VP35L_MOUSE
ID VP35L_MOUSE Reviewed; 963 AA.
AC Q8BWQ6; Q3UWS3; Q3UXM0; Q7TQF5; Q80XN3; Q8R3A8; Q91VY3; Q9D307;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=VPS35 endosomal protein-sorting factor-like {ECO:0000305};
GN Name=Vps35l {ECO:0000312|MGI:MGI:1918767};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Colon, Egg, Liver, and Muellerian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Brain, Kidney, and Mammary tumor;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=31712251; DOI=10.1136/jmedgenet-2019-106213;
RA Kato K., Oka Y., Muramatsu H., Vasilev F.F., Otomo T., Oishi H., Kawano Y.,
RA Kidokoro H., Nakazawa Y., Ogi T., Takahashi Y., Saitoh S.;
RT "Biallelic VPS35L pathogenic variants cause 3C/Ritscher-Schinzel-like
RT syndrome through dysfunction of retriever complex.";
RL J. Med. Genet. 57:245-253(2020).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BWQ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BWQ6-2; Sequence=VSP_029541, VSP_029542;
CC Name=3;
CC IsoId=Q8BWQ6-3; Sequence=VSP_029539, VSP_029540;
CC -!- DISRUPTION PHENOTYPE: Homozygous VPS35L knockout is embryonic lethal at
CC an early stage of embryo development, between 7.5 and 10.5 dpc.
CC {ECO:0000269|PubMed:31712251}.
CC -!- SIMILARITY: Belongs to the VPS35L family. {ECO:0000305}.
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DR EMBL; AK018573; BAB31285.1; -; mRNA.
DR EMBL; AK050302; BAC34176.1; -; mRNA.
DR EMBL; AK135468; BAE22543.1; -; mRNA.
DR EMBL; AK136140; BAE22841.1; -; mRNA.
DR EMBL; BC007154; AAH07154.1; -; mRNA.
DR EMBL; BC025808; AAH25808.1; -; mRNA.
DR EMBL; BC043674; AAH43674.1; -; mRNA.
DR EMBL; BC054720; AAH54720.1; -; mRNA.
DR CCDS; CCDS21776.2; -. [Q8BWQ6-1]
DR RefSeq; NP_082091.3; NM_027815.4.
DR AlphaFoldDB; Q8BWQ6; -.
DR BioGRID; 214753; 1.
DR IntAct; Q8BWQ6; 3.
DR STRING; 10090.ENSMUSP00000051263; -.
DR iPTMnet; Q8BWQ6; -.
DR PhosphoSitePlus; Q8BWQ6; -.
DR SwissPalm; Q8BWQ6; -.
DR EPD; Q8BWQ6; -.
DR jPOST; Q8BWQ6; -.
DR MaxQB; Q8BWQ6; -.
DR PaxDb; Q8BWQ6; -.
DR PeptideAtlas; Q8BWQ6; -.
DR PRIDE; Q8BWQ6; -.
DR Antibodypedia; 52453; 51 antibodies from 14 providers.
DR DNASU; 71517; -.
DR Ensembl; ENSMUST00000033280; ENSMUSP00000033280; ENSMUSG00000030982. [Q8BWQ6-3]
DR GeneID; 71517; -.
DR KEGG; mmu:71517; -.
DR UCSC; uc009jkp.2; mouse. [Q8BWQ6-3]
DR CTD; 57020; -.
DR MGI; MGI:1918767; Vps35l.
DR VEuPathDB; HostDB:ENSMUSG00000030982; -.
DR eggNOG; KOG3682; Eukaryota.
DR GeneTree; ENSGT00390000011343; -.
DR InParanoid; Q8BWQ6; -.
DR OrthoDB; 247677at2759; -.
DR PhylomeDB; Q8BWQ6; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 71517; 5 hits in 71 CRISPR screens.
DR PRO; PR:Q8BWQ6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BWQ6; protein.
DR Bgee; ENSMUSG00000030982; Expressed in animal zygote and 254 other tissues.
DR ExpressionAtlas; Q8BWQ6; baseline and differential.
DR Genevisible; Q8BWQ6; MM.
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:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR029705; VPS35L.
DR PANTHER; PTHR13673; PTHR13673; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..963
FT /note="VPS35 endosomal protein-sorting factor-like"
FT /id="PRO_0000311353"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 43..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
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"
FT VAR_SEQ 1..235
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029539"
FT VAR_SEQ 236..241
FT /note="DILDTF -> MLLAGH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029540"
FT VAR_SEQ 409..434
FT /note="ALLTEMMERCKKLGNNALLLNSVMSA -> CALSSLPSLLSELRGLSHLWRC
FT AEAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029541"
FT VAR_SEQ 435..963
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029542"
FT CONFLICT 208
FT /note="L -> V (in Ref. 1; BAE22841)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="T -> M (in Ref. 2; AAH07154/AAH25808)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="I -> M (in Ref. 1; BAE22543)"
FT /evidence="ECO:0000305"
FT CONFLICT 781
FT /note="S -> C (in Ref. 1; BAC34176)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="I -> M (in Ref. 2; AAH25808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 963 AA; 109077 MW; 0A7A7A73FDBDF740 CRC64;
MAVFPWHSRN RNYKAELASC RLETVPLECG DYHPLKPITV TESKTKKVSR KGSTSSTSSS
SSSSVIDPLS SVLDGTDPLS MFAATSDPAA TGTVTDSSRK KRDKDENSFV GPDFEPWANK
RVEILARYTT TEKLSINLFM GSEKGRGGAA ASAMSEKVRT RLEELDDFEE GSQKELLNLT
QQDYVNRIEE LNQSLKDAWA SDQKVKALKI VIQCSKLLSD TSVIQFYPSK FVLITDILDT
FGKLVYERIS SMCVDSRSAL PDHFSPENVN DTAKETCLNW FFKIASIREL IPRFYVEASI
LKCNKFLSKT GISECLPRLT CMIRGIGDPL VSVYARAYLC RVGIEVAPHL KESLNKNFFD
FLLTFKQIHG DTVQNQLVAQ GVELLSYLPL YSPAMGWIFQ CVSYHAPEAL LTEMMERCKK
LGNNALLLNS VMSAFRAEFV ATRSMDFIGM IKECDESGFP KHLLFRSLGL NLALADPPEN
DRLQILNEAW KVITKLKSPQ DYINCAEVWV EYTCRHFTKR EVNTVLADVI KHMTPDRAFE
DSYPQLQSII QKVIAHFHDF SVLFSVEKFL PFLDMFQKES VRVEVCKCIM EAFIKHQQEP
TKDPVILNAL LHICKTMHDS VNALTLEDEK RTLAHLINGF IKMVSFGRDF EQQLSFYVES
RSMFCNLEPV LVQLIHSVNR LAMETRKVMK GNHSRKTAAF VRACVAYCFI TIPSLVGIFT
RLNLYLHSGQ VALANQCLSQ ADAFFKAAIG LVPEVPKTIS IDGKLRPSEP FLLEFLCNFF
STLLIVPDHP EHGVLFLVRE LLNVIQDYTW EDSSDDKIRI YTSVLHLLSA MSQDTYLYHI
DKVDSNDSLY GGDSKFLAEN SKLCEAVMAQ ILEHLKTLAK DEALKRQSLL GLSFFNSILA
HGDLRNNKLN QLSVNLWHLA QRHGCADTRT MVKTLDYIKK RSKQPDMNHL SELALRLPLQ
TRT
