VP35L_RAT
ID VP35L_RAT Reviewed; 936 AA.
AC Q5XI83;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=VPS35 endosomal protein-sorting factor-like {ECO:0000305};
GN Name=Vps35l {ECO:0000312|RGD:1564485};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC083805; AAH83805.1; -; mRNA.
DR RefSeq; NP_001017463.1; NM_001017463.1.
DR AlphaFoldDB; Q5XI83; -.
DR IntAct; Q5XI83; 1.
DR STRING; 10116.ENSRNOP00000043528; -.
DR iPTMnet; Q5XI83; -.
DR PhosphoSitePlus; Q5XI83; -.
DR jPOST; Q5XI83; -.
DR PaxDb; Q5XI83; -.
DR PRIDE; Q5XI83; -.
DR Ensembl; ENSRNOT00000050393; ENSRNOP00000043528; ENSRNOG00000016063.
DR GeneID; 361635; -.
DR KEGG; rno:361635; -.
DR UCSC; RGD:1564485; rat.
DR CTD; 57020; -.
DR RGD; 1564485; Vps35l.
DR eggNOG; KOG3682; Eukaryota.
DR GeneTree; ENSGT00390000011343; -.
DR HOGENOM; CLU_012270_0_0_1; -.
DR InParanoid; Q5XI83; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q5XI83; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016063; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; Q5XI83; baseline and differential.
DR Genevisible; Q5XI83; RN.
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:0006893; P:Golgi to plasma membrane transport; ISO:RGD.
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..936
FT /note="VPS35 endosomal protein-sorting factor-like"
FT /id="PRO_0000311355"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 43..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..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 936 AA; 106151 MW; 5D27B332D2CF5DB2 CRC64;
MAVFPWHSRN RNYKAELASC RLETVPLECG DYHPLKPITV TESKTKKVSR KGSTSSTSSS
SSSSVVDPLS SVLDGTDPLS MFAATSDPAA TVTVTESSRK KRDKDDNSFV GPDFEPWANK
RGEILARYTT TEKLSINLFM GSEKGRAGAA ASAMSEKVRT RLEELDDFEE GSQKELLNLT
QQDYVNRIEE LNQSLKDAWA SDQKVKALKI VIQCSKLLSD TSVIQFYPSK FVLITDILDT
FGKLVYERIY SMCVDSRGAL PDHFSPENVN DTAKETCLNW FFKIASIREL IPRFYVEASI
LKCNKFLSKT GISECLPRLT CMIRGIGDPL VSVYARAYLC RVGMEVAPHL KESLTRNFFD
FLLTFKQIHG DTVQNQLVAQ GVELLSYLPL YSPAMGWIFQ CVSYHAPEAL LTEMMERCKK
LGNNALLLNS VMSAFRAEFI ATRSMDFIGM IKECDESGFP KHLLFRSLGV NLALADPPEN
DRLQILNEAW KVITKLKSPQ DYINCAEVWV EYTCRHFTKR EVNTVLADVI KHMTPDRAFE
DSYPQLQSII KKVIAHFHDF SVLFSVEKFL PFLDMFQKES VRVEVCKCIM EAFINALTLE
DEKRMLAHLI NGFIKMVSFG RDFEQQLSFY VESRSMFCNL EPVLVQLIHS VNRLAMETRK
VMKGNHSRKT AAFVRACVAY CFITIPSLVG IFTRLNLYLH SGQVALANQC LSQADAFFKA
AISLVPEVPK SISIDGKLRP SEPFLLEFLC NFFSTLLIVP DHPEHGVLFL VRELLNVIQD
YTWEDSSDDK IRIYTSVLHL LSAMSQDTYL YHIDKVDSND SLYGGDSRFL AENSKLCEAA
MVQILEHLKT LAKDEALKRQ SLLGLSFFNS ILAHGDLRNN KLNQLSVNLW HLAQRHGCAD
TRTMVKTLDY IKKRSKQPDM NHLSELALRL PLQTRT