BSCL2_RAT
ID BSCL2_RAT Reviewed; 377 AA.
AC Q5FVJ6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Seipin;
DE AltName: Full=Bernardinelli-Seip congenital lipodystrophy type 2 protein homolog;
GN Name=Bscl2 {ECO:0000250|UniProtKB:Q96G97};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:12584444},
RC GK {ECO:0000269|PubMed:12584444}, and Wistar {ECO:0000269|PubMed:12584444};
RX PubMed=12584444; DOI=10.1159/000068538;
RA Kaisaki P.J., Sebag-Montefiore L.M., Brown J.H., Magre J., Lathrop M.,
RA Capeau J., Gauguier D.;
RT "Localization, cDNA sequence and genomic organization of the rat seipin
RT gene (Bscl2) and sequence analysis in inbred rat models of Type 2 diabetes
RT mellitus.";
RL Cytogenet. Genome Res. 98:71-74(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342 AND SER-345, AND
RP IDENTIFICATION BY 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: 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}.
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DR EMBL; BC089942; AAH89942.1; -; mRNA.
DR RefSeq; NP_001012171.1; NM_001012171.1.
DR AlphaFoldDB; Q5FVJ6; -.
DR SMR; Q5FVJ6; -.
DR STRING; 10116.ENSRNOP00000061399; -.
DR GlyGen; Q5FVJ6; 2 sites.
DR iPTMnet; Q5FVJ6; -.
DR PhosphoSitePlus; Q5FVJ6; -.
DR PaxDb; Q5FVJ6; -.
DR PRIDE; Q5FVJ6; -.
DR Ensembl; ENSRNOT00000098204; ENSRNOP00000095921; ENSRNOG00000052393.
DR GeneID; 361722; -.
DR KEGG; rno:361722; -.
DR UCSC; RGD:1308135; rat.
DR CTD; 26580; -.
DR RGD; 1308135; Bscl2.
DR eggNOG; KOG4200; Eukaryota.
DR GeneTree; ENSGT00390000011639; -.
DR InParanoid; Q5FVJ6; -.
DR OrthoDB; 1390748at2759; -.
DR PhylomeDB; Q5FVJ6; -.
DR PRO; PR:Q5FVJ6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0060612; P:adipose tissue development; ISO:RGD.
DR GO; GO:0061725; P:cytosolic lipolysis; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
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:0043086; P:negative regulation of catalytic activity; ISO:RGD.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0014853; P:regulation of excitatory postsynaptic membrane potential involved in skeletal muscle contraction; ISO:RGD.
DR GO; GO:1905693; P:regulation of phosphatidic acid biosynthetic process; ISO:RGD.
DR GO; GO:0048515; P:spermatid differentiation; ISO:RGD.
DR InterPro; IPR009617; Seipin.
DR PANTHER; PTHR21212; PTHR21212; 1.
DR Pfam; PF06775; Seipin; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..377
FT /note="Seipin"
FT /id="PRO_0000191681"
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..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 279..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..377
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 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 377 AA; 42409 MW; 38118CF3C0779E35 CRC64;
MVNDPPVPAL LWAQEVGHVL AGRARRLMLQ FGVLFCTILL LLWVSVFLYG SFYYSYMPTV
SHLSPVHFYY RTDCDSSTAS LCSFPVANVS LTKSGRDRVL MYGQPYRVTL ELELPESPVN
QDLGMFLVTV SCYTRGGRII STSSRSVMLH YRSQLLQMLD TLVFSSLLLF GFAEQKQLLE
VELYSDYREN SYVPTTGAII EVHSKRVQMY GAYLRIHAHF TGLRYLLYNF PMTCAFVGVA
SNFTFLSVIA LFSYMQWVWG AVWPRHRFSL QVNIRQRDNS GHGAQRRISR HQPGQASTQQ
SDVTEDGESP EDPSGTEGQL SEEEKPEKQP LNGEGEQEPE ASDGSWEDAA LLTEASTSAL
APETLGSLRQ RQTCSSS
