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1.R.1.1.1
Membrane Contact Site (MCS).  Functions include lipid and ion transport between organelles as well as organelle positioning and division (Wu et al. 2018).
Constituents include:
Seipin, 398 aas and 2 - 4 TMSs, Q96G97;
Protrudin, 411 aas and 4 - 5 TMSs, Q5T4F4
Spastin (SPAST, ADPSP, FSP2, SPG4), 616 aas, 1 N-terminal TMS, Q9UBP0
Vesicle-associated membrane protein-associated protein A, (VAPA, VAP33). 249 aas, 1 C-terninal TMS, a member of TC family 9.B.17), Q9P0L0
Vesicle-associated membane protein associated, VAPB/C (see TC 9.B.17.1.1), 243 aas and 1 C-terminal TMS, O95292.
Dynamin 2 (Dyn2, Dnm2) GTPase, 870 aas, 1 TMS, see TC# 8.A.34.1.4, P50570
Mitofusin 2 (Mfn2, CPRP1) GTPase, 757 aas, 0 - 2 TMSs, (see TC# 1.N.6.1.2), O95140
Acyl-CoA binding domain-containing protein 5, ACBD5, 534 aas, 1 C-terminal TMS, Q5T8D3The heptad repeat domain 1 of Mitofusin has membrane destabilization function in mitochondrial fusion (Daste et al. 2018).

Accession Number:O95292
Protein Name:VAP-B/C
Length:243
Molecular Weight:27228.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Cell membrane1 / Single-pass type IV membrane protein2
Substrate

Cross database links:

Genevestigator: O95292
eggNOG: prNOG14301
HEGENOM: HBG446464
RefSeq: NP_004729.1   
Entrez Gene ID: 9217   
Pfam: PF00635   
OMIM: 182980  phenotype
605704  gene
608627  phenotype
KEGG: hsa:9217   

Gene Ontology

GO:0005789 C:endoplasmic reticulum membrane
GO:0005794 C:Golgi apparatus
GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0048487 F:beta-tubulin binding
GO:0019899 F:enzyme binding
GO:0046982 F:protein heterodimerization activity
GO:0042803 F:protein homodimerization activity
GO:0005198 F:structural molecule activity
GO:0008219 P:cell death
GO:0030968 P:endoplasmic reticulum unfolded protein resp...
GO:0045070 P:positive regulation of viral genome replica...
GO:0019048 P:virus-host interaction

References (14)

[1] “Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins.”  Nishimura Y.et.al.   9920726
[2] “Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.”  Hu R.-M.et.al.   10931946
[3] “The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.”  Clark H.F.et.al.   12975309
[4] “The DNA sequence and comparative analysis of human chromosome 20.”  Deloukas P.et.al.   11780052
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.”  Gevaert K.et.al.   12665801
[7] “Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B.”  Hamamoto I.et.al.   16227268
[8] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[9] “Phosphoproteome analysis of the human mitotic spindle.”  Nousiainen M.et.al.   16565220
[10] “Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis.”  Wang B.et.al.   19007248
[11] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[12] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[13] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
[14] “A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis.”  Nishimura A.L.et.al.   15372378
Structure:
2MDK   3IKK     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAKVEQVLSL EPQHELKFRG PFTDVVTTNL KLGNPTDRNV CFKVKTTAPR RYCVRPNSGI 
61:	IDAGASINVS VMLQPFDYDP NEKSKHKFMV QSMFAPTDTS DMEAVWKEAK PEDLMDSKLR 
121:	CVFELPAEND KPHDVEINKI ISTTASKTET PIVSKSLSSS LDDTEVKKVM EECKRLQGEV 
181:	QRLREENKQF KEEDGLRMRK TVQSNSPISA LAPTGKEEGL STRLLALVVL FFIVGVIIGK 
241:	IAL