ID   SEI3_ARATH              Reviewed;         509 AA.
AC   Q8L615; O64707;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Seipin-3 {ECO:0000303|PubMed:26362606};
DE            Short=AtSEIPIN3 {ECO:0000303|PubMed:26362606};
GN   Name=SEI3 {ECO:0000305};
GN   OrderedLocusNames=At2g34380 {ECO:0000312|Araport:AT2G34380};
GN   ORFNames=F13P17.31 {ECO:0000312|EMBL:AAM14953.1},
GN   T31E10 {ECO:0000312|EMBL:AAC26703.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|EMBL:AAM20522.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX   PubMed=26362606; DOI=10.1105/tpc.15.00588;
RA   Cai Y., Goodman J.M., Pyc M., Mullen R.T., Dyer J.M., Chapman K.D.;
RT   "Arabidopsis SEIPIN proteins modulate triacylglycerol accumulation and
RT   influence lipid droplet proliferation.";
RL   Plant Cell 27:2616-2636(2015).
CC   -!- FUNCTION: Involved in lipid metabolism and lipid droplet (LD)
CC       morphology, number, and size. Supports the formation of small-sized LDs
CC       and modulates triacylglycerol accumulation. Induces probably a
CC       reorganization of the endoplasmic reticulum into LD-forming domains.
CC       {ECO:0000269|PubMed:26362606}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:26362606}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localized to the lipid droplet-forming sites.
CC       {ECO:0000269|PubMed:26362606}.
CC   -!- TISSUE SPECIFICITY: Expressed in seeds, seedlings, leaves, stems and
CC       roots. Not detected in flowers. {ECO:0000269|PubMed:26362606}.
CC   -!- DOMAIN: The N-terminal domain (1-230) determines the lipid droplet
CC       size. {ECO:0000269|PubMed:26362606}.
CC   -!- SIMILARITY: Belongs to the seipin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC26703.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAM14953.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC004077; AAC26703.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AC004481; AAM14953.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002685; AEC08966.1; -; Genomic_DNA.
DR   EMBL; AY099671; AAM20522.1; -; mRNA.
DR   EMBL; BT000262; AAN15581.1; -; mRNA.
DR   PIR; T02326; T02326.
DR   RefSeq; NP_850230.1; NM_179899.1.
DR   AlphaFoldDB; Q8L615; -.
DR   IntAct; Q8L615; 1.
DR   STRING; 3702.AT2G34380.1; -.
DR   PaxDb; Q8L615; -.
DR   PRIDE; Q8L615; -.
DR   ProteomicsDB; 232783; -.
DR   EnsemblPlants; AT2G34380.1; AT2G34380.1; AT2G34380.
DR   GeneID; 818001; -.
DR   Gramene; AT2G34380.1; AT2G34380.1; AT2G34380.
DR   KEGG; ath:AT2G34380; -.
DR   Araport; AT2G34380; -.
DR   TAIR; locus:2040884; AT2G34380.
DR   eggNOG; KOG4200; Eukaryota.
DR   HOGENOM; CLU_035656_1_1_1; -.
DR   InParanoid; Q8L615; -.
DR   OMA; LAIRIAW; -.
DR   OrthoDB; 782411at2759; -.
DR   PhylomeDB; Q8L615; -.
DR   PRO; PR:Q8L615; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8L615; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0140042; P:lipid droplet formation; IGI:TAIR.
DR   GO; GO:0034389; P:lipid droplet organization; IMP:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR   GO; GO:0009846; P:pollen germination; IGI:TAIR.
DR   GO; GO:0080155; P:regulation of double fertilization forming a zygote and endosperm; IGI:TAIR.
DR   GO; GO:0010162; P:seed dormancy process; IGI:TAIR.
DR   InterPro; IPR009617; Seipin.
DR   PANTHER; PTHR21212; PTHR21212; 1.
DR   Pfam; PF06775; Seipin; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid metabolism; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..509
FT                   /note="Seipin-3"
FT                   /id="PRO_0000434817"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          33..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  57416 MW;  14FB8169306A7597 CRC64;
     MESESESSST HSSCDRFLDA EDEFFYDSFS NHYDCLNSSP PANLRRRRLP MDTDSSSSSS
     TSSLESCEKR STVGENDELE VSLVDFETIE IDVDVTDSAN SSIDSISEKG EDFEVIDSCT
     DTEKNMGEND SGRVDPFTVT TLNDERGEIY TGPEYTSTDW SLTSLVIRSI EFQVSLMITF
     IRFPPWLISK CLSFVFDPYR TMRRGRRYLV SWIVGLCDSG LKDDKPVLEL VRRVTWGLFC
     AVYVGIMLFA LLVSAFMISG FVITYLAHEP LVIKESLNFD YTKSSPEAYV PISSCAGVAF
     GLSGKESIET GKVKGLKDRT EITVSMTLPE SEYNRNLGMF QVRVDFLSAS GHVLASSRRP
     CMVKFSSEPI RLVQTLLKIA PLVTGYVSEI QTLNLKLKGL VEKDIIPTAC LKIMIEQRAE
     FRPGAGIPEI YDASLFLESK LPFLKRIIWN WRKTLFVWIS MSLFIMELLF ALVFFRPLII
     PRTGQRTQQR DGTHSINNNL YLDGQAGSR