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Protein

V-type proton ATPase subunit D

Gene

ATP6V1D

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium.By similarity1 Publication

GO - Molecular functioni

  1. ATPase activity, coupled to transmembrane movement of substances Source: InterPro

GO - Biological processi

  1. cellular iron ion homeostasis Source: Reactome
  2. cilium assembly Source: UniProtKB
  3. insulin receptor signaling pathway Source: Reactome
  4. interaction with host Source: Reactome
  5. phagosome maturation Source: Reactome
  6. protein localization to cilium Source: UniProtKB
  7. proton transport Source: UniProtKB-KW
  8. transferrin transport Source: Reactome
  9. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS02107-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit D
Short name:
V-ATPase subunit D
Alternative name(s):
V-ATPase 28 kDa accessory protein
Vacuolar proton pump subunit D
Gene namesi
Name:ATP6V1D
Synonyms:ATP6M, VATD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:13527. ATP6V1D.

Subcellular locationi

  1. Membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

  2. Note: Localizes to centrosome and the base of the cilium.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. lysosomal membrane Source: UniProtKB
  4. membrane Source: UniProtKB
  5. proton-transporting V-type ATPase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25157.

Polymorphism and mutation databases

BioMutaiATP6V1D.
DMDMi10720351.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247V-type proton ATPase subunit DPRO_0000144231Add
BLAST

Proteomic databases

MaxQBiQ9Y5K8.
PaxDbiQ9Y5K8.
PeptideAtlasiQ9Y5K8.
PRIDEiQ9Y5K8.

PTM databases

PhosphoSiteiQ9Y5K8.

Expressioni

Gene expression databases

BgeeiQ9Y5K8.
CleanExiHS_ATP6V1D.
ExpressionAtlasiQ9Y5K8. baseline and differential.
GenevestigatoriQ9Y5K8.

Organism-specific databases

HPAiHPA031515.
HPA057316.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). Interacts with SNX10; may play a role in ciliogenesis.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
VPS52Q8N1B43EBI-2684998,EBI-2799833

Protein-protein interaction databases

BioGridi119513. 27 interactions.
IntActiQ9Y5K8. 6 interactions.
STRINGi9606.ENSP00000216442.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5K8.
SMRiQ9Y5K8. Positions 8-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase D subunit family.Curated

Phylogenomic databases

eggNOGiCOG1394.
GeneTreeiENSGT00390000010770.
HOGENOMiHOG000230791.
HOVERGENiHBG000483.
InParanoidiQ9Y5K8.
KOiK02149.
OMAiQTAFMIL.
OrthoDBiEOG7QG46J.
PhylomeDBiQ9Y5K8.
TreeFamiTF300160.

Family and domain databases

InterProiIPR002699. V_ATPase_D.
[Graphical view]
PANTHERiPTHR11671. PTHR11671. 1 hit.
PfamiPF01813. ATP-synt_D. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00309. V_ATPase_subD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y5K8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGKDRIEIF PSRMAQTIMK ARLKGAQTGR NLLKKKSDAL TLRFRQILKK
60 70 80 90 100
IIETKMLMGE VMREAAFSLA EAKFTAGDFS TTVIQNVNKA QVKIRAKKDN
110 120 130 140 150
VAGVTLPVFE HYHEGTDSYE LTGLARGGEQ LAKLKRNYAK AVELLVELAS
160 170 180 190 200
LQTSFVTLDE AIKITNRRVN AIEHVIIPRI ERTLAYIITE LDEREREEFY
210 220 230 240
RLKKIQEKKK ILKEKSEKDL EQRRAAGEVL EPANLLAEEK DEDLLFE
Length:247
Mass (Da):28,263
Last modified:November 1, 1999 - v1
Checksum:i4185E5F6A74EFB1C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2358EVLEPANL → RCWSLLIF in AAD40384 (PubMed:10931946).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF145316 mRNA. Translation: AAD33953.1.
AF100741 mRNA. Translation: AAD40384.1.
AF104629 mRNA. Translation: AAG30726.1.
AK315784 mRNA. Translation: BAG38130.1.
CH471061 Genomic DNA. Translation: EAW80931.1.
BC001411 mRNA. Translation: AAH01411.1.
CCDSiCCDS9780.1.
RefSeqiNP_057078.1. NM_015994.3.
UniGeneiHs.272630.

Genome annotation databases

EnsembliENST00000216442; ENSP00000216442; ENSG00000100554.
ENST00000554087; ENSP00000451167; ENSG00000100554.
GeneIDi51382.
KEGGihsa:51382.
UCSCiuc001xjf.3. human.

Polymorphism and mutation databases

BioMutaiATP6V1D.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF145316 mRNA. Translation: AAD33953.1.
AF100741 mRNA. Translation: AAD40384.1.
AF104629 mRNA. Translation: AAG30726.1.
AK315784 mRNA. Translation: BAG38130.1.
CH471061 Genomic DNA. Translation: EAW80931.1.
BC001411 mRNA. Translation: AAH01411.1.
CCDSiCCDS9780.1.
RefSeqiNP_057078.1. NM_015994.3.
UniGeneiHs.272630.

3D structure databases

ProteinModelPortaliQ9Y5K8.
SMRiQ9Y5K8. Positions 8-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119513. 27 interactions.
IntActiQ9Y5K8. 6 interactions.
STRINGi9606.ENSP00000216442.

PTM databases

PhosphoSiteiQ9Y5K8.

Polymorphism and mutation databases

BioMutaiATP6V1D.
DMDMi10720351.

Proteomic databases

MaxQBiQ9Y5K8.
PaxDbiQ9Y5K8.
PeptideAtlasiQ9Y5K8.
PRIDEiQ9Y5K8.

Protocols and materials databases

DNASUi51382.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216442; ENSP00000216442; ENSG00000100554.
ENST00000554087; ENSP00000451167; ENSG00000100554.
GeneIDi51382.
KEGGihsa:51382.
UCSCiuc001xjf.3. human.

Organism-specific databases

CTDi51382.
GeneCardsiGC14M067761.
HGNCiHGNC:13527. ATP6V1D.
HPAiHPA031515.
HPA057316.
MIMi609398. gene.
neXtProtiNX_Q9Y5K8.
PharmGKBiPA25157.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1394.
GeneTreeiENSGT00390000010770.
HOGENOMiHOG000230791.
HOVERGENiHBG000483.
InParanoidiQ9Y5K8.
KOiK02149.
OMAiQTAFMIL.
OrthoDBiEOG7QG46J.
PhylomeDBiQ9Y5K8.
TreeFamiTF300160.

Enzyme and pathway databases

BioCyciMetaCyc:HS02107-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

ChiTaRSiATP6V1D. human.
GeneWikiiATP6V1D.
GenomeRNAii51382.
NextBioi54891.
PROiQ9Y5K8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5K8.
CleanExiHS_ATP6V1D.
ExpressionAtlasiQ9Y5K8. baseline and differential.
GenevestigatoriQ9Y5K8.

Family and domain databases

InterProiIPR002699. V_ATPase_D.
[Graphical view]
PANTHERiPTHR11671. PTHR11671. 1 hit.
PfamiPF01813. ATP-synt_D. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00309. V_ATPase_subD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Zhao Y., Cao H.Q., Wei Y.J., Jiang Y.X., Zhao X.W., Liu D.Q., Meng X.M., Liu Y.Q., Xu Y.Y., Sheng H., Liu S., Qiao M., Hui R.T., Ding J.F.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  3. "cDNA of human vacuolar H-ATPase subunit D (VATD) interacts with Rb."
    Quan L., Hong W., Shizhou A.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Trachea.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Placenta.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo."
    Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S., Lin S., Shu X., Pei D.
    Cell Res. 22:333-345(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CILIOGENESIS, INTERACTION WITH SNX10, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiVATD_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5K8
Secondary accession number(s): B2RE33, Q9Y688
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: April 29, 2015
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.