VAPB_MOUSE
ID VAPB_MOUSE Reviewed; 243 AA.
AC Q9QY76;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Vesicle-associated membrane protein-associated protein B;
DE Short=VAMP-B;
DE Short=VAMP-associated protein B;
DE Short=VAP-B;
DE AltName: Full=VAMP-associated protein 33b;
GN Name=Vapb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tang B.L., Low D.L.H., Lock M.L., Hong W.;
RT "Two forms of mammalian VAP33.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP INTERACTION WITH ZFYVE27.
RX PubMed=24251978; DOI=10.1111/gtc.12109;
RA Ohnishi T., Shirane M., Hashimoto Y., Saita S., Nakayama K.I.;
RT "Identification and characterization of a neuron-specific isoform of
RT protrudin.";
RL Genes Cells 19:97-111(2014).
CC -!- FUNCTION: Participates in the endoplasmic reticulum unfolded protein
CC response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular
CC calcium homeostasis regulation. {ECO:0000250|UniProtKB:O95292}.
CC -!- SUBUNIT: Homodimer, and heterodimer with VAPA. Interacts with RMDN3,
CC VAMP1 and VAMP2 (By similarity). Interacts (via MSP domain) with
CC ZFYVE27 (PubMed:24251978). Interacts with KIF5A in a ZFYVE27-dependent
CC manner (By similarity). Interacts with STARD3 (via FFAT motif) (By
CC similarity). Interacts with STARD3NL (via FFAT motif) (By similarity).
CC Interacts with CERT1 (By similarity). Interacts with PLEKHA3 and SACM1L
CC to form a ternary complex (By similarity). Interacts with VPS13A (via
CC FFAT motif) (By similarity). {ECO:0000250|UniProtKB:O95292,
CC ECO:0000269|PubMed:24251978}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95292}; Single-pass type IV membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC family. {ECO:0000305}.
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DR EMBL; AF115504; AAF23077.1; -; mRNA.
DR CCDS; CCDS17146.1; -.
DR AlphaFoldDB; Q9QY76; -.
DR SMR; Q9QY76; -.
DR IntAct; Q9QY76; 3.
DR MINT; Q9QY76; -.
DR STRING; 10090.ENSMUSP00000064699; -.
DR iPTMnet; Q9QY76; -.
DR PhosphoSitePlus; Q9QY76; -.
DR EPD; Q9QY76; -.
DR jPOST; Q9QY76; -.
DR MaxQB; Q9QY76; -.
DR PaxDb; Q9QY76; -.
DR PRIDE; Q9QY76; -.
DR ProteomicsDB; 298271; -.
DR ABCD; Q9QY76; 1 sequenced antibody.
DR MGI; MGI:1928744; Vapb.
DR eggNOG; KOG0439; Eukaryota.
DR InParanoid; Q9QY76; -.
DR PhylomeDB; Q9QY76; -.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR ChiTaRS; Vapb; mouse.
DR PRO; PR:Q9QY76; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QY76; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0033149; F:FFAT motif binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0090114; P:COPII-coated vesicle budding; ISO:MGI.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:MGI.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IBA:GO_Central.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:0044830; P:modulation by host of viral RNA genome replication; ISO:MGI.
DR GO; GO:0044828; P:negative regulation by host of viral genome replication; ISO:MGI.
DR GO; GO:0046725; P:negative regulation by virus of viral protein levels in host cell; ISO:MGI.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; ISO:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:MGI.
DR GO; GO:0019076; P:viral release from host cell; ISO:MGI.
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 Acetylation; Coiled coil; Endoplasmic reticulum; Isopeptide bond; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation; 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_0000213474"
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 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 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95292"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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; 26946 MW; 9D88CBC31701C84E CRC64;
MAKVEQVLSL EPQHELKFRG PFTDVVTTNL KLGNPTDRNV CFKVKTTVPR RYCVRPNSGV
IDAGASLNVS VMLQPFDYDP NEKSKHKFMV QSMFAPPDTS DMEAVWKEAK PEDLMDSKLR
CVFELPAENA KPHDVEINKI IPTSASKTEA PAAAKSLTSP LDDTEVKKVM EECRRLQGEV
QRLREESRQL KEEDGLRVRK AMPSNSPVAA LAATGKEEGL SARLLALVVL FFIVGVIIGK
IAL
