VPS36_RAT
ID VPS36_RAT Reviewed; 386 AA.
AC P0C0A2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Vacuolar protein-sorting-associated protein 36;
DE AltName: Full=ELL-associated protein of 45 kDa;
DE AltName: Full=ESCRT-II complex subunit VPS36;
GN Name=Vps36; Synonyms=Eap45;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PROTEIN SEQUENCE OF 35-46; 233-247 AND 357-362, AND IDENTIFICATION IN A
RP COMPLEX WITH ELL; VPS25 AND SNF8.
RX PubMed=11278625; DOI=10.1074/jbc.m010142200;
RA Kamura T., Burian D., Khalili H., Schmidt S.L., Sato S., Liu W.-J.,
RA Conrad M.N., Conaway R.C., Conaway J.W., Shilatifard A.;
RT "Cloning and characterization of ELL-associated proteins EAP45 and EAP20. a
RT role for yeast EAP-like proteins in regulation of gene expression by
RT glucose.";
RL J. Biol. Chem. 276:16528-16533(2001).
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. Its ability to
CC bind ubiquitin probably plays a role in endosomal sorting of
CC ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex
CC may also play a role in transcription regulation, possibly via its
CC interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3 (By
CC similarity). {ECO:0000250|UniProtKB:Q86VN1,
CC ECO:0000250|UniProtKB:Q91XD6}.
CC -!- SUBUNIT: Component of a complex at least composed of ELL, SNF8/EAP30,
CC VPS25/EAP20 and VPS36/EAP45 (PubMed:11278625). Component of the
CC endosomal sorting complex required for transport II (ESCRT-II),
CC composed of SNF8, VPS36 and two copies of VPS25 (By similarity).
CC Interacts with VPS25, SNF8, TSG101 and CHMP6 (By similarity). Interacts
CC (via GLUE domain) with ubiquitin (By similarity). Interacts with RILPL1
CC (via the C-terminal domain); which recruits ESCRT-II to the endosome
CC membranes (By similarity). Interacts with ECPAS (By similarity).
CC {ECO:0000250|UniProtKB:Q86VN1, ECO:0000250|UniProtKB:Q91XD6,
CC ECO:0000269|PubMed:11278625}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome {ECO:0000250}. Late endosome
CC {ECO:0000250|UniProtKB:Q91XD6}. Membrane {ECO:0000250}. Nucleus
CC {ECO:0000305}. Note=Colocalizes with ubiquitinated proteins on late
CC endosomes. Recruited to the endosome membrane to participate in vesicle
CC formation. {ECO:0000250|UniProtKB:Q91XD6}.
CC -!- DOMAIN: The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates
CC binding to ubiquitin and phosphoinosides.
CC {ECO:0000250|UniProtKB:Q91XD6}.
CC -!- SIMILARITY: Belongs to the VPS36 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03100673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03103040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03103985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C0A2; -.
DR SMR; P0C0A2; -.
DR IntAct; P0C0A2; 2.
DR STRING; 10116.ENSRNOP00000016995; -.
DR jPOST; P0C0A2; -.
DR PaxDb; P0C0A2; -.
DR PRIDE; P0C0A2; -.
DR RGD; 1309754; Vps36.
DR eggNOG; KOG2760; Eukaryota.
DR InParanoid; P0C0A2; -.
DR PhylomeDB; P0C0A2; -.
DR Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR PRO; PR:P0C0A2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0000814; C:ESCRT II complex; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0031902; C:late endosome membrane; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
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; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR021648; GLUE_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR037855; Vps36.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13128; PTHR13128; 1.
DR Pfam; PF04157; EAP30; 1.
DR Pfam; PF11605; Vps36_ESCRT-II; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR PROSITE; PS51495; GLUE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Direct protein sequencing; Endosome; Lipid-binding;
KW Membrane; Nucleus; Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..386
FT /note="Vacuolar protein-sorting-associated protein 36"
FT /id="PRO_0000215224"
FT DOMAIN 1..88
FT /note="GLUE N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT DOMAIN 105..138
FT /note="GLUE C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT COILED 160..185
FT /evidence="ECO:0000255"
SQ SEQUENCE 386 AA; 43718 MW; 292B6DCD8C53F04C CRC64;
MDRFVWTSGL LEINETLVIQ QRGVRVYDGE EKIKFDAGTL LLSTHRLIWR DQKNNECCMA
IPLSQIVFIE EQAAGIGKSA KIVVHLHPAP PNKEPGPFQS SKNSYIKLSF KEHGQIEFYR
RLSEEMTQRR WETVPVSQSL QTKKGPQPGR IRAVGIVGIE RKLEEKRKET DKNISEAFED
LSKLMIQAKE MVELSKSIAN KIKEKQGDVT EDETIRFKSY LLSMGIANPV TRETYGSGTQ
YHMQLAKQLA GILQAPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEGLKLP
VRLRVFDSGV MVIELQTHKE EEMVASALET VSERGSLTSE EFAKLVGMSV LLAKERLLLA
EKMGHLCRDD SVEGLRFYPN LFMTQN
