Q91XD6 (VPS36_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar protein-sorting-associated protein 36

Alternative name(s):
ESCRT-II complex subunit VPS36

Gene names

Name:

Vps36

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 By similarity. 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. 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 By similarity. Endosome By similarity. Late endosome By similarity. Membrane By similarity. Nucleus By similarity. 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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endosomal transport Inferred by curator PubMed 15755741. Source: MGI 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 direct assay PubMed 15755741. Source: MGI lysosome Inferred from direct assay PubMed 15755741. Source: MGI membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphatidylinositol-3-phosphate binding Inferred from electronic annotation. Source: InterPro ubiquitin binding Inferred from direct assay PubMed 15755741. Source: MGI
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_0000215223

Regions

Domain

1 – 88

88

GLUE N-terminal

Domain

105 – 138

34

GLUE C-terminal

Coiled coil

160 – 185

26

Potential

Secondary structure

1

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386

Helix Strand Turn

Details...

Beta strand

17 – 30

14

Beta strand

37 – 45

9

Beta strand

47 – 53

7

Helix

54 – 56

3

Beta strand

63 – 65

3

Beta strand

68 – 71

4

Beta strand

82 – 85

4

Beta strand

106 – 113

8

Turn

115 – 117

3

Helix

118 – 127

10

Sequences

	Sequence		Length	Mass (Da)
	Q91XD6 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0036479499DD89C8	FASTA	386	43,736
	10 20 30 40 50 60 MDRFVWTSGL LEINETLVIQ QRGVRVYDGE EKIKFDAGTL LLSTHRLIWR DQKNNECCMA 70 80 90 100 110 120 IPLSQIVFIE EQAAGIGKSA KIVVHLHPAP SNKEPGPFQS SKNSYIRLSF KEHGQIEFYR 130 140 150 160 170 180 RLSEEMTQRR WETVPVSQSL QTNKGPQPGR VRAVGIVGIE RKLEEKRKET DKNISEAFED 190 200 210 220 230 240 LSKLMIKAKE MVELSKSIAN KIKEKQGDVT EDETIRFKSY LLSMGIANPV TRETYGSGTQ 250 260 270 280 290 300 YHMQLAKQLA GILQAPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEALKLP 310 320 330 340 350 360 IRLRVFDSGV MVIELQTHKE EEMVASALET VSERGSLTSE EFAKLVGMSV LLAKERLLLA 370 380 EKMGHLCRDD SVEGLRFYPN LFMTQN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-161. Strain: C57BL/6J. Tissue: Stomach.
[3]	"Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain." Hirano S., Suzuki N., Slagsvold T., Kawasaki M., Trambaiolo D., Kato R., Stenmark H., Wakatsuki S. Nat. Struct. Mol. Biol. 13:1031-1032(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 1-139 IN COMPLEX WITH RPS27A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BC010811 mRNA. Translation: AAH10811.1.
AK008946 mRNA. Translation: BAB25984.1.

IPI

IPI00129014.

RefSeq

NP_081614.1. NM_027338.1.

UniGene

Mm.41453.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DX5	X-ray	3.35	A	1-139	[»]

ProteinModelPortal

Q91XD6.

SMR

Q91XD6. Positions 3-131, 172-386.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29247N.

PTM databases

PhosphoSite

Q91XD6.

Proteomic databases

PaxDb

Q91XD6.

PRIDE

Q91XD6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000033866; ENSMUSP00000033866; ENSMUSG00000031479.

GeneID

70160.

KEGG

mmu:70160.

Organism-specific databases

CTD

51028.

MGI

MGI:1917410. Vps36.

Phylogenomic databases

eggNOG

NOG262969.

GeneTree

ENSGT00390000017209.

HOGENOM

HOG000006822.

HOVERGEN

HBG083632.

InParanoid

Q91XD6.

KO

K12190.

OMA

CCIAIPL.

OrthoDB

EOG4XPQG2.

Gene expression databases

ArrayExpress

Q91XD6.

Bgee

Q91XD6.

CleanEx

MM_VPS36.

Genevestigator

Q91XD6.

GermOnline

ENSMUSG00000031479. Mus musculus.

Family and domain databases

Gene3D

1.10.10.10. 2 hits.

InterPro

IPR007286. EAP30.
IPR021648. VPS36_GLUE.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF04157. EAP30. 1 hit.
PF11605. Vps36_ESCRT-II. 1 hit.
[Graphical view]

PROSITE

PS51495. GLUE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q91XD6.

NextBio

331106.

SOURCE

Search...

Entry information

Entry name

VPS36_MOUSE

Accession

Primary (citable) accession number: Q91XD6
Secondary accession number(s): Q9CVA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program