VAPB_PIG
ID VAPB_PIG Reviewed; 243 AA.
AC A5GFS8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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. Interacts (via MSP domain) with ZFYVE27. Interacts
CC with KIF5A in a ZFYVE27-dependent manner. 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:O95292}.
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; CR956404; CAN13351.1; -; Genomic_DNA.
DR RefSeq; NP_001116685.1; NM_001123213.1.
DR AlphaFoldDB; A5GFS8; -.
DR BMRB; A5GFS8; -.
DR SMR; A5GFS8; -.
DR STRING; 9823.ENSSSCP00000008012; -.
DR PaxDb; A5GFS8; -.
DR PeptideAtlas; A5GFS8; -.
DR PRIDE; A5GFS8; -.
DR Ensembl; ENSSSCT00070037731; ENSSSCP00070031559; ENSSSCG00070019099.
DR Ensembl; ENSSSCT00070037773; ENSSSCP00070031593; ENSSSCG00070019099.
DR GeneID; 100144536; -.
DR KEGG; ssc:100144536; -.
DR CTD; 9217; -.
DR eggNOG; KOG0439; Eukaryota.
DR HOGENOM; CLU_032848_0_1_1; -.
DR InParanoid; A5GFS8; -.
DR OrthoDB; 1332028at2759; -.
DR TreeFam; TF317024; -.
DR Reactome; R-SSC-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-SSC-8980692; RHOA GTPase cycle.
DR Reactome; R-SSC-9013106; RHOC GTPase cycle.
DR Reactome; R-SSC-9013404; RAC2 GTPase cycle.
DR Reactome; R-SSC-9013405; RHOD GTPase cycle.
DR Reactome; R-SSC-9013408; RHOG GTPase cycle.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 17.
DR Genevisible; A5GFS8; SS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IBA:GO_Central.
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: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; -; 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 3: Inferred from homology;
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_0000308178"
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 REGION 185..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..196
FT /evidence="ECO:0000255"
FT COMPBIAS 185..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95292"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95292"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95292"
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; 27053 MW; 36DAA84CF63E0BB8 CRC64;
MAKVEQVLSL EPQHELKFRG PFTDVVTTNL KLGNPTDRNV CFKVKTTAPR RYCVRPNSGI
IDAGASINVS VMLQPFDYDP NEKSKHKFMV QSMFAPADTS DMEAAWKEAK PEDLMDSKLR
CVFELPAEND KPHDVEINKI ISTTASKTET PVVSKALSSA LDDTEVKKVM EECKRLQSEV
QRLREENKQL KEEDGLRMRK PVLSNSPAPA PATPGKEEGL STRLLALVVL FFIVGVIIGK
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