GenomeNet

Database: UniProt
Entry: Q9WV55
LinkDB: Q9WV55
Original site: Q9WV55 
ID   VAPA_MOUSE              Reviewed;         249 AA.
AC   Q9WV55; Q3TJM1; Q9QY77;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   17-JUN-2020, entry version 170.
DE   RecName: Full=Vesicle-associated membrane protein-associated protein A;
DE            Short=VAMP-A;
DE            Short=VAMP-associated protein A;
DE            Short=VAP-A;
DE   AltName: Full=33 kDa VAMP-associated protein;
DE            Short=VAP-33;
GN   Name=Vapa; Synonyms=Vap33;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   TISSUE=Brain;
RX   PubMed=10655491; DOI=10.1073/pnas.97.3.1101;
RA   Skehel P.A., Fabian-Fine R., Kandel E.R.;
RT   "Mouse VAP33 is associated with the endoplasmic reticulum and
RT   microtubules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:1101-1106(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Fetal liver, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-242.
RA   Tang B.L., Low D.L.H., Lock M.L., Hong W.;
RT   "Two forms of mammalian VAP33.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 199-214, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   INTERACTION WITH ZFYVE27.
RX   PubMed=24251978; DOI=10.1111/gtc.12109;
RA   Ohnishi T., Shirane M., Hashimoto Y., Saita S., Nakayama K.I.;
RT   "Identification and characterization of a neuron-specific isoform of
RT   protrudin.";
RL   Genes Cells 19:97-111(2014).
RN   [9]
RP   STRUCTURE BY NMR OF 8-141.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the MSP domain of mouse VAMP-associated protein A.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Binds to OSBPL3, which mediates recruitment of VAPA to plasma
CC       membrane sites. The ORP3-VAPA complex stimulates RRAS signaling which
CC       in turn attenuates integrin beta-1 (ITGB1) activation at the cell
CC       surface. With OSBPL3, may regulate ER morphology. May play a role in
CC       vesicle trafficking. {ECO:0000250|UniProtKB:Q9P0L0}.
CC   -!- SUBUNIT: Homodimer, and heterodimer with VAPB. Interacts with VAMP1,
CC       VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain of OCLN.
CC       Interacts with OSBPL1A (By similarity). Interacts (via MSP domain) with
CC       ZFYVE27 (PubMed:24251978). May retain ZFYVE27 in the endoplasmic
CC       reticulum and regulate its function in cell projections formation.
CC       Interacts with OSBP. Interacts (via C-terminus) with RSAD2/viperin (via
CC       C-terminus). Interacts with OSBPL3 (phosphorylated form). Interacts
CC       with KIF5A in a ZFYVE27-dependent manner (By similarity). Interacts
CC       with STARD3 (via FFAT motif) (By similarity). Interacts with STARD3NL
CC       (via FFAT motif) (By similarity). Interacts with CERT1 (By similarity).
CC       Interacts with PLEKHA3 and SACM1L to form a ternary complex (By
CC       similarity). Interacts with VPS13A (via FFAT motif) (By similarity).
CC       {ECO:0000250|UniProtKB:Q9P0L0, ECO:0000250|UniProtKB:Q9Z270,
CC       ECO:0000269|PubMed:24251978}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:10655491}; Single-pass type IV membrane protein
CC       {ECO:0000250|UniProtKB:Q9P0L0}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein
CC       {ECO:0000305}. Cell junction, tight junction
CC       {ECO:0000250|UniProtKB:Q9P0L0}. Nucleus membrane
CC       {ECO:0000250|UniProtKB:Q9Z270}. Note=Present in the plasma membrane and
CC       in intracellular vesicles, together with SNARE proteins. May also
CC       associate with the cytoskeleton. Colocalizes with OCLN at the tight
CC       junction in polarized epithelial cells. {ECO:0000250|UniProtKB:Q9P0L0}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD45320.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB22868.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AF157497; AAD45320.1; ALT_INIT; mRNA.
DR   EMBL; AK003576; BAB22868.1; ALT_INIT; mRNA.
DR   EMBL; AK167381; BAE39474.1; -; mRNA.
DR   EMBL; AK168824; BAE40651.1; -; mRNA.
DR   EMBL; AK159582; BAE35202.1; -; mRNA.
DR   EMBL; BC003866; AAH03866.2; -; mRNA.
DR   EMBL; AF115503; AAF23076.1; -; mRNA.
DR   CCDS; CCDS37677.1; -.
DR   RefSeq; NP_038961.2; NM_013933.3.
DR   PDB; 2CRI; NMR; -; A=8-141.
DR   PDBsum; 2CRI; -.
DR   SMR; Q9WV55; -.
DR   BioGRID; 206035; 9.
DR   ComplexPortal; CPX-507; Vapa-Osbp complex.
DR   IntAct; Q9WV55; 14.
DR   MINT; Q9WV55; -.
DR   STRING; 10090.ENSMUSP00000024897; -.
DR   iPTMnet; Q9WV55; -.
DR   PhosphoSitePlus; Q9WV55; -.
DR   SwissPalm; Q9WV55; -.
DR   EPD; Q9WV55; -.
DR   jPOST; Q9WV55; -.
DR   MaxQB; Q9WV55; -.
DR   PaxDb; Q9WV55; -.
DR   PeptideAtlas; Q9WV55; -.
DR   PRIDE; Q9WV55; -.
DR   TopDownProteomics; Q9WV55; -.
DR   Antibodypedia; 2287; 274 antibodies.
DR   DNASU; 30960; -.
DR   Ensembl; ENSMUST00000024897; ENSMUSP00000024897; ENSMUSG00000024091.
DR   GeneID; 30960; -.
DR   KEGG; mmu:30960; -.
DR   UCSC; uc008dgd.2; mouse.
DR   CTD; 9218; -.
DR   MGI; MGI:1353561; Vapa.
DR   eggNOG; KOG0439; Eukaryota.
DR   eggNOG; COG5066; LUCA.
DR   GeneTree; ENSGT00940000154799; -.
DR   HOGENOM; CLU_032848_0_1_1; -.
DR   InParanoid; Q9WV55; -.
DR   KO; K06096; -.
DR   OMA; TTQVEIC; -.
DR   OrthoDB; 1332028at2759; -.
DR   PhylomeDB; Q9WV55; -.
DR   TreeFam; TF317024; -.
DR   Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   BioGRID-ORCS; 30960; 2 hits in 14 CRISPR screens.
DR   ChiTaRS; Vapa; mouse.
DR   EvolutionaryTrace; Q9WV55; -.
DR   PRO; PR:Q9WV55; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9WV55; protein.
DR   Bgee; ENSMUSG00000024091; Expressed in metanephric cortical collecting duct and 287 other tissues.
DR   ExpressionAtlas; Q9WV55; baseline and differential.
DR   Genevisible; Q9WV55; MM.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0033149; F:FFAT motif binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR   GO; GO:0090114; P:COPII-coated vesicle budding; ISO:MGI.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR   GO; GO:0044828; P:negative regulation by host of viral genome replication; ISO:MGI.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:MGI.
DR   GO; GO:0044791; P:positive regulation by host of viral release from host cell; ISO:MGI.
DR   GO; GO:0070972; P:protein localization to endoplasmic reticulum; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000535; MSP_dom.
DR   InterPro; IPR008962; PapD-like_sf.
DR   InterPro; IPR016763; VAP.
DR   InterPro; IPR030229; VAPA.
DR   PANTHER; PTHR10809; PTHR10809; 1.
DR   PANTHER; PTHR10809:SF40; PTHR10809:SF40; 1.
DR   Pfam; PF00635; Motile_Sperm; 1.
DR   PIRSF; PIRSF019693; VAMP-associated; 1.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   PROSITE; PS50202; MSP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell junction; Cell membrane; Coiled coil;
KW   Direct protein sequencing; Endoplasmic reticulum; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT   CHAIN           2..249
FT                   /note="Vesicle-associated membrane protein-associated
FT                   protein A"
FT                   /id="PRO_0000213471"
FT   TOPO_DOM        2..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          14..131
FT                   /note="MSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT   COILED          168..207
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT   MOD_RES         125
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT   MOD_RES         170
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT   CONFLICT        10..11
FT                   /note="KH -> ND (in Ref. 4; AAF23076)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="K -> R (in Ref. 4; AAF23076)"
FT                   /evidence="ECO:0000305"
FT   STRAND          15..26
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   STRAND          29..31
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   STRAND          35..40
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   STRAND          43..45
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   STRAND          47..54
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   STRAND          58..67
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   STRAND          73..80
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   STRAND          95..101
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   HELIX           109..115
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   TURN            118..120
FT                   /evidence="ECO:0000244|PDB:2CRI"
FT   STRAND          122..131
FT                   /evidence="ECO:0000244|PDB:2CRI"
SQ   SEQUENCE   249 AA;  27855 MW;  FE8F956C1F2C71CA CRC64;
     MASASGAMAK HEQILVLDPP SDLKFKGPFT DVVTTNLKLQ NPSDRKVCFK VKTTAPRRYC
     VRPNSGIIDP GSIVTVSVML QPFDYDPNEK SKHKFMVQTI FAPPNISDME AVWKEAKPDE
     LMDSKLRCVF EMPNENDKLN DMEPSKAVPL NASKQDGPLP KPHSVSLNDT ETRKLMEECK
     RLQGEMMKLS EENRHLRDEG LRLRKVAHSD KPGSTSAVSF RDNVTSPLPS LLVVIAAIFI
     GFFLGKFIL
//
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