VPS25_MOUSE
ID VPS25_MOUSE Reviewed; 176 AA.
AC Q9CQ80; A2A4J9; A2A4K1; Q3UBT0; Q9D167;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Vacuolar protein-sorting-associated protein 25;
DE AltName: Full=ESCRT-II complex subunit VPS25;
GN Name=Vps25; Synonyms=D11Wsu68e;
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=Bone marrow, Kidney, and Lung;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; 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).
RN [4]
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).
CC -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex
CC required for transport II), which is required for multivesicular body
CC (MVB) formation and sorting of endosomal cargo proteins into MVBs. The
CC MVB pathway mediates delivery of transmembrane proteins into the lumen
CC of the lysosome for degradation. The ESCRT-II complex is probably
CC involved in the recruitment of the ESCRT-III complex. The ESCRT-II
CC complex may also play a role in transcription regulation, possibly via
CC its interaction with ELL (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex at least composed of ELL, SNF8/EAP30,
CC VPS25/EAP20 and VPS36/EAP45 (By similarity). Component of the endosomal
CC sorting complex required for transport II (ESCRT-II), composed of SNF8,
CC VPS36 and 2 copies of VPS25. Interacts with CFTR; the interaction
CC requires misfolded CFTR. Interacts (via C-terminal half) with the
CC ESCRT-III subunit CHMP6 (via N-terminal half) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane
CC {ECO:0000250}. Nucleus {ECO:0000250}. Note=Distributes diffusely
CC throughout the cytoplasm and nucleoplasm, but exhibits a punctate
CC distribution on coexpression with CHMP6. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CQ80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQ80-2; Sequence=VSP_015341;
CC -!- SIMILARITY: Belongs to the VPS25 family. {ECO:0000305}.
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DR EMBL; AK002500; BAB22148.1; -; mRNA.
DR EMBL; AK003715; BAB22955.1; -; mRNA.
DR EMBL; AK003877; BAB23054.1; -; mRNA.
DR EMBL; AK145811; BAE26665.1; -; mRNA.
DR EMBL; AK150822; BAE29884.1; -; mRNA.
DR EMBL; AK166008; BAE38516.1; -; mRNA.
DR EMBL; AL590969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029181; AAH29181.1; -; mRNA.
DR CCDS; CCDS25458.1; -. [Q9CQ80-1]
DR CCDS; CCDS70312.1; -. [Q9CQ80-2]
DR RefSeq; NP_001271340.1; NM_001284411.1.
DR RefSeq; NP_001271343.1; NM_001284414.1. [Q9CQ80-2]
DR RefSeq; NP_081052.2; NM_026776.4. [Q9CQ80-1]
DR AlphaFoldDB; Q9CQ80; -.
DR SMR; Q9CQ80; -.
DR BioGRID; 205754; 8.
DR IntAct; Q9CQ80; 3.
DR STRING; 10090.ENSMUSP00000042088; -.
DR iPTMnet; Q9CQ80; -.
DR PhosphoSitePlus; Q9CQ80; -.
DR EPD; Q9CQ80; -.
DR jPOST; Q9CQ80; -.
DR MaxQB; Q9CQ80; -.
DR PaxDb; Q9CQ80; -.
DR PeptideAtlas; Q9CQ80; -.
DR PRIDE; Q9CQ80; -.
DR ProteomicsDB; 299956; -. [Q9CQ80-1]
DR ProteomicsDB; 299957; -. [Q9CQ80-2]
DR Antibodypedia; 29407; 231 antibodies from 31 providers.
DR DNASU; 28084; -.
DR Ensembl; ENSMUST00000007533; ENSMUSP00000007533; ENSMUSG00000078656. [Q9CQ80-2]
DR Ensembl; ENSMUST00000042477; ENSMUSP00000042088; ENSMUSG00000078656. [Q9CQ80-1]
DR GeneID; 28084; -.
DR KEGG; mmu:28084; -.
DR UCSC; uc007loa.2; mouse. [Q9CQ80-1]
DR UCSC; uc007lob.2; mouse. [Q9CQ80-2]
DR CTD; 84313; -.
DR MGI; MGI:106354; Vps25.
DR VEuPathDB; HostDB:ENSMUSG00000078656; -.
DR eggNOG; KOG4068; Eukaryota.
DR GeneTree; ENSGT00390000014892; -.
DR HOGENOM; CLU_087657_1_0_1; -.
DR InParanoid; Q9CQ80; -.
DR OMA; SQEFHGM; -.
DR OrthoDB; 1094121at2759; -.
DR PhylomeDB; Q9CQ80; -.
DR TreeFam; TF317731; -.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 28084; 35 hits in 74 CRISPR screens.
DR ChiTaRS; Vps25; mouse.
DR PRO; PR:Q9CQ80; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQ80; protein.
DR Bgee; ENSMUSG00000078656; Expressed in yolk sac and 189 other tissues.
DR ExpressionAtlas; Q9CQ80; baseline and differential.
DR Genevisible; Q9CQ80; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0000814; C:ESCRT II complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISO:MGI.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.10.570; -; 1.
DR InterPro; IPR008570; ESCRT-II_cplx_Vps25-sub.
DR InterPro; IPR014041; ESCRT-II_cplx_Vps25-sub_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13149; PTHR13149; 1.
DR Pfam; PF05871; ESCRT-II; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endosome; Membrane; Nucleus;
KW Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..176
FT /note="Vacuolar protein-sorting-associated protein 25"
FT /id="PRO_0000215217"
FT VAR_SEQ 140..176
FT /note="EFHGLDEATLLRALQALQQEHKAEIITVSDGRGVKFF -> ASSRFVGVS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015341"
SQ SEQUENCE 176 AA; 20748 MW; B85B3A4617BA40A3 CRC64;
MAMSFEWPWQ YRFPPFFTLQ PNVDTRQKQL AAWCSLVLSF CRLHKQSSMT VMEAQESPLF
NNVKLQRKLP VESIQIVLEE LRKKGNLEWL DKNKSSFLIM WRRPEEWGKL IYQWVSRSGQ
NNSVFTLYEL TSGEDTEDEE FHGLDEATLL RALQALQQEH KAEIITVSDG RGVKFF
