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   27-MAR-2024, entry version 158.
DE   RecName: Full=Vesicle-associated membrane protein-associated protein B {ECO:0000305};
DE            Short=VAMP-B;
DE            Short=VAMP-associated protein B;
DE            Short=VAP-B;
GN   Name=Vapb {ECO:0000312|RGD:68326};
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 [MRNA].
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   [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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 176-182, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, 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).
CC   -!- FUNCTION: Endoplasmic reticulum (ER)-anchored protein that mediates the
CC       formation of contact sites between the ER and endosomes via interaction
CC       with FFAT motif-containing proteins such as STARD3 or WDR44. Interacts
CC       with STARD3 in a FFAT motif phosphorylation dependent manner. Via
CC       interaction with WDR44 participates in neosynthesized protein export.
CC       Participates in the endoplasmic reticulum unfolded protein response
CC       (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium
CC       homeostasis regulation. {ECO:0000250|UniProtKB:O95292}.
CC   -!- SUBUNIT: Homodimer, and heterodimer with VAPA. Interacts with VAMP1 and
CC       VAMP2. Interacts (via MSP domain) with ZFYVE27. Interacts with RMDN3.
CC       Interacts with KIF5A in a ZFYVE27-dependent manner. Interacts (via MSP
CC       domain) with STARD3 (via phospho-FFAT motif). Interacts with STARD3NL
CC       (via FFAT motif). Interacts with CERT1. Interacts with PLEKHA3 and
CC       SACM1L to form a ternary complex. Interacts with VPS13A (via FFAT
CC       motif). Interacts with RB1CC1 (via phosphorylated FFAT motif), MIGA2
CC       (via phosphorylated FFAT motif), RMDN3 (via phosphorylated FFAT motif),
CC       OSBPL1A (via FFAT motif), KCNB1 (via phosphorylated FFAT motif) and
CC       KCNB2 (via phosphorylated FFAT motif). Interacts (via MSP domain) with
CC       WDR44; the interactions connect the endoplasmic reticulum (ER) with the
CC       endosomal tubule (By similarity). {ECO:0000250|UniProtKB:O95292}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:O95292}; Single-pass type IV membrane protein
CC       {ECO:0000250|UniProtKB:Q9P0L0}. Note=Present in mitochondria-associated
CC       membranes that are endoplasmic reticulum membrane regions closely
CC       apposed to the outer mitochondrial membrane.
CC       {ECO:0000250|UniProtKB:O95292}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The MSP domain binds the FFAT motif of many proteins.
CC       {ECO:0000250|UniProtKB:O95292}.
CC   -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC       family. {ECO:0000305}.
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DR   EMBL; AF086631; AAD13580.1; -; mRNA.
DR   EMBL; BC065576; AAH65576.1; -; mRNA.
DR   RefSeq; NP_068619.1; NM_021847.3.
DR   AlphaFoldDB; Q9Z269; -.
DR   SMR; Q9Z269; -.
DR   BioGRID; 248831; 1.
DR   IntAct; Q9Z269; 2.
DR   MINT; Q9Z269; -.
DR   STRING; 10116.ENSRNOP00000007554; -.
DR   iPTMnet; Q9Z269; -.
DR   PhosphoSitePlus; Q9Z269; -.
DR   SwissPalm; Q9Z269; -.
DR   jPOST; Q9Z269; -.
DR   PaxDb; 10116-ENSRNOP00000007554; -.
DR   ABCD; Q9Z269; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000007554.5; ENSRNOP00000007554.2; ENSRNOG00000005331.5.
DR   Ensembl; ENSRNOT00055001546; ENSRNOP00055001235; ENSRNOG00055000924.
DR   Ensembl; ENSRNOT00060002348; ENSRNOP00060001521; ENSRNOG00060001564.
DR   Ensembl; ENSRNOT00065021467; ENSRNOP00065016621; ENSRNOG00065013095.
DR   GeneID; 60431; -.
DR   KEGG; rno:60431; -.
DR   UCSC; RGD:68326; rat.
DR   AGR; RGD:68326; -.
DR   CTD; 9217; -.
DR   RGD; 68326; Vapb.
DR   eggNOG; KOG0439; Eukaryota.
DR   GeneTree; ENSGT00940000155769; -.
DR   HOGENOM; CLU_032848_0_1_1; -.
DR   InParanoid; Q9Z269; -.
DR   OMA; AENAKPH; -.
DR   OrthoDB; 122649at2759; -.
DR   PhylomeDB; Q9Z269; -.
DR   TreeFam; TF317024; -.
DR   Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR   Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR   Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR   Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR   Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR   PRO; PR:Q9Z269; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000005331; Expressed in skeletal muscle tissue and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR   GO; GO:0033149; F:FFAT motif binding; ISO:RGD.
DR   GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0030301; P:cholesterol transport; ISO:RGD.
DR   GO; GO:0090114; P:COPII-coated vesicle budding; ISO:RGD.
DR   GO; GO:0090158; P:endoplasmic reticulum membrane organization; IBA:GO_Central.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:RGD.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR   GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IBA:GO_Central.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0036498; P:IRE1-mediated unfolded protein response; ISS:UniProtKB.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR10809:SF12; VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN B_C; 1.
DR   Pfam; PF00635; Motile_Sperm; 1.
DR   PIRSF; PIRSF019693; VAMP-associated; 1.
DR   SUPFAM; SSF49354; PapD-like; 1.
DR   PROSITE; PS50202; MSP; 1.
DR   Genevisible; Q9Z269; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Direct protein sequencing; Endoplasmic reticulum;
KW   Isopeptide bond; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Ubl conjugation;
KW   Unfolded protein response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O95292"
FT   CHAIN           2..243
FT                   /note="Vesicle-associated membrane protein-associated
FT                   protein B"
FT                   /id="PRO_0000213475"
FT   TOPO_DOM        2..218
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          7..124
FT                   /note="MSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT   COILED          161..196
FT                   /evidence="ECO:0000255"
FT   SITE            43
FT                   /note="Involved in binding the phosphorylated serine of the
FT                   phospho-FFAT motif"
FT                   /evidence="ECO:0000250|UniProtKB:O95292"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O95292"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95292"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95292"
FT   CROSSLNK        147
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:O95292"
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
//