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VAPB_BOVIN
ID   VAPB_BOVIN              Reviewed;         243 AA.
AC   A2VDZ9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 104.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-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; BC133497; AAI33498.1; -; mRNA.
DR   RefSeq; NP_001075892.1; NM_001082423.1.
DR   AlphaFoldDB; A2VDZ9; -.
DR   BMRB; A2VDZ9; -.
DR   SMR; A2VDZ9; -.
DR   STRING; 9913.ENSBTAP00000023164; -.
DR   PaxDb; A2VDZ9; -.
DR   PeptideAtlas; A2VDZ9; -.
DR   PRIDE; A2VDZ9; -.
DR   Ensembl; ENSBTAT00000023164; ENSBTAP00000023164; ENSBTAG00000017424.
DR   GeneID; 326580; -.
DR   KEGG; bta:326580; -.
DR   CTD; 9217; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017424; -.
DR   VGNC; VGNC:36764; VAPB.
DR   eggNOG; KOG0439; Eukaryota.
DR   GeneTree; ENSGT00940000155769; -.
DR   HOGENOM; CLU_032848_0_1_1; -.
DR   InParanoid; A2VDZ9; -.
DR   OMA; TQRMAFK; -.
DR   OrthoDB; 1332028at2759; -.
DR   TreeFam; TF317024; -.
DR   Reactome; R-BTA-1660661; Sphingolipid de novo biosynthesis.
DR   Reactome; R-BTA-8980692; RHOA GTPase cycle.
DR   Reactome; R-BTA-9013404; RAC2 GTPase cycle.
DR   Reactome; R-BTA-9013405; RHOD GTPase cycle.
DR   Reactome; R-BTA-9013408; RHOG GTPase cycle.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000017424; Expressed in hypothalamus and 102 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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:0033149; F:FFAT motif binding; IBA:GO_Central.
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:0061817; P:endoplasmic reticulum-plasma membrane tethering; IBA:GO_Central.
DR   GO; GO:0036498; P:IRE1-mediated unfolded protein response; 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   2: Evidence at transcript 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_0000308177"
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          186..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         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         160
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;  27158 MW;  1ECA446A771C28AA CRC64;
     MAKVEQVLSL EPQHELKFRG PFTDVVTTNL KLGNPTDRNV CFKVKTTAPR RYCVRPNSGI
     IDAGASINVS VMLQPFDYDP NEKSKHKFMV QSMFAPTDTS DMEAVWKEAK PEDLMDSKLR
     CVFELPAEND KPHDVEINKI IPTTASKTET PTVSKALSSS LDDTEVKKVM EECKRLQSEV
     QRLREENKQF KEEDGLRMRK TAQSNSPAPA SAMAGKEEGL STRLLALVVL FFIVGVIIGK
     IAL
 
 
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