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Protein

Vesicle-associated membrane protein-associated protein A

Gene

Vapa

Organism
Mus musculus (Mouse)
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. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With OSBPL3, may regulate ER morphology. May play a role in vesicle trafficking.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1353561. Vapa.

Subcellular locationi

  • Endoplasmic reticulum membrane 1 Publication; Single-pass type IV membrane protein By similarity
  • Cell membrane By similarity; Single-pass type IV membrane protein Curated
  • Cell junctiontight junction By similarity
  • Nucleus membrane By similarity

  • 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.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 228227CytoplasmicSequence analysisAdd
BLAST
Transmembranei229 – 24921Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 249248Vesicle-associated membrane protein-associated protein APRO_0000213471Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei125 – 1251N6-acetyllysineBy similarity
Modified residuei214 – 2141PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9WV55.
MaxQBiQ9WV55.
PaxDbiQ9WV55.
PRIDEiQ9WV55.
TopDownProteomicsiQ9WV55.

PTM databases

iPTMnetiQ9WV55.
PhosphoSiteiQ9WV55.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9WV55.
GenevisibleiQ9WV55. MM.

Interactioni

Subunit structurei

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 OSBPL3 (phosphorylated form).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi206035. 4 interactions.
IntActiQ9WV55. 14 interactions.
MINTiMINT-4998482.
STRINGi10090.ENSMUSP00000024897.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 2612Combined sources
Beta strandi29 – 313Combined sources
Beta strandi35 – 406Combined sources
Beta strandi43 – 453Combined sources
Beta strandi47 – 548Combined sources
Beta strandi58 – 6710Combined sources
Beta strandi73 – 808Combined sources
Beta strandi95 – 1017Combined sources
Helixi109 – 1157Combined sources
Turni118 – 1203Combined sources
Beta strandi122 – 13110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRINMR-A8-141[»]
ProteinModelPortaliQ9WV55.
SMRiQ9WV55. Positions 8-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WV55.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 131118MSPPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili168 – 20740Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 MSP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0439. Eukaryota.
COG5066. LUCA.
GeneTreeiENSGT00390000006947.
HOGENOMiHOG000293182.
HOVERGENiHBG028551.
InParanoidiQ9WV55.
KOiK06096.
OMAiFEMPSEN.
OrthoDBiEOG7CK389.
PhylomeDBiQ9WV55.
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]

Sequencei

Sequence statusi: Complete.

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

Q9WV55-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASASGAMAK HEQILVLDPP SDLKFKGPFT DVVTTNLKLQ NPSDRKVCFK
60 70 80 90 100
VKTTAPRRYC VRPNSGIIDP GSIVTVSVML QPFDYDPNEK SKHKFMVQTI
110 120 130 140 150
FAPPNISDME AVWKEAKPDE LMDSKLRCVF EMPNENDKLN DMEPSKAVPL
160 170 180 190 200
NASKQDGPLP KPHSVSLNDT ETRKLMEECK RLQGEMMKLS EENRHLRDEG
210 220 230 240
LRLRKVAHSD KPGSTSAVSF RDNVTSPLPS LLVVIAAIFI GFFLGKFIL
Length:249
Mass (Da):27,855
Last modified:January 9, 2007 - v2
Checksum:iFE8F956C1F2C71CA
GO

Sequence cautioni

The sequence AAD45320.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB22868.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 112KH → ND in AAF23076 (Ref. 4) Curated
Sequence conflicti154 – 1541K → R in AAF23076 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157497 mRNA. Translation: AAD45320.1. Different initiation.
AK003576 mRNA. Translation: BAB22868.1. Different initiation.
AK167381 mRNA. Translation: BAE39474.1.
AK168824 mRNA. Translation: BAE40651.1.
AK159582 mRNA. Translation: BAE35202.1.
BC003866 mRNA. Translation: AAH03866.2.
AF115503 mRNA. Translation: AAF23076.1.
CCDSiCCDS37677.1.
RefSeqiNP_038961.2. NM_013933.3.
UniGeneiMm.266767.
Mm.476204.

Genome annotation databases

EnsembliENSMUST00000024897; ENSMUSP00000024897; ENSMUSG00000024091.
GeneIDi30960.
KEGGimmu:30960.
UCSCiuc008dgd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157497 mRNA. Translation: AAD45320.1. Different initiation.
AK003576 mRNA. Translation: BAB22868.1. Different initiation.
AK167381 mRNA. Translation: BAE39474.1.
AK168824 mRNA. Translation: BAE40651.1.
AK159582 mRNA. Translation: BAE35202.1.
BC003866 mRNA. Translation: AAH03866.2.
AF115503 mRNA. Translation: AAF23076.1.
CCDSiCCDS37677.1.
RefSeqiNP_038961.2. NM_013933.3.
UniGeneiMm.266767.
Mm.476204.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRINMR-A8-141[»]
ProteinModelPortaliQ9WV55.
SMRiQ9WV55. Positions 8-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206035. 4 interactions.
IntActiQ9WV55. 14 interactions.
MINTiMINT-4998482.
STRINGi10090.ENSMUSP00000024897.

PTM databases

iPTMnetiQ9WV55.
PhosphoSiteiQ9WV55.

Proteomic databases

EPDiQ9WV55.
MaxQBiQ9WV55.
PaxDbiQ9WV55.
PRIDEiQ9WV55.
TopDownProteomicsiQ9WV55.

Protocols and materials databases

DNASUi30960.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024897; ENSMUSP00000024897; ENSMUSG00000024091.
GeneIDi30960.
KEGGimmu:30960.
UCSCiuc008dgd.2. mouse.

Organism-specific databases

CTDi9218.
MGIiMGI:1353561. Vapa.

Phylogenomic databases

eggNOGiKOG0439. Eukaryota.
COG5066. LUCA.
GeneTreeiENSGT00390000006947.
HOGENOMiHOG000293182.
HOVERGENiHBG028551.
InParanoidiQ9WV55.
KOiK06096.
OMAiFEMPSEN.
OrthoDBiEOG7CK389.
PhylomeDBiQ9WV55.
TreeFamiTF317024.

Enzyme and pathway databases

ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiVapa. mouse.
EvolutionaryTraceiQ9WV55.
PROiQ9WV55.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WV55.
GenevisibleiQ9WV55. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse VAP33 is associated with the endoplasmic reticulum and microtubules."
    Skehel P.A., Fabian-Fine R., Kandel E.R.
    Proc. Natl. Acad. Sci. U.S.A. 97:1101-1106(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Tissue: Brain.
  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].
    Strain: C57BL/6J.
    Tissue: Embryo, Fetal liver and Placenta.
  3. "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: Mammary tumor.
  4. "Two forms of mammalian VAP33."
    Tang B.L., Low D.L.H., Lock M.L., Hong W.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-242.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 199-214, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "Solution structure of the MSP domain of mouse VAMP-associated protein A."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 8-141.

Entry informationi

Entry nameiVAPA_MOUSE
AccessioniPrimary (citable) accession number: Q9WV55
Secondary accession number(s): Q3TJM1, Q9QY77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 9, 2007
Last modified: June 8, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.