nutrient supply and cell
CC       signaling. Involved in copper-dependent ATP7A trafficking between the
CC       trans-Golgi network and vesicles in the cell periphery; the function is
CC       proposed to depend on its association with the CCC complex and
CC       cooperation with the WASH complex on early endosomes. Seems not to be
CC       required for CCC complex stability. {ECO:0000250|UniProtKB:Q7Z3J2}.
CC   -!- SUBUNIT: Component of the heterotrimeric retriever complex formed by
CC       VPS26C, VPS29 and VPS35L. Interacts with VPS29. Interacts with COMMD1,
CC       CCDC93 and CCDC22; associates with the CCC (COMMD/CCDC22/CCDC93)
CC       complex which contains at least COMMD1 (and possibly other COMM domain-
CC       containing proteins), CCDC22 and CCDC93. Interacts with WASHC1, WASHC2A
CC       and WASHC2C. Interacts with SNX17 and SNX31.
CC       {ECO:0000250|UniProtKB:Q7Z3J2}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}. Endosome {ECO:0000250|UniProtKB:Q7Z3J2}.
CC       Note=Endosome location is dependent of the association with the CCC and
CC       WASH complexes. {ECO:0000250|UniProtKB:Q7Z3J2}.
CC   -!- SIMILARITY: Belongs to the VPS35L family. {ECO:0000305}.
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DR   EMBL; CR859717; CAH91876.1; -; mRNA.
DR   RefSeq; NP_001126088.1; NM_001132616.1.
DR   AlphaFoldDB; Q5R8N4; -.
DR   STRING; 9601.ENSPPYP00000008083; -.
DR   GeneID; 100173041; -.
DR   KEGG; pon:100173041; -.
DR   CTD; 57020; -.
DR   eggNOG; KOG3682; Eukaryota.
DR   OrthoDB; 247677at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..963
FT                   /note="VPS35 endosomal protein-sorting factor-like"
FT                   /id="PRO_0000311354"
FT   TRANSMEM        703..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          43..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..113
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"
FT   COMPBIAS        96..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z3J2"
SQ   SEQUENCE   963 AA;  109494 MW;  9089C54FDD0BEE98 CRC64;
     MAVFPWHSRN RNYKAEFASC RLEAVPLEFG DYHPLKPITV TESKTKKVNR KGSTSSTSSS
     SSSSVVDPLS SVLDGTDPLS MFAATADPAA LAAATDSSRK KRDRDDNSIV GSDFEPWANK
     RGEILARYTT TEKLSINLFM GSEKGKAGTA TLAMSEKVRT RLEELDDFEE GSQKELLNLT
     QQDYVNRIEE LNQSLKDAWA SDQKVKALKI VIQCSKLPSD TSVIQFYPSK FVLITDILDT
     FGKLVYERIF SMCVDNRSVL PDHFSPENAN DTAKETCLNW FFKIASIREL IPRFYVEASI
     LKCNKFLSKT GISECLPRLT CMIRGIGDPL VSVYARAYLC RVGMEVAPHL KETLNKNFFD
     FLLTFKQIHG DTVQNQLVVQ GVELPSYLPL YPPAMDWIFQ CISYHAPEAL LTEMMERCKK
     LGNNALLLNS VMSAFRAEFI ATRSMDFIGM IKECDESGFP KHLLFRSLGL NLALADPPES
     DRLQILNEAW KVITKLKNPQ DYINCAEVWV EYTCKHFTKR EVNTVLADVI KHMTPDRAFE
     DSYPQLQLII KKVIAHFHDF SVLLSVEKFL PFLDMFQKES VRVEVCKCIM DAFIKHQQEP
     TKDPVILNAL LHVCKTMHDS VNALTLEDEK RMLSYLINGF IKMVSFGRDF EQQLSFYVES
     RSMFCNLEPV LVQLIHSVNR LAMETRKVMK GNHSRKTAAF VRACVAYCFI TIPSLVGIFT
     RLNLYLHSGQ VALANQCLSQ ADAFFKAAIS LVPEVPKMIN IDGKMRPSES FLLEFLCNFF
     STLLIVPDHP EHGVLFLVRE LLNVIQDYTW EDNSDEKIRI YTCVLHLLSA MSQETYLYHI
     DKVDSNDSLY GGDSKFLAEN NKLCETVMAQ ILEHLKTLAK DEALKRQSSL GLSFFNSILA
     HGDLRNNKLN QLSVNLWHLA QRHGCADTRT MVKTLEYIKK QSKQPDMTHL TELALRLPLQ
     TRT