VPS41_MOUSE
ID VPS41_MOUSE Reviewed; 853 AA.
AC Q5KU39; Q05AE9; Q3TPS1; Q80V99; Q8BKK6; Q8CG01; Q8CJC3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Vacuolar protein sorting-associated protein 41 homolog;
DE AltName: Full=VAM2 homolog;
DE Short=mVAM2;
GN Name=Vps41;
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Wakabayashi T., Nakamura N., Wada Y., Futai M.;
RT "Mouse cDNA for yeast Vam2p Homologue (mVAM2).";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ; TISSUE=Liver;
RA Dell'Angelica E.C., Peters L.L.;
RT "A mouse homolog of yeast VPS41.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Spinal ganglion;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, 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).
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC lysosomal compartments including the endocytic membrane transport and
CC autophagic pathways. Believed to act in part as a core component of the
CC putative HOPS endosomal tethering complex is proposed to be involved in
CC the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and
CC via binding SNAREs and SNARE complexes to mediate tethering and docking
CC events during SNARE-mediated membrane fusion. The HOPS complex is
CC proposed to be recruited to Rab7 on the late endosomal membrane and to
CC regulate late endocytic, phagocytic and autophagic traffic towards
CC lysosomes. Involved in homotypic vesicle fusions between late endosomes
CC and in heterotypic fusions between late endosomes and lysosomes
CC implicated in degradation of endocytosed cargo. Required for fusion of
CC autophagosomes with lysosomes. Links the HOPS complex to endosomal via
CC its association with RILP and to lysosomal membranes via its
CC association with ARL8B, suggesting that these interactions may bring
CC the compartments to close proximity for fusion (By similarity).
CC Involved in the direct trans-Golgi network to late endosomes transport
CC of lysosomal membrane proteins independently of HOPS (By similarity).
CC Involved in sorting to the regulated secretory pathway presumably
CC implicating the AP-3 adapter complex (By similarity). May play a role
CC in HOPS-independent function in the regulated secretory pathway (By
CC similarity). {ECO:0000250|UniProtKB:D3ZVH6,
CC ECO:0000250|UniProtKB:P49754}.
CC -!- SUBUNIT: Component of the putative homotypic fusion and vacuole protein
CC sorting (HOPS) complex; the core of which composed of the class C Vps
CC proteins VPS11, VPS16, VPS18 and VPS33A, is associated with VPS39 and
CC VPS41. Interacts with RILP, MON1B. Interacts with ARL8B (GTP-bound
CC form); involved in recruitment to lysosomes and probably hierarchial
CC assembly of the HOPS complex at lysosomal membranes. In vitro can self-
CC assemble into a lattice. Associates with adapter protein complex 3 (AP-
CC 3) and clathrin:AP-3 complexes. Interacts with STX17; this interaction
CC is increased in the absence of TMEM39A. Interacts with ARL8B and
CC PLEKHM1; the interaction mediates the recruitment of the HOPS complex
CC to lysosomes. {ECO:0000250|UniProtKB:P49754}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:P49754};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P49754}. Late
CC endosome membrane {ECO:0000250|UniProtKB:P49754}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P49754}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P49754}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49754}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P49754}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P49754}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:P49754}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:P49754}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P49754}.
CC -!- SIMILARITY: Belongs to the VPS41 family. {ECO:0000305}.
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DR EMBL; AB028843; BAD88410.1; -; mRNA.
DR EMBL; AF327407; AAN73032.1; -; mRNA.
DR EMBL; AK051658; BAC34707.1; -; mRNA.
DR EMBL; AK164177; BAE37664.1; -; mRNA.
DR EMBL; BC023243; AAH23243.1; -; mRNA.
DR EMBL; BC049916; AAH49916.1; -; mRNA.
DR EMBL; BC119362; AAI19363.1; -; mRNA.
DR EMBL; BC125299; AAI25300.1; -; mRNA.
DR CCDS; CCDS26257.1; -.
DR RefSeq; NP_742118.3; NM_172120.4.
DR AlphaFoldDB; Q5KU39; -.
DR SMR; Q5KU39; -.
DR BioGRID; 229988; 13.
DR IntAct; Q5KU39; 9.
DR STRING; 10090.ENSMUSP00000072729; -.
DR iPTMnet; Q5KU39; -.
DR PhosphoSitePlus; Q5KU39; -.
DR EPD; Q5KU39; -.
DR MaxQB; Q5KU39; -.
DR PaxDb; Q5KU39; -.
DR PeptideAtlas; Q5KU39; -.
DR PRIDE; Q5KU39; -.
DR ProteomicsDB; 297816; -.
DR Antibodypedia; 13056; 131 antibodies from 30 providers.
DR DNASU; 218035; -.
DR Ensembl; ENSMUST00000072961; ENSMUSP00000072729; ENSMUSG00000041236.
DR GeneID; 218035; -.
DR KEGG; mmu:218035; -.
DR UCSC; uc007pok.2; mouse.
DR CTD; 27072; -.
DR MGI; MGI:1929215; Vps41.
DR VEuPathDB; HostDB:ENSMUSG00000041236; -.
DR eggNOG; KOG2066; Eukaryota.
DR GeneTree; ENSGT00390000000481; -.
DR HOGENOM; CLU_001285_2_2_1; -.
DR InParanoid; Q5KU39; -.
DR OMA; KFKYQRI; -.
DR OrthoDB; 722805at2759; -.
DR PhylomeDB; Q5KU39; -.
DR TreeFam; TF300451; -.
DR BioGRID-ORCS; 218035; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Vps41; mouse.
DR PRO; PR:Q5KU39; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q5KU39; protein.
DR Bgee; ENSMUSG00000041236; Expressed in rostral migratory stream and 265 other tissues.
DR Genevisible; Q5KU39; MM.
DR GO; GO:0030123; C:AP-3 adaptor complex; ISO:MGI.
DR GO; GO:0071439; C:clathrin complex; ISO:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
DR GO; GO:0030897; C:HOPS complex; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISO:MGI.
DR GO; GO:1902501; C:lysosomal HOPS complex; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0034058; P:endosomal vesicle fusion; ISO:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
DR GO; GO:0048193; P:Golgi vesicle transport; ISO:MGI.
DR GO; GO:1902774; P:late endosome to lysosome transport; ISO:MGI.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR016902; VPS41.
DR InterPro; IPR045111; Vps41/Vps8.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12616; PTHR12616; 1.
DR Pfam; PF00637; Clathrin; 1.
DR PIRSF; PIRSF028921; VPS41; 1.
DR SMART; SM00299; CLH; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW Lysosome; Membrane; Metal-binding; Protein transport; Reference proteome;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..853
FT /note="Vacuolar protein sorting-associated protein 41
FT homolog"
FT /id="PRO_0000253020"
FT REPEAT 567..711
FT /note="CHCR"
FT ZN_FING 790..838
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..539
FT /note="Interaction with ARL8B"
FT /evidence="ECO:0000250|UniProtKB:P49754"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 16
FT /note="T -> K (in Ref. 3; BAE37664)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="G -> C (in Ref. 3; BAC34707)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="V -> L (in Ref. 2; AAN73032)"
FT /evidence="ECO:0000305"
FT CONFLICT 427..428
FT /note="LW -> HR (in Ref. 2; AAN73032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 853 AA; 98602 MW; A4D54AA7C5D0F2DD CRC64;
MAEAEEQETE SLEESTDESE EESEEEPKLK YERLSNGVTE ILQKDAASCM TVHDKFLALG
THYGKVYLLD VQGNITQKFD VSPVKINQIS LDDSGEHMGV CSEDGKLQVF GLYSGEEFHE
TFDCPIKIIA VHPQFVRSSC KQFVTGGKKL LLFERTWMNR WKSSVLHEGE GNIRSVKWRG
HLIAWANNMG VKVFDITSKQ RISNVPRDDI SLRPDMYPCS LCWKDNVTLI IGWGTSIKIC
SVKERHASEM RDLPSRYVEI VSQFETEFYI SGLAPLCDQL VVLSYVKEVS EKTEREYCAR
PRLDIIQPLP ETCEEISSDA LTVRGFQENE CRDYHLEYSE GESLFYVVSP RDVVVAKERD
QDDHIDWLLE KKKYEEALMA AEISQRNIKR HKILDIGLAY VNHLVERGEY DMAARKCQKI
LGKNASLWEY EVYKFKEIGQ LKAISPYLPR GDPVLKPLIY EMILHEFLES DYEGFATLIR
EWPGDLYNNS VIVQAVRDHL KKDSQNKTLL KTLAELYTYD KNYGNALEIY LTLRHKDVFQ
LIHKHNLFSS IKDKIVLLMD FDSEKAVDML LDNEDKISIK KVVEELEDRP ELQHVYLHKL
FKRDHHKGQR YHEKQISLYA EYDRPNLLPF LRDSTHCPLE KALEICQQRN FVEETVYLLS
RMGNSRSALK MIMEELHDVD KAIEFAKEQD DGELWEDLIL YSIDKPPFIT GLLNNIGTHV
DPILLIHRIK EGMEIPNLRD SLVKILQDYN LQILLREGCK KILVADSLSL LKKMHRTQMK
GVLVDEENIC ESCLSPILPT DAAKPFSVVV FHCRHMFHKE CLPMPSMNAP AQYCNICSAK
NRGPGSAILE MKK
