ID   VAPB_RAT                Reviewed;         243 AA.
AC   Q9Z269;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-NOV-2011, entry version 81.
DE   RecName: Full=Vesicle-associated membrane protein-associated protein B;
DE            Short=VAMP-B;
DE            Short=VAMP-associated protein B;
DE            Short=VAP-B;
GN   Name=Vapb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   MEDLINE=99121183; 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   PROTEIN SEQUENCE OF 176-182, AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: May play a role in vesicle trafficking.
CC   -!- SUBUNIT: Homodimer, and heterodimer with VAPA. Interacts with
CC       VAMP1 and VAMP2. Interacts (via MSP domain) with ZFYVE27 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type IV membrane protein (By similarity).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF086631; AAD13580.1; -; mRNA.
DR   EMBL; BC065576; AAH65576.1; -; mRNA.
DR   IPI; IPI00209283; -.
DR   RefSeq; NP_068619.1; NM_021847.3.
DR   UniGene; Rn.52500; -.
DR   ProteinModelPortal; Q9Z269; -.
DR   SMR; Q9Z269; 1-134.
DR   MINT; MINT-4566897; -.
DR   STRING; Q9Z269; -.
DR   PRIDE; Q9Z269; -.
DR   Ensembl; ENSRNOT00000007554; ENSRNOP00000007554; ENSRNOG00000005331.
DR   GeneID; 60431; -.
DR   KEGG; rno:60431; -.
DR   UCSC; NM_021847; rat.
DR   CTD; 9217; -.
DR   RGD; 68326; Vapb.
DR   eggNOG; roNOG07345; -.
DR   GeneTree; ENSGT00390000006947; -.
DR   HOVERGEN; HBG028551; -.
DR   InParanoid; Q9Z269; -.
DR   OMA; VMSKSIS; -.
DR   OrthoDB; EOG4DNF5D; -.
DR   PhylomeDB; Q9Z269; -.
DR   NextBio; 612154; -.
DR   ArrayExpress; Q9Z269; -.
DR   Genevestigator; Q9Z269; -.
DR   GermOnline; ENSRNOG00000005331; Rattus norvegicus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; ISS:UniProtKB.
DR   GO; GO:0019048; P:virus-host interaction; ISS:UniProtKB.
DR   InterPro; IPR000535; Major_sperm.
DR   InterPro; IPR008962; PapD-like.
DR   InterPro; IPR016763; Vesicle-associated_membrane.
DR   Gene3D; G3DSA:2.60.40.360; MSP; 1.
DR   KO; K10707; -.
DR   Pfam; PF00635; Motile_Sperm; 1.
DR   PIRSF; PIRSF019693; VAMP-associated; 1.
DR   SUPFAM; SSF49354; PapD-like; 1.
DR   PROSITE; PS50202; MSP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Complete proteome;
KW   Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    243       Vesicle-associated membrane protein-
FT                                associated protein B.
FT                                /FTId=PRO_0000213475.
FT   TOPO_DOM      2    218       Cytoplasmic (Potential).
FT   TRANSMEM    219    239       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   DOMAIN        7    124       MSP.
FT   COILED      161    196       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES     159    159       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
SQ   SEQUENCE   243 AA;  26916 MW;  870B177B0798B4EA CRC64;
     MAKVEQVLSL EPQHELKFRG PFTDVVTTNL KLGNPTDRNV CFKVKTTAPR RYCVRPNSGV
     IDAGASLNVS VMLQPFDYDP NEKSKHKFMV QSMFAPPDTS DMEAVWKEAK PEDLMDSKLR
     CVFELPAENA KPHDVEINKI MPTSASKTEA PVAAKPLTSP LDDAEVKKVM EECRRLQGEV
     QRLREESRQL KEEDGLRARK ALPSNSPMAA LAASGKEEGL SARLLALVVL FFIVGVIIGK
     IAL
//