P0C0A2 (VPS36_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar protein-sorting-associated protein 36

Alternative name(s):
ELL-associated protein of 45 kDa
ESCRT-II complex subunit VPS36

Gene names

Name:	Vps36
Synonyms:	Eap45

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3 By similarity.
Subunit structure	Component of a complex at least composed of ELL, SNF8/EAP30, VPS25/EAP20 and VPS36/EAP45. Component of the endosomal sorting complex required for transport II (ESCRT-II), composed of SNF8, VPS36 and two copies of VPS25. Interacts with VPS25, SNF8, TSG101 and VPS36 By similarity. Interacts (via GLUE domain) with ubiquitin By similarity. Interacts with RILPL1 (via the C-terminal domain); which recruits ESCRT-II to the endosome membranes By similarity. Interacts with ECM29 By similarity.
Subcellular location	Cytoplasm. Endosome By similarity. Late endosome By similarity. Membrane By similarity. Nucleus Probable. Note: Colocalizes with ubiquitinated proteins on late endosomes By similarity. Recruited to the endosome membrane to participate in vesicle formation By similarity.
Domain	The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates the binding to ubiquitin and phosphoinosides By similarity.
Sequence similarities	Belongs to the VPS36 family. Contains 1 GLUE C-terminal domain. Contains 1 GLUE N-terminal domain.

Ontologies

Keywords
Biological process	Protein transport Transcription Transcription regulation Transport
Cellular component	Cytoplasm Endosome Membrane Nucleus
Domain	Coiled coil
Ligand	Lipid-binding
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	late endosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 386	386	Vacuolar protein-sorting-associated protein 36		PRO_0000215224
Regions
	Domain	1 – 88	88	GLUE N-terminal
	Domain	105 – 138	34	GLUE C-terminal
	Coiled coil	160 – 185	26	Potential

Sequences

	Sequence		Length	Mass (Da)
	P0C0A2 [UniParc]. Last modified August 30, 2005. Version 1. Checksum: 292B6DCD8C53F04C	FASTA	386	43,718
	10 20 30 40 50 60 MDRFVWTSGL LEINETLVIQ QRGVRVYDGE EKIKFDAGTL LLSTHRLIWR DQKNNECCMA 70 80 90 100 110 120 IPLSQIVFIE EQAAGIGKSA KIVVHLHPAP PNKEPGPFQS SKNSYIKLSF KEHGQIEFYR 130 140 150 160 170 180 RLSEEMTQRR WETVPVSQSL QTKKGPQPGR IRAVGIVGIE RKLEEKRKET DKNISEAFED 190 200 210 220 230 240 LSKLMIQAKE MVELSKSIAN KIKEKQGDVT EDETIRFKSY LLSMGIANPV TRETYGSGTQ 250 260 270 280 290 300 YHMQLAKQLA GILQAPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEGLKLP 310 320 330 340 350 360 VRLRVFDSGV MVIELQTHKE EEMVASALET VSERGSLTSE EFAKLVGMSV LLAKERLLLA 370 380 EKMGHLCRDD SVEGLRFYPN LFMTQN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed: 15057822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"Cloning and characterization of ELL-associated proteins EAP45 and EAP20. a role for yeast EAP-like proteins in regulation of gene expression by glucose." Kamura T., Burian D., Khalili H., Schmidt S.L., Sato S., Liu W.-J., Conrad M.N., Conaway R.C., Conaway J.W., Shilatifard A. J. Biol. Chem. 276:16528-16533(2001) [PubMed: 11278625] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-46; 233-247 AND 357-362, IDENTIFICATION IN A COMPLEX WITH ELL; VPS25 AND SNF8.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03100673 Genomic DNA. No translation available. AABR03103040 Genomic DNA. No translation available. AABR03103985 Genomic DNA. No translation available.
IPI	IPI00194085.
UniGene	Rn.12707.
3D structure databases
ProteinModelPortal	P0C0A2.
SMR	P0C0A2. Positions 3-131.
ModBase	Search...
Protein-protein interaction databases
STRING	P0C0A2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	1309754. Vps36.
Phylogenomic databases
eggNOG	roNOG14204.
GeneTree	ENSGT00390000017209.
HOVERGEN	HBG083632.
InParanoid	P0C0A2.
OrthoDB	EOG4XPQG2.
Gene expression databases
ArrayExpress	P0C0A2.
Genevestigator	P0C0A2.
GermOnline	ENSRNOG00000012654. Rattus norvegicus.
Family and domain databases
InterPro	IPR007286. EAP30. IPR021648. VPS36_ESCRT-II. [Graphical view]
Pfam	PF04157. EAP30. 1 hit. PF11605. Vps36_ESCRT-II. 1 hit. [Graphical view]
PROSITE	PS51495. GLUE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

VPS36_RAT

Accession

Primary (citable) accession number: P0C0A2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	August 30, 2005
Last modified:	September 21, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program