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 Genevisible; Q9Z269; RN.
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.
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
//
