UniProt Accession

 VATD_MOUSE; P57746 

Genbank Protein ID

 AF298810; BC033457 

Genbank Nucleotide ID

 AAG30225.1; AAH33457.1 

Protein Name

 V-type proton ATPase subunit D 

Protein Synonyms/Alias

 V-ATPase subunit D; V-ATPase 28 kDa accessory protein; Vacuolar proton pump subunit D 

Gene Name

 Atp6v1d 

Gene Synonyms/Alias

 Atp6m; Vatd 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
20	RMAQTIMKARLKGAQ	ubiquitination	[1]
89	TVIQNVNKAQVKIRA	ubiquitination	[1]
98	QVKIRAKKDNVAGVT	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

Functional Description

 Subunit of the peripheral V1 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity). 

Sequence Annotation

  

Keyword

 Cilium biogenesis/degradation; Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Reference proteome; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 247 AA 

Protein Sequence

Gene Ontology

 GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IEA:Compara.
 GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
 GO:0042384; P:cilium assembly; ISS:UniProtKB.
 GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
 GO:0015992; P:proton transport; IEA:UniProtKB-KW. 

Interpro

 IPR002699; V_ATPase_D. 

Pfam

 PF01813; ATP-synt_D 

SMART

  

PROSITE

  

PRINTS