VAPA_MOUSE
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 03-AUG-2022, entry version 179.
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};
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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 AlphaFoldDB; Q9WV55; -.
DR SMR; Q9WV55; -.
DR BioGRID; 206035; 22.
DR ComplexPortal; CPX-507; Vapa-Osbp complex.
DR IntAct; Q9WV55; 12.
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 ProteomicsDB; 300212; -.
DR TopDownProteomics; Q9WV55; -.
DR ABCD; Q9WV55; 3 sequenced antibodies.
DR Antibodypedia; 2287; 296 antibodies from 33 providers.
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 VEuPathDB; HostDB:ENSMUSG00000024091; -.
DR eggNOG; KOG0439; Eukaryota.
DR GeneTree; ENSGT00940000154799; -.
DR HOGENOM; CLU_032848_0_1_1; -.
DR InParanoid; Q9WV55; -.
DR OMA; QSVIAPE; -.
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; 7 hits in 76 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 260 other tissues.
DR ExpressionAtlas; Q9WV55; baseline and differential.
DR Genevisible; Q9WV55; MM.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
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:0035627; P:ceramide transport; ISO:MGI.
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:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:MGI.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISO:MGI.
DR GO; GO:0015918; P:sterol transport; ISO:MGI.
DR GO; GO:0019076; P:viral release from host cell; ISO:MGI.
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 PANTHER; PTHR10809; PTHR10809; 2.
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 REGION 135..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007829|PDB:2CRI"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2CRI"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2CRI"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2CRI"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:2CRI"
FT STRAND 58..67
FT /evidence="ECO:0007829|PDB:2CRI"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:2CRI"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2CRI"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:2CRI"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2CRI"
FT STRAND 122..131
FT /evidence="ECO:0007829|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
