位置:首页 > 蛋白库 > VAPB_RAT
VAPB_RAT
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   03-AUG-2022, entry version 149.
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   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: 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   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; Q9Z269; -.
DR   PRIDE; Q9Z269; -.
DR   ABCD; Q9Z269; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000007554; ENSRNOP00000007554; ENSRNOG00000005331.
DR   GeneID; 60431; -.
DR   KEGG; rno:60431; -.
DR   UCSC; RGD:68326; rat.
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; TQRMAFK; -.
DR   OrthoDB; 1332028at2759; -.
DR   PhylomeDB; Q9Z269; -.
DR   TreeFam; TF317024; -.
DR   Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
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 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
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: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   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   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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024