VPS28_MOUSE
ID VPS28_MOUSE Reviewed; 221 AA.
AC Q9D1C8;
DT 01-FEB-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 28 homolog;
DE AltName: Full=Caspase-activated DNase inhibitor that interacts with ASK1;
DE Short=CIIA;
DE AltName: Full=ESCRT-I complex subunit VPS28;
GN Name=Vps28;
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=BALB/cJ;
RX PubMed=14557248; DOI=10.1083/jcb.200303003;
RA Cho S.-G., Kim J.W., Lee Y.H., Hwang H.S., Kim M.S., Ryoo K., Kim M.J.,
RA Noh K.T., Kim E.K., Cho J.H., Yoon K.W., Cho E.G., Park H.S., Chi S.W.,
RA Lee M.J., Kang S.S., Ichijo H., Choi E.J.;
RT "Identification of a novel antiapoptotic protein that antagonizes ASK1 and
RT CAD activities.";
RL J. Cell Biol. 163:71-81(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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-I complex, a regulator of vesicular
CC trafficking process. {ECO:0000250}.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, a VPS37
CC protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry.
CC Interacts with TSG101, VPS37B, VPS37C, MVB12A and MVB12B. Component of
CC an ESCRT-I complex (endosomal sorting complex required for transport I)
CC which consists of TSG101, VPS28, VPS37A and UBAP1 in a 1:1:1:1
CC stoichiometry. Interacts WITH VPS36; the interaction mediates the
CC association with the ESCRT-II complex. Interacts with SNF8 and VPS25.
CC Interacts with CEP55 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9D1C8; O54788: Dffb; NbExp=6; IntAct=EBI-309205, EBI-7365197;
CC Q9D1C8; O35099: Map3k5; NbExp=3; IntAct=EBI-309205, EBI-777493;
CC Q9D1C8; Q99683: MAP3K5; Xeno; NbExp=5; IntAct=EBI-309205, EBI-476263;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Late endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS28 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00642, ECO:0000255|PROSITE-ProRule:PRU00645}.
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DR EMBL; AF373710; AAN71982.1; -; mRNA.
DR EMBL; AK003699; BAB22945.1; -; mRNA.
DR EMBL; BC013535; AAH13535.1; -; mRNA.
DR CCDS; CCDS27579.1; -.
DR RefSeq; NP_001292597.1; NM_001305668.1.
DR RefSeq; NP_080118.1; NM_025842.4.
DR AlphaFoldDB; Q9D1C8; -.
DR BMRB; Q9D1C8; -.
DR SMR; Q9D1C8; -.
DR BioGRID; 211806; 41.
DR IntAct; Q9D1C8; 40.
DR MINT; Q9D1C8; -.
DR iPTMnet; Q9D1C8; -.
DR PhosphoSitePlus; Q9D1C8; -.
DR EPD; Q9D1C8; -.
DR MaxQB; Q9D1C8; -.
DR PaxDb; Q9D1C8; -.
DR PeptideAtlas; Q9D1C8; -.
DR PRIDE; Q9D1C8; -.
DR ProteomicsDB; 300183; -.
DR Antibodypedia; 14872; 205 antibodies from 31 providers.
DR DNASU; 66914; -.
DR Ensembl; ENSMUST00000078803; ENSMUSP00000077856; ENSMUSG00000115987.
DR GeneID; 66914; -.
DR KEGG; mmu:66914; -.
DR UCSC; uc007wlc.2; mouse.
DR CTD; 51160; -.
DR MGI; MGI:1914164; Vps28.
DR VEuPathDB; HostDB:ENSMUSG00000115987; -.
DR GeneTree; ENSGT00390000007486; -.
DR HOGENOM; CLU_076417_2_0_1; -.
DR InParanoid; Q9D1C8; -.
DR OMA; CDEFPTV; -.
DR OrthoDB; 1281819at2759; -.
DR PhylomeDB; Q9D1C8; -.
DR TreeFam; TF313364; -.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 66914; 13 hits in 26 CRISPR screens.
DR ChiTaRS; Vps28; mouse.
DR PRO; PR:Q9D1C8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D1C8; protein.
DR Bgee; ENSMUSG00000115987; Expressed in ankle joint and 262 other tissues.
DR ExpressionAtlas; Q9D1C8; baseline and differential.
DR Genevisible; Q9D1C8; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0000813; C:ESCRT I complex; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; 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 GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
DR Gene3D; 1.20.120.1130; -; 1.
DR Gene3D; 1.20.1440.200; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR007143; Vps28.
DR InterPro; IPR017899; VPS28_C.
DR InterPro; IPR037206; VPS28_C_sf.
DR InterPro; IPR017898; VPS28_N.
DR InterPro; IPR038358; VPS28_N_sf.
DR PANTHER; PTHR12937; PTHR12937; 1.
DR Pfam; PF03997; VPS28; 1.
DR PIRSF; PIRSF017535; VPS28; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR SUPFAM; SSF140427; SSF140427; 1.
DR PROSITE; PS51310; VPS28_C; 1.
DR PROSITE; PS51313; VPS28_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..221
FT /note="Vacuolar protein sorting-associated protein 28
FT homolog"
FT /id="PRO_0000120952"
FT DOMAIN 13..120
FT /note="VPS28 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00645"
FT DOMAIN 124..220
FT /note="VPS28 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00642"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK41"
SQ SEQUENCE 221 AA; 25452 MW; DC144A4A27857245 CRC64;
MFHGIPATPG VGAPGNKPEL YEEVKLYKNA REREKYDNMA ELFAVVKTMQ ALEKAYIKDC
VTPNEYTAAC SRLLVQYKAA FRQVQGSEIS SIDEFCRKFR LDCPLAMERI KEDRPITIKD
DKGNLNRCIA DVVSLFITVM DKLRLEIRAM DEIQPDLREL METMHRMSHL PPDFEGRQTV
SQWLQTLSGM SASDELDDSQ VRQMLFDLES AYNAFNRFLH A
