VAPA_RAT
ID VAPA_RAT Reviewed; 249 AA.
AC Q9Z270; Q6P723;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-249.
RC TISSUE=Heart;
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 vesicle-
RT associated membrane protein-associated (VAMP-associated) proteins.";
RL Biochem. Biophys. Res. Commun. 254:21-26(1999).
RN [3]
RP FUNCTION, AND INTERACTION WITH ZFYVE27.
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 with
RT vesicle-associated membrane protein-associated protein.";
RL J. Biol. Chem. 284:13766-13777(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=24262037; DOI=10.1042/bj20131186;
RA Yamamoto Y., Yoshida A., Miyazaki N., Iwasaki K., Sakisaka T.;
RT "Arl6IP1 has the ability to shape the mammalian ER membrane in a reticulon-
RT like fashion.";
RL Biochem. J. 458:69-79(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 8-132 IN COMPLEX WITH OSBPL1A, AND
RP MUTAGENESIS OF LYS-94 AND MET-96.
RX PubMed=16004875; DOI=10.1016/j.str.2005.04.010;
RA Kaiser S.E., Brickner J.H., Reilein A.R., Fenn T.D., Walter P.,
RA Brunger A.T.;
RT "Structural basis of FFAT motif-mediated ER targeting.";
RL Structure 13:1035-1045(2005).
CC -!- FUNCTION: Binds to OSBPL3, which mediates recruitment of VAPA to plasma
CC membrane sites (By similarity). The ORP3-VAPA complex stimulates RRAS
CC signaling which in turn attenuates integrin beta-1 (ITGB1) activation
CC at the cell surface (By similarity). With OSBPL3, may regulate ER
CC morphology (By similarity). May play a role in vesicle trafficking
CC (PubMed:19289470). {ECO:0000250|UniProtKB:Q9P0L0,
CC ECO:0000269|PubMed:19289470}.
CC -!- SUBUNIT: Homodimer, and heterodimer with VAPB. Interacts with VAMP1,
CC VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain of OCLN (By
CC similarity). Interacts with OSBP (By similarity). Interacts (via C-
CC terminus) with RSAD2/viperin (via C-terminus) (By similarity).
CC Interacts with OSBPL1A (PubMed:16004875). Interacts (via MSP domain)
CC with ZFYVE27; may retain ZFYVE27 in the endoplasmic reticulum and
CC regulate its function in cell projections formation (PubMed:19289470).
CC Interacts with OSBPL3 (phosphorylated form). Interacts with KIF5A in a
CC ZFYVE27-dependent manner (By similarity). Interacts with STARD3 (via
CC FFAT motif) (By similarity). Interacts with STARD3NL (via FFAT motif)
CC (By similarity). Interacts with CERT1 (By similarity).Interacts with
CC PLEKHA3 and SACM1L to form a ternary complex (By similarity). Interacts
CC with VPS13A (via FFAT motif) (By similarity).
CC {ECO:0000250|UniProtKB:Q9P0L0, ECO:0000269|PubMed:16004875,
CC ECO:0000269|PubMed:19289470}.
CC -!- INTERACTION:
CC Q9Z270; Q8K4M9: Osbpl1a; NbExp=6; IntAct=EBI-2909425, EBI-15554439;
CC Q9Z270; Q9Z270: Vapa; NbExp=2; IntAct=EBI-2909425, EBI-2909425;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24262037}; 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:0000269|PubMed:24262037}. 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}.
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DR EMBL; BC061875; AAH61875.2; -; mRNA.
DR EMBL; AF086630; AAD13579.1; -; mRNA.
DR RefSeq; NP_113819.3; NM_031631.2.
DR PDB; 1Z9L; X-ray; 1.70 A; A=8-132.
DR PDB; 1Z9O; X-ray; 1.90 A; A/B/C/D/E/F=8-132.
DR PDBsum; 1Z9L; -.
DR PDBsum; 1Z9O; -.
DR AlphaFoldDB; Q9Z270; -.
DR SMR; Q9Z270; -.
DR BioGRID; 248655; 4.
DR DIP; DIP-48448N; -.
DR IntAct; Q9Z270; 5.
DR MINT; Q9Z270; -.
DR STRING; 10116.ENSRNOP00000020681; -.
DR iPTMnet; Q9Z270; -.
DR PhosphoSitePlus; Q9Z270; -.
DR SwissPalm; Q9Z270; -.
DR jPOST; Q9Z270; -.
DR PaxDb; Q9Z270; -.
DR PRIDE; Q9Z270; -.
DR ABCD; Q9Z270; 3 sequenced antibodies.
DR DNASU; 58857; -.
DR Ensembl; ENSRNOT00000020681; ENSRNOP00000020681; ENSRNOG00000014765.
DR GeneID; 58857; -.
DR KEGG; rno:58857; -.
DR UCSC; RGD:61803; rat.
DR CTD; 9218; -.
DR RGD; 61803; Vapa.
DR eggNOG; KOG0439; Eukaryota.
DR GeneTree; ENSGT00940000154799; -.
DR HOGENOM; CLU_032848_0_1_1; -.
DR InParanoid; Q9Z270; -.
DR OMA; QSVIAPE; -.
DR OrthoDB; 1332028at2759; -.
DR PhylomeDB; Q9Z270; -.
DR TreeFam; TF317024; -.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; Q9Z270; -.
DR PRO; PR:Q9Z270; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000014765; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; Q9Z270; baseline and differential.
DR Genevisible; Q9Z270; RN.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0033149; F:FFAT motif binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0008219; P:cell death; IMP:UniProtKB.
DR GO; GO:0035627; P:ceramide transport; ISO:RGD.
DR GO; GO:0090114; P:COPII-coated vesicle budding; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:RGD.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0015914; P:phospholipid transport; ISO:RGD.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:RGD.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISO:RGD.
DR GO; GO:0015918; P:sterol transport; ISO:RGD.
DR GO; GO:0019076; P:viral release from host cell; ISO:RGD.
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 Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Tight junction; Transmembrane; 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_0000213472"
FT TOPO_DOM 2..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
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:0007744|PubMed:22673903"
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 MUTAGEN 94
FT /note="K->D: Loss of interaction with OSBPL1A; when
FT associated with D-96."
FT /evidence="ECO:0000269|PubMed:16004875"
FT MUTAGEN 96
FT /note="M->D: Loss of interaction with OSBPL1A; when
FT associated with D-94."
FT /evidence="ECO:0000269|PubMed:16004875"
FT CONFLICT 126
FT /note="L -> P (in Ref. 2; AAD13579)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> S (in Ref. 2; AAD13579)"
FT /evidence="ECO:0000305"
FT STRAND 15..27
FT /evidence="ECO:0007829|PDB:1Z9L"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1Z9L"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1Z9L"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1Z9L"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1Z9L"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1Z9L"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1Z9L"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1Z9L"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:1Z9L"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:1Z9L"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1Z9L"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:1Z9L"
SQ SEQUENCE 249 AA; 27841 MW; A30D08E31F3379C1 CRC64;
MASASGAMAK HEQILVLDPP SDLKFKGPFT DVVTTNLKLQ NPSDRKVCFK VKTTAPRRYC
VRPNSGVIDP GSIVTVSVML QPFDYDPNEK SKHKFMVQTI FAPPNISDME AVWKEAKPDE
LMDSKLRCVF EMPNENDKLN DMEPSKAVPL NASKQDGPLP KPHSVSLNDT ETRKLMEECK
RLQGEMMKLS EENRHLRDEG LRLRKVAHSD KPGSTSAVSF RDNVTSPLPS LLVVIAAIFI
GFFLGKFIL
