BSCL2_BOVIN
ID BSCL2_BOVIN Reviewed; 394 AA.
AC Q5E9P6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Seipin;
DE AltName: Full=Bernardinelli-Seip congenital lipodystrophy type 2 protein homolog;
GN Name=BSCL2 {ECO:0000312|EMBL:AAX08891.1};
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Plays a crucial role in the formation of lipid droplets (LDs)
CC which are storage organelles at the center of lipid and energy
CC homeostasis (By similarity). In association with LDAF1, defines the
CC sites of LD formation in the ER (By similarity). Also required for
CC growth and maturation of small nascent LDs into larger mature LDs (By
CC similarity). Mediates the formation and/or stabilization of endoplasmic
CC reticulum-lipid droplets (ER-LD) contacts, facilitating protein and
CC lipid delivery from the ER into growing LDs (By similarity). Regulates
CC the maturation of ZFYVE1-positive nascent LDs and the function of the
CC RAB18-ZFYVE1 complex in mediating the formation of ER-LD contacts (By
CC similarity). Binds anionic phospholipids including phosphatidic acid
CC (By similarity). Plays an important role in the differentiation and
CC development of adipocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q96G97, ECO:0000250|UniProtKB:Q9Z2E9}.
CC -!- SUBUNIT: Undecamer (an oligomer having eleven subunits) (By
CC similarity). Oligomerization is important for its function in lipid
CC droplet formation (By similarity). Interacts with LDAF1 to form an
CC oligomeric complex (By similarity). Interacts with RAB18 (By
CC similarity). Interacts with ZFYVE1 in a RAB18-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q96G97}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96G97}; Multi-pass membrane protein
CC {ECO:0000255}. Lipid droplet {ECO:0000250|UniProtKB:Q96G97}.
CC Note=Localizes at endoplasmic reticulum-lipid droplets (ER-LD) contact
CC sites. {ECO:0000250|UniProtKB:Q96G97}.
CC -!- SIMILARITY: Belongs to the seipin 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; BT020874; AAX08891.1; -; mRNA.
DR RefSeq; NP_001015589.1; NM_001015589.1.
DR AlphaFoldDB; Q5E9P6; -.
DR SMR; Q5E9P6; -.
DR STRING; 9913.ENSBTAP00000003254; -.
DR PaxDb; Q5E9P6; -.
DR GeneID; 513558; -.
DR KEGG; bta:513558; -.
DR CTD; 26580; -.
DR eggNOG; KOG4200; Eukaryota.
DR HOGENOM; CLU_049458_1_1_1; -.
DR InParanoid; Q5E9P6; -.
DR OrthoDB; 1390748at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; ISS:UniProtKB.
DR GO; GO:0019915; P:lipid storage; ISS:UniProtKB.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; ISS:UniProtKB.
DR InterPro; IPR009617; Seipin.
DR PANTHER; PTHR21212; PTHR21212; 1.
DR Pfam; PF06775; Seipin; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..394
FT /note="Seipin"
FT /id="PRO_0000191678"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..242
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 281..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96G97"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVJ6"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVJ6"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q96G97"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 394 AA; 44016 MW; DEE1A3E1C7008AA2 CRC64;
MVNDPPVPAL LWAQEMGHVM AGRARKLLLQ FGVFFCTILL LLWVSVFLYG SFYYSYMPTV
SHLSPVHFHY RTDCESSTSL LCSFPVANVT LAKGGRDRVL MYGQPYRVTL ELELPESPVN
QDLGMFLVTI SCYTRGGRII STSSRSVMLH YRSSLLQMLD TLVFSSLLLF GFAEQKQLLE
VELYPEYREN SYVPTTGAII EIHSKRIQMY GAYLRIHAHF TGLRYLLYNF PMTCAFVGVA
SNFTFLSVIV LFSYMQWVWG GIWPRQRLSL QVNIRNRKRS RKDIQRKVSA HQPGPQGQEE
SPQLSPVTED GESHADPSGT EGQLSEEEKT EQQPLSGEEE LEPEASDGSG SWEDAALLTE
ANLAASGSAP APETVGSSEP SAGSVRQRPI CSSS
