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Q9P0L0 (VAPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:VAPA
Synonyms:VAP33
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in vesicle trafficking. Ref.9 Ref.10

Subunit structure

Homodimer, and heterodimer with VAPB. Interacts with VAMP1, VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain of OCLN. Interacts with OSBPL1A. Interacts (via MSP domain) with ZFYVE27; may retain ZFYVE27 in the endoplasmic reticulum and regulate its function in cell projections formation. Interacts with OSBP. Interacts (via C-terminus) with RSAD2/viperin (via C-terminus). Interacts with HCV protein NS5A and NS5B. Interacts with IFITM3. Ref.1 Ref.6 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15

Subcellular location

Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Note: Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells. Ref.1 Ref.10

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the VAMP-associated protein (VAP) (TC 9.B.17) family. [View classification]

Contains 1 MSP domain.

Sequence caution

The sequence AAD09742.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAF72105.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BG488667 differs from that shown. Reason: Frameshift at positions 72, 207 and 241.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from mutant phenotype Ref.10. Source: UniProtKB

membrane fusion

Traceable author statement Ref.6. Source: ProtInc

neuron projection development

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

protein localization to endoplasmic reticulum

Inferred from mutant phenotype Ref.10. Source: UniProtKB

signal transduction

Inferred from mutant phenotype PubMed 12761501. Source: GOC

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid biosynthetic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.10. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

vesicle

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionprotein heterodimerization activity

Inferred from physical interaction PubMed 16227268Ref.7. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P279585EBI-1059156,EBI-6904388From a different organism.
Q034633EBI-1059156,EBI-8803426From a different organism.
EGFRP005332EBI-1059156,EBI-297353
OPRM1P353723EBI-1059156,EBI-2624570
ZFYVE27Q5T4F45EBI-1059156,EBI-3892947

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P0L0-1)

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.
Isoform 2 (identifier: Q9P0L0-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Vesicle-associated membrane protein-associated protein A
PRO_0000213470

Regions

Topological domain1 – 227227Cytoplasmic Potential
Transmembrane228 – 24821Helical; Anchor for type IV membrane protein; Potential
Domain14 – 131118MSP
Coiled coil169 – 20537 Potential

Amino acid modifications

Modified residue1251N6-acetyllysine Ref.11

Natural variations

Alternative sequence1391L → LGITPPGNAPTVTSMSSINN TVATPASYHTKDDPRGLSVL KQEKQK in isoform 2.
VSP_038648
Natural variant81M → T.
Corresponds to variant rs1044163 [ dbSNP | Ensembl ].
VAR_050440
Natural variant1041P → L.
Corresponds to variant rs1127666 [ dbSNP | Ensembl ].
VAR_050441

Experimental info

Mutagenesis941K → D: Alters interaction with ZFYVE27; when associated with D-96. Ref.10
Mutagenesis961M → D: Alters interaction with ZFYVE27; when associated with D-94. Ref.10
Sequence conflict10 – 112KH → ND in AAC26508. Ref.6
Sequence conflict10 – 112KH → ND in AAV38424. Ref.8
Sequence conflict1601P → S in AAF72105. Ref.2

Secondary structure

.......................... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 9, 2007. Version 3.
Checksum: 68B603F3A9FA5475

FASTA24927,893
        10         20         30         40         50         60 
MASASGAMAK HEQILVLDPP TDLKFKGPFT DVVTTNLKLR NPSDRKVCFK VKTTAPRRYC 

        70         80         90        100        110        120 
VRPNSGIIDP GSTVTVSVML QPFDYDPNEK SKHKFMVQTI FAPPNTSDME AVWKEAKPDE 

       130        140        150        160        170        180 
LMDSKLRCVF EMPNENDKLN DMEPSKAVPL NASKQDGPMP KPHSVSLNDT ETRKLMEECK 

       190        200        210        220        230        240 
RLQGEMMKLS EENRHLRDEG LRLRKVAHSD KPGSTSTASF RDNVTSPLPS LLVVIAAIFI 


GFFLGKFIL 

« Hide

Isoform 2 [UniParc].

Checksum: 8B2D033706621878
Show »

FASTA29432,614

References

« Hide 'large scale' references
[1]"VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction."
Lapierre L.A., Tuma P.L., Navarre J., Goldenring J.R., Anderson J.M.
J. Cell Sci. 112:3723-3732(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH OCLN.
Tissue: Liver.
[2]"Cloning and isolating human 33kDa Vamp-associated protein cDNA."
Zhou H.J., Huang X.W., Zhou Y., Hu S.L., Yuan J.G., Qiang B.Q.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-199 (ISOFORM 2).
Tissue: Lung.
[6]"Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP."
Weir M.L., Klip A., Trimble W.S.
Biochem. J. 333:247-251(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1), INTERACTION WITH VAMP1 AND VAMP2.
Tissue: Pancreatic islet.
[7]"Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins."
Nishimura Y., Hayashi M., Inada H., Tanaka T.
Biochem. Biophys. Res. Commun. 254:21-26(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1).
Tissue: B-cell.
[8]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-249 (ISOFORM 1).
[9]"VAP-A binds promiscuously to both v- and tSNAREs."
Weir M.L., Xie H., Klip A., Trimble W.S.
Biochem. Biophys. Res. Commun. 286:616-621(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VAPB; VAMP1; VAMP2; STX1A; BET1 AND SEC22C.
[10]"Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein."
Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I.
J. Biol. Chem. 284:13766-13777(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ZFYVE27, MUTAGENESIS OF LYS-94 AND MET-96, SUBCELLULAR LOCATION.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Viperin inhibits hepatitis C virus replication by interfering with binding of NS5A to host protein hVAP-33."
Wang S., Wu X., Pan T., Song W., Wang Y., Zhang F., Yuan Z.
J. Gen. Virol. 93:83-92(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RSAD2 AND HCV PROTEIN NS5A AND NS5B.
[14]"The antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry."
Amini-Bavil-Olyaee S., Choi Y.J., Lee J.H., Shi M., Huang I.C., Farzan M., Jung J.U.
Cell Host Microbe 13:452-464(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IFITM3.
[15]"Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies."
Furuita K., Jee J., Fukada H., Mishima M., Kojima C.
J. Biol. Chem. 285:12961-12970(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 11-135, INTERACTION WITH OSBP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_003565.4. NM_003574.5.
NP_919415.2. NM_194434.2.
UniGeneHs.165195.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-A11-135[»]
ProteinModelPortalQ9P0L0.
SMRQ9P0L0. Positions 9-135.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114651. 37 interactions.
IntActQ9P0L0. 44 interactions.
MINTMINT-109415.
STRING9606.ENSP00000345656.

PTM databases

PhosphoSiteQ9P0L0.

Polymorphism databases

DMDM122066680.

Proteomic databases

PaxDbQ9P0L0.
PRIDEQ9P0L0.

Protocols and materials databases

DNASU9218.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340541; ENSP00000345656; ENSG00000101558. [Q9P0L0-2]
ENST00000400000; ENSP00000382880; ENSG00000101558. [Q9P0L0-1]
GeneID9218.
KEGGhsa:9218.
UCSCuc002koj.3. human. [Q9P0L0-2]
uc002kok.3. human. [Q9P0L0-1]

Organism-specific databases

CTD9218.
GeneCardsGC18P009904.
H-InvDBHIX0115359.
HGNCHGNC:12648. VAPA.
HPAHPA009174.
MIM605703. gene.
neXtProtNX_Q9P0L0.
PharmGKBPA37272.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5066.
HOGENOMHOG000293182.
HOVERGENHBG028551.
KOK06096.
OMAFEMPSEN.
OrthoDBEOG7CK389.
PhylomeDBQ9P0L0.
TreeFamTF317024.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9P0L0.
BgeeQ9P0L0.
CleanExHS_VAPA.
GenevestigatorQ9P0L0.

Family and domain databases

Gene3D2.60.40.360. 1 hit.
InterProIPR000535. MSP_dom.
IPR008962. PapD-like.
IPR016763. Vesicle-associated_membrane.
[Graphical view]
PfamPF00635. Motile_Sperm. 1 hit.
[Graphical view]
PIRSFPIRSF019693. VAMP-associated. 1 hit.
SUPFAMSSF49354. SSF49354. 1 hit.
PROSITEPS50202. MSP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVAPA. human.
EvolutionaryTraceQ9P0L0.
GeneWikiVAPA.
GenomeRNAi9218.
NextBio34557.
PMAP-CutDBQ9P0L0.
PROQ9P0L0.
SOURCESearch...

Entry information

Entry nameVAPA_HUMAN
AccessionPrimary (citable) accession number: Q9P0L0
Secondary accession number(s): A6NDZ0 expand/collapse secondary AC list , D3DUI3, O75453, Q5U0E7, Q9UBZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM