Bscl2
entrez
14705
canonical
uniprot
Q9Z2E9
canonical
ensembl
ENSMUSG00000071657
resolver
ensp
ENSMUSP00000083224
resolver
ensp
ENSMUSP00000123976
resolver
ensp
ENSMUSP00000125422
resolver
ensp
ENSMUSP00000127685
resolver
ensp
ENSMUSP00000290904
resolver
enst
ENSMUST00000086058
resolver
enst
ENSMUST00000159634
resolver
enst
ENSMUST00000160556
resolver
enst
ENSMUST00000171649
resolver
genesymbol
Bscl2
resolver
genesymbol_syn
Gng3lg
resolver
uniprot
A0A0R4J225
resolver
uniprot
Q3TY41
resolver
uniprot
Q3U1S5
resolver
uniprot
Q810B0
resolver
uniprot
Q9JJC2
resolver
uniprot
Q9JMF1
resolver
uniprot_entry
A0A0R4J225_MOUSE
resolver
uniprot_entry
BSCL2_MOUSE
resolver
uniprot_sec
Q3TY41
resolver
uniprot_sec
Q3U1S5
resolver
uniprot_sec
Q810B0
resolver
uniprot_sec
Q9JJC2
resolver
uniprot_sec
Q9JMF1
resolver
amino_acid_sequence
MVNDPPVPALLWAQEVGHVLAGRARRLMLQFGVLFCTILLLLWVSVFLYGSFYYSYMPTVSHLSPVHFHYRTDCDSSTASLCSFPVANVSLAKSGRDRVLMYGQPYRVTLELELPESPVNQDLGMFLVTVSCYTRGGRIISTSSRSVMLHYRSQLLQVLDTLLFSSLLLFGFAEQKQLLEVELYSDYRENSYVPTTGAIIEIHSKRIQMYGAYLRIHAHFTGLRYLLYNFPMTCAFVGVASNFTFLSVIVLFSYMQWVWGAVWPRHRFSLQVNIRQRDNSHHGAPRRISRHQPGQESTQQSDVTEDGESPEDPSGTEGQLSEEEKPEKRPLNGEEEQEPEASDGSWEDAALLTEANPPTSASASALAPETLGSLRQRPTCSSS
uniprot
proteins
function
FUNCTION: Mediates the formation of lipid droplets during the differentiation and maturation of adipocytes (PubMed:18458148, PubMed:19574402, PubMed:21551454, PubMed:22269949, PubMed:23458123, PubMed:41196993). Together with LDAF1, defines the sites of lipid droplet formation in the endoplasmic reticulum and promotes the aggregation of triacylglycerol molecules to form the core of a lipid droplet (nucleation) in the endoplasmic reticulum and drive budding of lipid droplets into the cytoplasm (By similarity). BSCL2 and LDAF1 also regulate protein and lipid delivery from the endoplasmic reticulum into growing lipid droplets: during early adipogenesis, BSCL2 inhibits GPAT3 and GPAT4 activity, thereby preventing phosphatidic acid accumulation that could antagonize PPARG and block differentiation (PubMed:41196993). This inhibition is then relieved by ADIG during adipocyte maturation, allowing expansion of lipid droplets (PubMed:41196993). Regulates the maturation of ZFYVE1-positive nascent lipid droplets and the function of the RAB18-ZFYVE1 complex in mediating the formation of endoplasmic reticulum-lipid droplet contacts (By similarity). Binds anionic phospholipids including phosphatidic acid (By similarity). {ECO:0000250|UniProtKB:Q96G97, ECO:0000269|PubMed:18458148, ECO:0000269|PubMed:19574402, ECO:0000269|PubMed:21551454, ECO:0000269|PubMed:22269949, ECO:0000269|PubMed:23458123, ECO:0000269|PubMed:41196993}.
uniprot
proteins
mass_dalton
43105
uniprot
proteins
protein_family
Seipin family
uniprot
proteins
pubmed
10679242
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18458148
uniprot
proteins
pubmed
19574402
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21551454
uniprot
proteins
pubmed
22269949
uniprot
proteins
pubmed
23049863
uniprot
proteins
pubmed
23458123
uniprot
proteins
pubmed
30901948
uniprot
proteins
pubmed
41196993
uniprot
proteins
pubmed
9790771
uniprot
proteins
sequence_length
383
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19574402, ECO:0000269|PubMed:23458123}; Multi-pass membrane protein {ECO:0000269|PubMed:41196993}. Lipid droplet {ECO:0000250|UniProtKB:Q96G97}. Note=Localizes at endoplasmic reticulum-lipid droplets (ER-LD) contact sites. {ECO:0000250|UniProtKB:Q96G97}.
uniprot
proteins
transmembrane_region
TRANSMEM 7..56; /note="Helical"; /evidence="ECO:0000269|PubMed:41196993, ECO:0007744|PDB:9C8D, ECO:0007744|PDB:9C8E"; TRANSMEM 222..261; /note="Helical"; /evidence="ECO:0000269|PubMed:41196993, ECO:0007744|PDB:9C8D, ECO:0007744|PDB:9C8E
uniprot
proteins