Full text data of VAPA
VAPA
(VAP33)
[Confidence: high (present in two of the MS resources)]
Vesicle-associated membrane protein-associated protein A; VAMP-A; VAMP-associated protein A; VAP-A (33 kDa VAMP-associated protein; VAP-33)
Vesicle-associated membrane protein-associated protein A; VAMP-A; VAMP-associated protein A; VAP-A (33 kDa VAMP-associated protein; VAP-33)
hRBCD
IPI00170692
IPI00170692 Vesicle-associated membrane protein-associated protein A Vesicle-associated membrane protein-associated protein A membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 3 2 n/a 2 n/a n/a 2 n/a n/a Type IV membrane protein, associated with vesicles and cytoskeleton also n/a found at its expected molecular weight found at molecular weight
IPI00170692 Vesicle-associated membrane protein-associated protein A Vesicle-associated membrane protein-associated protein A membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 3 2 n/a 2 n/a n/a 2 n/a n/a Type IV membrane protein, associated with vesicles and cytoskeleton also n/a found at its expected molecular weight found at molecular weight
Comments
Isoform Q9P0L0-2 was detected.
Isoform Q9P0L0-2 was detected.
UniProt
Q9P0L0
ID VAPA_HUMAN Reviewed; 249 AA.
AC Q9P0L0; A6NDZ0; D3DUI3; O75453; Q5U0E7; Q9UBZ2;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 09-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 127.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH OCLN.
RC TISSUE=Liver;
RX PubMed=10523508;
RA Lapierre L.A., Tuma P.L., Navarre J., Goldenring J.R., Anderson J.M.;
RT "VAP-33 localizes to both an intracellular vesicle population and with
RT occludin at the tight junction.";
RL J. Cell Sci. 112:3723-3732(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhou H.J., Huang X.W., Zhou Y., Hu S.L., Yuan J.G., Qiang B.Q.;
RT "Cloning and isolating human 33kDa Vamp-associated protein cDNA.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-199 (ISOFORM 2).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1), AND INTERACTION WITH
RP VAMP1 AND VAMP2.
RC TISSUE=Pancreatic islet;
RX PubMed=9657962;
RA Weir M.L., Klip A., Trimble W.S.;
RT "Identification of a human homologue of the vesicle-associated
RT membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a
RT broadly expressed protein that binds to VAMP.";
RL Biochem. J. 333:247-251(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=9920726; DOI=10.1006/bbrc.1998.9876;
RA Nishimura Y., Hayashi M., Inada H., Tanaka T.;
RT "Molecular cloning and characterization of mammalian homologues of
RT vesicle-associated membrane protein-associated (VAMP-associated)
RT proteins.";
RL Biochem. Biophys. Res. Commun. 254:21-26(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-249 (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND INTERACTION WITH VAPB; VAMP1; VAMP2; STX1A; BET1 AND
RP SEC22C.
RX PubMed=11511104; DOI=10.1006/bbrc.2001.5437;
RA Weir M.L., Xie H., Klip A., Trimble W.S.;
RT "VAP-A binds promiscuously to both v- and tSNAREs.";
RL Biochem. Biophys. Res. Commun. 286:616-621(2001).
RN [10]
RP FUNCTION, INTERACTION WITH ZFYVE27, MUTAGENESIS OF LYS-94 AND MET-96,
RP AND SUBCELLULAR LOCATION.
RX PubMed=19289470; DOI=10.1074/jbc.M807938200;
RA Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I.;
RT "Promotion of neurite extension by protrudin requires its interaction
RT with vesicle-associated membrane protein-associated protein.";
RL J. Biol. Chem. 284:13766-13777(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH RSAD2 AND HCV PROTEIN NS5A AND NS5B.
RX PubMed=21957124; DOI=10.1099/vir.0.033860-0;
RA Wang S., Wu X., Pan T., Song W., Wang Y., Zhang F., Yuan Z.;
RT "Viperin inhibits hepatitis C virus replication by interfering with
RT binding of NS5A to host protein hVAP-33.";
RL J. Gen. Virol. 93:83-92(2012).
RN [14]
RP INTERACTION WITH IFITM3.
RX PubMed=23601107; DOI=10.1016/j.chom.2013.03.006;
RA Amini-Bavil-Olyaee S., Choi Y.J., Lee J.H., Shi M., Huang I.C.,
RA Farzan M., Jung J.U.;
RT "The antiviral effector IFITM3 disrupts intracellular cholesterol
RT homeostasis to block viral entry.";
RL Cell Host Microbe 13:452-464(2013).
RN [15]
RP STRUCTURE BY NMR OF 11-135, AND INTERACTION WITH OSBP.
RX PubMed=20178991; DOI=10.1074/jbc.M109.082602;
RA Furuita K., Jee J., Fukada H., Mishima M., Kojima C.;
RT "Electrostatic interaction between oxysterol-binding protein and VAMP-
RT associated protein A revealed by NMR and mutagenesis studies.";
RL J. Biol. Chem. 285:12961-12970(2010).
CC -!- FUNCTION: May play a role in vesicle trafficking.
CC -!- SUBUNIT: Homodimer, and heterodimer with VAPB. Interacts with
CC VAMP1, VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain
CC of OCLN. Interacts with OSBPL1A. Interacts (via MSP domain) with
CC ZFYVE27; may retain ZFYVE27 in the endoplasmic reticulum and
CC regulate its function in cell projections formation. Interacts
CC with OSBP. Interacts (via C-terminus) with RSAD2/viperin (via C-
CC terminus). Interacts with HCV protein NS5A and NS5B. Interacts
CC with IFITM3.
CC -!- INTERACTION:
CC P27958:- (xeno); NbExp=5; IntAct=EBI-1059156, EBI-6904388;
CC Q03463:- (xeno); NbExp=3; IntAct=EBI-1059156, EBI-8803426;
CC P00533:EGFR; NbExp=2; IntAct=EBI-1059156, EBI-297353;
CC P35372:OPRM1; NbExp=3; IntAct=EBI-1059156, EBI-2624570;
CC Q5T4F4:ZFYVE27; NbExp=5; IntAct=EBI-1059156, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type IV membrane protein. 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
CC tight junction in polarized epithelial cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P0L0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0L0-2; Sequence=VSP_038648;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP)
CC (TC 9.B.17) family.
CC -!- SIMILARITY: Contains 1 MSP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09742.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAF72105.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BG488667; Type=Frameshift; Positions=72, 207, 241;
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DR EMBL; AF044670; AAD09742.1; ALT_INIT; mRNA.
DR EMBL; AF154847; AAF72105.1; ALT_INIT; mRNA.
DR EMBL; AC006238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01591.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01592.1; -; Genomic_DNA.
DR EMBL; BC002992; AAH02992.2; -; mRNA.
DR EMBL; BG488667; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF057358; AAC26508.1; -; mRNA.
DR EMBL; AF086627; AAD13576.1; -; mRNA.
DR EMBL; BT019618; AAV38424.1; -; mRNA.
DR RefSeq; NP_003565.4; NM_003574.5.
DR RefSeq; NP_919415.2; NM_194434.2.
DR UniGene; Hs.165195; -.
DR PDB; 2RR3; NMR; -; A=11-135.
DR PDBsum; 2RR3; -.
DR ProteinModelPortal; Q9P0L0; -.
DR SMR; Q9P0L0; 9-135.
DR IntAct; Q9P0L0; 41.
DR MINT; MINT-109415; -.
DR STRING; 9606.ENSP00000345656; -.
DR PhosphoSite; Q9P0L0; -.
DR DMDM; 122066680; -.
DR PaxDb; Q9P0L0; -.
DR PRIDE; Q9P0L0; -.
DR DNASU; 9218; -.
DR Ensembl; ENST00000340541; ENSP00000345656; ENSG00000101558.
DR Ensembl; ENST00000400000; ENSP00000382880; ENSG00000101558.
DR GeneID; 9218; -.
DR KEGG; hsa:9218; -.
DR UCSC; uc002kok.3; human.
DR CTD; 9218; -.
DR GeneCards; GC18P009904; -.
DR H-InvDB; HIX0115359; -.
DR HGNC; HGNC:12648; VAPA.
DR HPA; HPA009174; -.
DR MIM; 605703; gene.
DR neXtProt; NX_Q9P0L0; -.
DR PharmGKB; PA37272; -.
DR eggNOG; COG5066; -.
DR HOGENOM; HOG000293182; -.
DR HOVERGEN; HBG028551; -.
DR KO; K06096; -.
DR OMA; FEMPSEN; -.
DR OrthoDB; EOG7CK389; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; VAPA; human.
DR EvolutionaryTrace; Q9P0L0; -.
DR GeneWiki; VAPA; -.
DR GenomeRNAi; 9218; -.
DR NextBio; 34557; -.
DR PMAP-CutDB; Q9P0L0; -.
DR PRO; PR:Q9P0L0; -.
DR ArrayExpress; Q9P0L0; -.
DR Bgee; Q9P0L0; -.
DR CleanEx; HS_VAPA; -.
DR Genevestigator; Q9P0L0; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008219; P:cell death; IMP:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR Gene3D; 2.60.40.360; -; 1.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like.
DR InterPro; IPR016763; Vesicle-associated_membrane.
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; Alternative splicing; Coiled coil;
KW Complete proteome; Endoplasmic reticulum; Membrane; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 249 Vesicle-associated membrane protein-
FT associated protein A.
FT /FTId=PRO_0000213470.
FT TOPO_DOM 1 227 Cytoplasmic (Potential).
FT TRANSMEM 228 248 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT DOMAIN 14 131 MSP.
FT COILED 169 205 Potential.
FT MOD_RES 125 125 N6-acetyllysine.
FT VAR_SEQ 139 139 L -> LGITPPGNAPTVTSMSSINNTVATPASYHTKDDPRG
FT LSVLKQEKQK (in isoform 2).
FT /FTId=VSP_038648.
FT VARIANT 8 8 M -> T (in dbSNP:rs1044163).
FT /FTId=VAR_050440.
FT VARIANT 104 104 P -> L (in dbSNP:rs1127666).
FT /FTId=VAR_050441.
FT MUTAGEN 94 94 K->D: Alters interaction with ZFYVE27;
FT when associated with D-96.
FT MUTAGEN 96 96 M->D: Alters interaction with ZFYVE27;
FT when associated with D-94.
FT CONFLICT 10 11 KH -> ND (in Ref. 6; AAC26508 and 8;
FT AAV38424).
FT CONFLICT 160 160 P -> S (in Ref. 2; AAF72105).
FT STRAND 14 21
FT STRAND 23 27
FT STRAND 33 40
FT STRAND 43 45
FT STRAND 47 54
FT TURN 56 58
FT STRAND 59 63
FT STRAND 65 68
FT STRAND 73 80
FT STRAND 94 101
FT HELIX 109 115
FT TURN 118 120
FT STRAND 122 131
SQ SEQUENCE 249 AA; 27893 MW; 68B603F3A9FA5475 CRC64;
MASASGAMAK HEQILVLDPP TDLKFKGPFT DVVTTNLKLR NPSDRKVCFK VKTTAPRRYC
VRPNSGIIDP GSTVTVSVML QPFDYDPNEK SKHKFMVQTI FAPPNTSDME AVWKEAKPDE
LMDSKLRCVF EMPNENDKLN DMEPSKAVPL NASKQDGPMP KPHSVSLNDT ETRKLMEECK
RLQGEMMKLS EENRHLRDEG LRLRKVAHSD KPGSTSTASF RDNVTSPLPS LLVVIAAIFI
GFFLGKFIL
//
ID VAPA_HUMAN Reviewed; 249 AA.
AC Q9P0L0; A6NDZ0; D3DUI3; O75453; Q5U0E7; Q9UBZ2;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 09-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 127.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH OCLN.
RC TISSUE=Liver;
RX PubMed=10523508;
RA Lapierre L.A., Tuma P.L., Navarre J., Goldenring J.R., Anderson J.M.;
RT "VAP-33 localizes to both an intracellular vesicle population and with
RT occludin at the tight junction.";
RL J. Cell Sci. 112:3723-3732(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhou H.J., Huang X.W., Zhou Y., Hu S.L., Yuan J.G., Qiang B.Q.;
RT "Cloning and isolating human 33kDa Vamp-associated protein cDNA.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-199 (ISOFORM 2).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1), AND INTERACTION WITH
RP VAMP1 AND VAMP2.
RC TISSUE=Pancreatic islet;
RX PubMed=9657962;
RA Weir M.L., Klip A., Trimble W.S.;
RT "Identification of a human homologue of the vesicle-associated
RT membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a
RT broadly expressed protein that binds to VAMP.";
RL Biochem. J. 333:247-251(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-249 (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=9920726; DOI=10.1006/bbrc.1998.9876;
RA Nishimura Y., Hayashi M., Inada H., Tanaka T.;
RT "Molecular cloning and characterization of mammalian homologues of
RT vesicle-associated membrane protein-associated (VAMP-associated)
RT proteins.";
RL Biochem. Biophys. Res. Commun. 254:21-26(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-249 (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND INTERACTION WITH VAPB; VAMP1; VAMP2; STX1A; BET1 AND
RP SEC22C.
RX PubMed=11511104; DOI=10.1006/bbrc.2001.5437;
RA Weir M.L., Xie H., Klip A., Trimble W.S.;
RT "VAP-A binds promiscuously to both v- and tSNAREs.";
RL Biochem. Biophys. Res. Commun. 286:616-621(2001).
RN [10]
RP FUNCTION, INTERACTION WITH ZFYVE27, MUTAGENESIS OF LYS-94 AND MET-96,
RP AND SUBCELLULAR LOCATION.
RX PubMed=19289470; DOI=10.1074/jbc.M807938200;
RA Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I.;
RT "Promotion of neurite extension by protrudin requires its interaction
RT with vesicle-associated membrane protein-associated protein.";
RL J. Biol. Chem. 284:13766-13777(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH RSAD2 AND HCV PROTEIN NS5A AND NS5B.
RX PubMed=21957124; DOI=10.1099/vir.0.033860-0;
RA Wang S., Wu X., Pan T., Song W., Wang Y., Zhang F., Yuan Z.;
RT "Viperin inhibits hepatitis C virus replication by interfering with
RT binding of NS5A to host protein hVAP-33.";
RL J. Gen. Virol. 93:83-92(2012).
RN [14]
RP INTERACTION WITH IFITM3.
RX PubMed=23601107; DOI=10.1016/j.chom.2013.03.006;
RA Amini-Bavil-Olyaee S., Choi Y.J., Lee J.H., Shi M., Huang I.C.,
RA Farzan M., Jung J.U.;
RT "The antiviral effector IFITM3 disrupts intracellular cholesterol
RT homeostasis to block viral entry.";
RL Cell Host Microbe 13:452-464(2013).
RN [15]
RP STRUCTURE BY NMR OF 11-135, AND INTERACTION WITH OSBP.
RX PubMed=20178991; DOI=10.1074/jbc.M109.082602;
RA Furuita K., Jee J., Fukada H., Mishima M., Kojima C.;
RT "Electrostatic interaction between oxysterol-binding protein and VAMP-
RT associated protein A revealed by NMR and mutagenesis studies.";
RL J. Biol. Chem. 285:12961-12970(2010).
CC -!- FUNCTION: May play a role in vesicle trafficking.
CC -!- SUBUNIT: Homodimer, and heterodimer with VAPB. Interacts with
CC VAMP1, VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain
CC of OCLN. Interacts with OSBPL1A. Interacts (via MSP domain) with
CC ZFYVE27; may retain ZFYVE27 in the endoplasmic reticulum and
CC regulate its function in cell projections formation. Interacts
CC with OSBP. Interacts (via C-terminus) with RSAD2/viperin (via C-
CC terminus). Interacts with HCV protein NS5A and NS5B. Interacts
CC with IFITM3.
CC -!- INTERACTION:
CC P27958:- (xeno); NbExp=5; IntAct=EBI-1059156, EBI-6904388;
CC Q03463:- (xeno); NbExp=3; IntAct=EBI-1059156, EBI-8803426;
CC P00533:EGFR; NbExp=2; IntAct=EBI-1059156, EBI-297353;
CC P35372:OPRM1; NbExp=3; IntAct=EBI-1059156, EBI-2624570;
CC Q5T4F4:ZFYVE27; NbExp=5; IntAct=EBI-1059156, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type IV membrane protein. 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
CC tight junction in polarized epithelial cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P0L0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0L0-2; Sequence=VSP_038648;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP)
CC (TC 9.B.17) family.
CC -!- SIMILARITY: Contains 1 MSP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD09742.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAF72105.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BG488667; Type=Frameshift; Positions=72, 207, 241;
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DR EMBL; AF044670; AAD09742.1; ALT_INIT; mRNA.
DR EMBL; AF154847; AAF72105.1; ALT_INIT; mRNA.
DR EMBL; AC006238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01591.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01592.1; -; Genomic_DNA.
DR EMBL; BC002992; AAH02992.2; -; mRNA.
DR EMBL; BG488667; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF057358; AAC26508.1; -; mRNA.
DR EMBL; AF086627; AAD13576.1; -; mRNA.
DR EMBL; BT019618; AAV38424.1; -; mRNA.
DR RefSeq; NP_003565.4; NM_003574.5.
DR RefSeq; NP_919415.2; NM_194434.2.
DR UniGene; Hs.165195; -.
DR PDB; 2RR3; NMR; -; A=11-135.
DR PDBsum; 2RR3; -.
DR ProteinModelPortal; Q9P0L0; -.
DR SMR; Q9P0L0; 9-135.
DR IntAct; Q9P0L0; 41.
DR MINT; MINT-109415; -.
DR STRING; 9606.ENSP00000345656; -.
DR PhosphoSite; Q9P0L0; -.
DR DMDM; 122066680; -.
DR PaxDb; Q9P0L0; -.
DR PRIDE; Q9P0L0; -.
DR DNASU; 9218; -.
DR Ensembl; ENST00000340541; ENSP00000345656; ENSG00000101558.
DR Ensembl; ENST00000400000; ENSP00000382880; ENSG00000101558.
DR GeneID; 9218; -.
DR KEGG; hsa:9218; -.
DR UCSC; uc002kok.3; human.
DR CTD; 9218; -.
DR GeneCards; GC18P009904; -.
DR H-InvDB; HIX0115359; -.
DR HGNC; HGNC:12648; VAPA.
DR HPA; HPA009174; -.
DR MIM; 605703; gene.
DR neXtProt; NX_Q9P0L0; -.
DR PharmGKB; PA37272; -.
DR eggNOG; COG5066; -.
DR HOGENOM; HOG000293182; -.
DR HOVERGEN; HBG028551; -.
DR KO; K06096; -.
DR OMA; FEMPSEN; -.
DR OrthoDB; EOG7CK389; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; VAPA; human.
DR EvolutionaryTrace; Q9P0L0; -.
DR GeneWiki; VAPA; -.
DR GenomeRNAi; 9218; -.
DR NextBio; 34557; -.
DR PMAP-CutDB; Q9P0L0; -.
DR PRO; PR:Q9P0L0; -.
DR ArrayExpress; Q9P0L0; -.
DR Bgee; Q9P0L0; -.
DR CleanEx; HS_VAPA; -.
DR Genevestigator; Q9P0L0; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008219; P:cell death; IMP:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR Gene3D; 2.60.40.360; -; 1.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like.
DR InterPro; IPR016763; Vesicle-associated_membrane.
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; Alternative splicing; Coiled coil;
KW Complete proteome; Endoplasmic reticulum; Membrane; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 249 Vesicle-associated membrane protein-
FT associated protein A.
FT /FTId=PRO_0000213470.
FT TOPO_DOM 1 227 Cytoplasmic (Potential).
FT TRANSMEM 228 248 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT DOMAIN 14 131 MSP.
FT COILED 169 205 Potential.
FT MOD_RES 125 125 N6-acetyllysine.
FT VAR_SEQ 139 139 L -> LGITPPGNAPTVTSMSSINNTVATPASYHTKDDPRG
FT LSVLKQEKQK (in isoform 2).
FT /FTId=VSP_038648.
FT VARIANT 8 8 M -> T (in dbSNP:rs1044163).
FT /FTId=VAR_050440.
FT VARIANT 104 104 P -> L (in dbSNP:rs1127666).
FT /FTId=VAR_050441.
FT MUTAGEN 94 94 K->D: Alters interaction with ZFYVE27;
FT when associated with D-96.
FT MUTAGEN 96 96 M->D: Alters interaction with ZFYVE27;
FT when associated with D-94.
FT CONFLICT 10 11 KH -> ND (in Ref. 6; AAC26508 and 8;
FT AAV38424).
FT CONFLICT 160 160 P -> S (in Ref. 2; AAF72105).
FT STRAND 14 21
FT STRAND 23 27
FT STRAND 33 40
FT STRAND 43 45
FT STRAND 47 54
FT TURN 56 58
FT STRAND 59 63
FT STRAND 65 68
FT STRAND 73 80
FT STRAND 94 101
FT HELIX 109 115
FT TURN 118 120
FT STRAND 122 131
SQ SEQUENCE 249 AA; 27893 MW; 68B603F3A9FA5475 CRC64;
MASASGAMAK HEQILVLDPP TDLKFKGPFT DVVTTNLKLR NPSDRKVCFK VKTTAPRRYC
VRPNSGIIDP GSTVTVSVML QPFDYDPNEK SKHKFMVQTI FAPPNTSDME AVWKEAKPDE
LMDSKLRCVF EMPNENDKLN DMEPSKAVPL NASKQDGPMP KPHSVSLNDT ETRKLMEECK
RLQGEMMKLS EENRHLRDEG LRLRKVAHSD KPGSTSTASF RDNVTSPLPS LLVVIAAIFI
GFFLGKFIL
//
MIM
605703
*RECORD*
*FIELD* NO
605703
*FIELD* TI
*605703 VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN A; VAPA
;;VAMP-ASSOCIATED PROTEIN A;;
read moreVAMP-ASSOCIATED PROTEIN, 33-KD; VAP33
*FIELD* TX
DESCRIPTION
SNAREs (see 603215) are compartmentally specific, cytoplasmically
oriented integral membrane proteins involved in the fusion of membranes
and the transport of intracellular proteins. Recognition of vesicles and
target membranes is mediated by v-SNAREs (e.g., VAMP8; 603177) and
t-SNAREs (e.g., SNAP23; 602534), respectively.
CLONING
By searching an EST database for human homologs of the Aplysia 33-kD
VAMP-associated protein (Vap33), Weir et al. (1998) identified a cDNA
encoding VAPA, which they termed VAP33. Sequence analysis predicted that
the 242-amino acid protein, which is 50% identical to the molluscan
sequence, contains 8 potential phosphorylation sites, an alpha-helical
coiled-coil domain, and a C-terminal transmembrane domain. Northern blot
analysis of mouse tissues detected a major 1.9-kb transcript and minor
3.9- and 7.1-kb transcripts in all tissues tested, with highest
expression in brain, testis, ovary, kidney and skeletal muscle. In
contrast, Vap33 expression is neuron specific in Aplysia.
Nishimura et al. (1999) identified cDNAs encoding VAPA and the 60%
homologous VAPB (605704). Northern blot analysis detected a 1.7-kb VAPA
transcript in all human tissues tested.
GENE FUNCTION
By Western blot analysis, Weir et al. (1998) showed that VAPA interacts
with VAMP1 (185880) and VAMP2 (185881) but not with SNAP25 (600322).
By SDS-PAGE analysis, Nishimura et al. (1999) demonstrated that the
transmembrane domain of recombinant VAPA interacted with VAPA and VAPB
fusion proteins.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VAPA
gene to chromosome 18 (TMAP stSG49693).
*FIELD* RF
1. Nishimura, Y.; Hayashi, M.; Inada, H.; Tanaka, T.: Molecular cloning
and characterization of mammalian homologues of vesicle-associated
membrane protein-associated (VAMP-associated) proteins. Biochem.
Biophys. Res. Commun. 254: 21-26, 1999.
2. Weir, M. L.; Klip, A.; Trimble, W. S.: 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. Biochem. J. 333: 247-251, 1998.
*FIELD* CD
Paul J. Converse: 2/28/2001
*FIELD* ED
carol: 01/07/2010
mgross: 2/28/2001
*RECORD*
*FIELD* NO
605703
*FIELD* TI
*605703 VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN A; VAPA
;;VAMP-ASSOCIATED PROTEIN A;;
read moreVAMP-ASSOCIATED PROTEIN, 33-KD; VAP33
*FIELD* TX
DESCRIPTION
SNAREs (see 603215) are compartmentally specific, cytoplasmically
oriented integral membrane proteins involved in the fusion of membranes
and the transport of intracellular proteins. Recognition of vesicles and
target membranes is mediated by v-SNAREs (e.g., VAMP8; 603177) and
t-SNAREs (e.g., SNAP23; 602534), respectively.
CLONING
By searching an EST database for human homologs of the Aplysia 33-kD
VAMP-associated protein (Vap33), Weir et al. (1998) identified a cDNA
encoding VAPA, which they termed VAP33. Sequence analysis predicted that
the 242-amino acid protein, which is 50% identical to the molluscan
sequence, contains 8 potential phosphorylation sites, an alpha-helical
coiled-coil domain, and a C-terminal transmembrane domain. Northern blot
analysis of mouse tissues detected a major 1.9-kb transcript and minor
3.9- and 7.1-kb transcripts in all tissues tested, with highest
expression in brain, testis, ovary, kidney and skeletal muscle. In
contrast, Vap33 expression is neuron specific in Aplysia.
Nishimura et al. (1999) identified cDNAs encoding VAPA and the 60%
homologous VAPB (605704). Northern blot analysis detected a 1.7-kb VAPA
transcript in all human tissues tested.
GENE FUNCTION
By Western blot analysis, Weir et al. (1998) showed that VAPA interacts
with VAMP1 (185880) and VAMP2 (185881) but not with SNAP25 (600322).
By SDS-PAGE analysis, Nishimura et al. (1999) demonstrated that the
transmembrane domain of recombinant VAPA interacted with VAPA and VAPB
fusion proteins.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VAPA
gene to chromosome 18 (TMAP stSG49693).
*FIELD* RF
1. Nishimura, Y.; Hayashi, M.; Inada, H.; Tanaka, T.: Molecular cloning
and characterization of mammalian homologues of vesicle-associated
membrane protein-associated (VAMP-associated) proteins. Biochem.
Biophys. Res. Commun. 254: 21-26, 1999.
2. Weir, M. L.; Klip, A.; Trimble, W. S.: 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. Biochem. J. 333: 247-251, 1998.
*FIELD* CD
Paul J. Converse: 2/28/2001
*FIELD* ED
carol: 01/07/2010
mgross: 2/28/2001