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Protein

Vesicle-associated membrane protein-associated protein A

Gene

VAPA

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

Functioni

Binds to OSBPL3, which mediates recruitment of VAPA to plasma membrane sites (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:25447204). With OSBPL3, may regulate ER morphology (PubMed:16143324). May play a role in vesicle trafficking (PubMed:11511104, PubMed:19289470).4 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • FFAT motif binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • signal transducer activity Source: UniProtKB

GO - Biological processi

  • cell death Source: UniProtKB
  • COPII-coated vesicle budding Source: UniProtKB
  • ER to Golgi vesicle-mediated transport Source: UniProtKB
  • membrane fusion Source: ProtInc
  • negative regulation by host of viral genome replication Source: AgBase
  • neuron projection development Source: UniProtKB
  • positive regulation by host of viral genome replication Source: AgBase
  • positive regulation by host of viral release from host cell Source: AgBase
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • protein localization to endoplasmic reticulum Source: UniProtKB
  • sphingolipid biosynthetic process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101558-MONOMER.
ReactomeiR-HSA-1660661. Sphingolipid de novo biosynthesis.
R-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-associated membrane protein-associated protein A
Short name:
VAMP-A
Short name:
VAMP-associated protein A
Short name:
VAP-A
Alternative name(s):
33 kDa VAMP-associated protein
Short name:
VAP-33
Gene namesi
Name:VAPA
Synonyms:VAP33
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:12648. VAPA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 227CytoplasmicSequence analysisAdd BLAST226
Transmembranei228 – 248Helical; Anchor for type IV membrane proteinSequence analysisAdd BLAST21

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB-SubCell
  • cell-cell adherens junction Source: BHF-UCL
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • Golgi membrane Source: GOC
  • integral component of membrane Source: UniProtKB-KW
  • microtubule cytoskeleton Source: Ensembl
  • nuclear membrane Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endoplasmic reticulum, Membrane, Nucleus, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi94K → D: Alters interaction with ZFYVE27; when associated with D-96. 1 Publication1
Mutagenesisi96M → D: Alters interaction with ZFYVE27; when associated with D-94. 1 Publication1

Organism-specific databases

DisGeNETi9218.
OpenTargetsiENSG00000101558.
PharmGKBiPA37272.

Polymorphism and mutation databases

BioMutaiVAPA.
DMDMi122066680.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002134702 – 249Vesicle-associated membrane protein-associated protein AAdd BLAST248

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei125N6-acetyllysineCombined sources1
Modified residuei166PhosphoserineCombined sources1
Modified residuei170PhosphothreonineCombined sources1
Modified residuei214PhosphoserineCombined sources1
Modified residuei216PhosphoserineCombined sources1
Modified residuei219PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9P0L0.
MaxQBiQ9P0L0.
PeptideAtlasiQ9P0L0.
PRIDEiQ9P0L0.
TopDownProteomicsiQ9P0L0-1. [Q9P0L0-1]
Q9P0L0-2. [Q9P0L0-2]

PTM databases

iPTMnetiQ9P0L0.
PhosphoSitePlusiQ9P0L0.
SwissPalmiQ9P0L0.

Miscellaneous databases

PMAP-CutDBQ9P0L0.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000101558.
CleanExiHS_VAPA.
ExpressionAtlasiQ9P0L0. baseline and differential.
GenevisibleiQ9P0L0. HS.

Organism-specific databases

HPAiHPA009174.

Interactioni

Subunit structurei

Homodimer, and heterodimer with VAPB (PubMed:11511104). Interacts with VAMP1, VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain of OCLN (PubMed:11511104, PubMed:9657962, PubMed:10523508). Interacts with OSBPL1A (By similarity). Interacts (via MSP domain) with ZFYVE27; may retain ZFYVE27 in the endoplasmic reticulum and regulate its function in cell projections formation (PubMed:19289470, PubMed:21976701). Interacts with OSBP (PubMed:20178991). Interacts (via C-terminus) with RSAD2/viperin (via C-terminus) (PubMed:21957124). Interacts with HCV protein NS5A and NS5B (PubMed:21957124). Interacts with IFITM3 (PubMed:23601107). Interacts with OSBPL3 (phosphorylated form) (PubMed:16143324, PubMed:25447204). Interacts with KIF5A in a ZFYVE27-dependent manner (PubMed:21976701).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279587EBI-1059156,EBI-8753518From a different organism.
Q034634EBI-1059156,EBI-8803426From a different organism.
Q99IB83EBI-1059156,EBI-9096996From a different organism.
EGFRP005332EBI-1059156,EBI-297353
OPRM1P353723EBI-1059156,EBI-2624570
OSBPL2Q9H1P33EBI-1059156,EBI-2828285
STARD3Q14849-14EBI-1059156,EBI-9819369
VAPBO952922EBI-1059156,EBI-1188298
VAPBO95292-12EBI-1059156,EBI-9350848
YIF1AO950703EBI-1059156,EBI-2799703
ZFYVE27Q5T4F45EBI-1059156,EBI-3892947

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • FFAT motif binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi114651. 249 interactors.
DIPiDIP-41135N.
IntActiQ9P0L0. 188 interactors.
MINTiMINT-109415.

Structurei

Secondary structure

1249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 21Combined sources8
Beta strandi23 – 27Combined sources5
Beta strandi33 – 40Combined sources8
Beta strandi43 – 45Combined sources3
Beta strandi47 – 54Combined sources8
Turni56 – 58Combined sources3
Beta strandi59 – 63Combined sources5
Beta strandi65 – 68Combined sources4
Beta strandi73 – 80Combined sources8
Beta strandi94 – 101Combined sources8
Helixi109 – 115Combined sources7
Turni118 – 120Combined sources3
Beta strandi122 – 131Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-A11-135[»]
ProteinModelPortaliQ9P0L0.
SMRiQ9P0L0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P0L0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 131MSPPROSITE-ProRule annotationAdd BLAST118

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili169 – 205Sequence analysisAdd BLAST37

Sequence similaritiesi

Contains 1 MSP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000006947.
HOGENOMiHOG000293182.
HOVERGENiHBG028551.
InParanoidiQ9P0L0.
KOiK06096.
OMAiFEMPSEN.
OrthoDBiEOG091G0KJ2.
PhylomeDBiQ9P0L0.
TreeFamiTF317024.

Family and domain databases

Gene3Di2.60.40.360. 1 hit.
InterProiIPR000535. MSP_dom.
IPR008962. PapD-like.
IPR016763. VAP.
IPR030229. VAPA.
[Graphical view]
PANTHERiPTHR10809. PTHR10809. 1 hit.
PTHR10809:SF40. PTHR10809:SF40. 1 hit.
PfamiPF00635. Motile_Sperm. 1 hit.
[Graphical view]
PIRSFiPIRSF019693. VAMP-associated. 1 hit.
SUPFAMiSSF49354. SSF49354. 1 hit.
PROSITEiPS50202. MSP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P0L0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASASGAMAK HEQILVLDPP TDLKFKGPFT DVVTTNLKLR NPSDRKVCFK
60 70 80 90 100
VKTTAPRRYC VRPNSGIIDP GSTVTVSVML QPFDYDPNEK SKHKFMVQTI
110 120 130 140 150
FAPPNTSDME AVWKEAKPDE LMDSKLRCVF EMPNENDKLN DMEPSKAVPL
160 170 180 190 200
NASKQDGPMP KPHSVSLNDT ETRKLMEECK RLQGEMMKLS EENRHLRDEG
210 220 230 240
LRLRKVAHSD KPGSTSTASF RDNVTSPLPS LLVVIAAIFI GFFLGKFIL
Length:249
Mass (Da):27,893
Last modified:January 9, 2007 - v3
Checksum:i68B603F3A9FA5475
GO
Isoform 2 (identifier: Q9P0L0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     139-139: L → LGITPPGNAPTVTSMSSINNTVATPASYHTKDDPRGLSVLKQEKQK

Show »
Length:294
Mass (Da):32,614
Checksum:i8B2D033706621878
GO

Sequence cautioni

The sequence AAD09742 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF72105 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BG488667 differs from that shown. Reason: Frameshift at positions 72, 207 and 241.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10 – 11KH → ND in AAC26508 (PubMed:9657962).Curated2
Sequence conflicti10 – 11KH → ND in AAV38424 (Ref. 8) Curated2
Sequence conflicti160P → S in AAF72105 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0504408M → T.Corresponds to variant rs1044163dbSNPEnsembl.1
Natural variantiVAR_050441104P → L.Corresponds to variant rs1127666dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_038648139L → LGITPPGNAPTVTSMSSINN TVATPASYHTKDDPRGLSVL KQEKQK in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044670 mRNA. Translation: AAD09742.1. Different initiation.
AF154847 mRNA. Translation: AAF72105.1. Different initiation.
AC006238 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01591.1.
CH471113 Genomic DNA. Translation: EAX01592.1.
BC002992 mRNA. Translation: AAH02992.2.
BG488667 mRNA. No translation available.
AF057358 mRNA. Translation: AAC26508.1.
AF086627 mRNA. Translation: AAD13576.1.
BT019618 mRNA. Translation: AAV38424.1.
CCDSiCCDS11847.2. [Q9P0L0-2]
CCDS11848.2. [Q9P0L0-1]
RefSeqiNP_003565.4. NM_003574.5. [Q9P0L0-2]
NP_919415.2. NM_194434.2. [Q9P0L0-1]
UniGeneiHs.165195.

Genome annotation databases

EnsembliENST00000340541; ENSP00000345656; ENSG00000101558. [Q9P0L0-2]
ENST00000400000; ENSP00000382880; ENSG00000101558. [Q9P0L0-1]
GeneIDi9218.
KEGGihsa:9218.
UCSCiuc002koj.4. human. [Q9P0L0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044670 mRNA. Translation: AAD09742.1. Different initiation.
AF154847 mRNA. Translation: AAF72105.1. Different initiation.
AC006238 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01591.1.
CH471113 Genomic DNA. Translation: EAX01592.1.
BC002992 mRNA. Translation: AAH02992.2.
BG488667 mRNA. No translation available.
AF057358 mRNA. Translation: AAC26508.1.
AF086627 mRNA. Translation: AAD13576.1.
BT019618 mRNA. Translation: AAV38424.1.
CCDSiCCDS11847.2. [Q9P0L0-2]
CCDS11848.2. [Q9P0L0-1]
RefSeqiNP_003565.4. NM_003574.5. [Q9P0L0-2]
NP_919415.2. NM_194434.2. [Q9P0L0-1]
UniGeneiHs.165195.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-A11-135[»]
ProteinModelPortaliQ9P0L0.
SMRiQ9P0L0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114651. 249 interactors.
DIPiDIP-41135N.
IntActiQ9P0L0. 188 interactors.
MINTiMINT-109415.

PTM databases

iPTMnetiQ9P0L0.
PhosphoSitePlusiQ9P0L0.
SwissPalmiQ9P0L0.

Polymorphism and mutation databases

BioMutaiVAPA.
DMDMi122066680.

Proteomic databases

EPDiQ9P0L0.
MaxQBiQ9P0L0.
PeptideAtlasiQ9P0L0.
PRIDEiQ9P0L0.
TopDownProteomicsiQ9P0L0-1. [Q9P0L0-1]
Q9P0L0-2. [Q9P0L0-2]

Protocols and materials databases

DNASUi9218.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340541; ENSP00000345656; ENSG00000101558. [Q9P0L0-2]
ENST00000400000; ENSP00000382880; ENSG00000101558. [Q9P0L0-1]
GeneIDi9218.
KEGGihsa:9218.
UCSCiuc002koj.4. human. [Q9P0L0-1]

Organism-specific databases

CTDi9218.
DisGeNETi9218.
GeneCardsiVAPA.
H-InvDBHIX0115359.
HGNCiHGNC:12648. VAPA.
HPAiHPA009174.
MIMi605703. gene.
neXtProtiNX_Q9P0L0.
OpenTargetsiENSG00000101558.
PharmGKBiPA37272.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000006947.
HOGENOMiHOG000293182.
HOVERGENiHBG028551.
InParanoidiQ9P0L0.
KOiK06096.
OMAiFEMPSEN.
OrthoDBiEOG091G0KJ2.
PhylomeDBiQ9P0L0.
TreeFamiTF317024.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000101558-MONOMER.
ReactomeiR-HSA-1660661. Sphingolipid de novo biosynthesis.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiVAPA. human.
EvolutionaryTraceiQ9P0L0.
GeneWikiiVAPA.
GenomeRNAii9218.
PMAP-CutDBQ9P0L0.
PROiQ9P0L0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101558.
CleanExiHS_VAPA.
ExpressionAtlasiQ9P0L0. baseline and differential.
GenevisibleiQ9P0L0. HS.

Family and domain databases

Gene3Di2.60.40.360. 1 hit.
InterProiIPR000535. MSP_dom.
IPR008962. PapD-like.
IPR016763. VAP.
IPR030229. VAPA.
[Graphical view]
PANTHERiPTHR10809. PTHR10809. 1 hit.
PTHR10809:SF40. PTHR10809:SF40. 1 hit.
PfamiPF00635. Motile_Sperm. 1 hit.
[Graphical view]
PIRSFiPIRSF019693. VAMP-associated. 1 hit.
SUPFAMiSSF49354. SSF49354. 1 hit.
PROSITEiPS50202. MSP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVAPA_HUMAN
AccessioniPrimary (citable) accession number: Q9P0L0
Secondary accession number(s): A6NDZ0
, D3DUI3, O75453, Q5U0E7, Q9UBZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 9, 2007
Last modified: November 30, 2016
This is version 158 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.