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SEI1_ARATH
ID   SEI1_ARATH              Reviewed;         368 AA.
AC   Q9FFD9;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Seipin-1 {ECO:0000303|PubMed:26362606};
DE            Short=AtSEIPIN1 {ECO:0000303|PubMed:26362606};
GN   Name=SEI1 {ECO:0000305};
GN   OrderedLocusNames=At5g16460 {ECO:0000312|Araport:AT5G16460};
GN   ORFNames=MQK4.19 {ECO:0000312|EMBL:BAB09613.1};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
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   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. Facilitates the formation of large-sized
CC       LDs 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 and young seedlings. Not
CC       detected in leaves. {ECO:0000269|PubMed:26362606}.
CC   -!- DOMAIN: The N-terminal domain (1-98) determines the lipid droplet size.
CC       {ECO:0000269|PubMed:26362606}.
CC   -!- MISCELLANEOUS: Knockdown mutants have a reduced accumulation of oil per
CC       seed and a reduced overall seed size. {ECO:0000269|PubMed:26362606}.
CC   -!- SIMILARITY: Belongs to the seipin family. {ECO:0000305}.
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DR   EMBL; AB005242; BAB09613.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92296.1; -; Genomic_DNA.
DR   RefSeq; NP_197150.1; NM_121651.2.
DR   AlphaFoldDB; Q9FFD9; -.
DR   SMR; Q9FFD9; -.
DR   STRING; 3702.AT5G16460.1; -.
DR   PaxDb; Q9FFD9; -.
DR   PRIDE; Q9FFD9; -.
DR   ProteomicsDB; 232892; -.
DR   EnsemblPlants; AT5G16460.1; AT5G16460.1; AT5G16460.
DR   GeneID; 831507; -.
DR   Gramene; AT5G16460.1; AT5G16460.1; AT5G16460.
DR   KEGG; ath:AT5G16460; -.
DR   Araport; AT5G16460; -.
DR   TAIR; locus:2171412; AT5G16460.
DR   eggNOG; KOG4200; Eukaryota.
DR   HOGENOM; CLU_035656_0_0_1; -.
DR   InParanoid; Q9FFD9; -.
DR   OMA; KSQPPWY; -.
DR   OrthoDB; 782411at2759; -.
DR   PhylomeDB; Q9FFD9; -.
DR   PRO; PR:Q9FFD9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FFD9; 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:0048316; P:seed development; IMP:TAIR.
DR   GO; GO:0010162; P:seed dormancy process; IGI:TAIR.
DR   GO; GO:0010344; P:seed oilbody biogenesis; IMP:UniProtKB.
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..368
FT                   /note="Seipin-1"
FT                   /id="PRO_0000434815"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          344..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  42479 MW;  5F303998BF779C7A CRC64;
     MRILQNKTMK EQDNQLKIPE PLRADWFMVL VTIQADLIYN ALVVLSSPFF LLYRSYRRAV
     VTVSAAEKAV KRAPAQIAGG AGRVVRRTWF GILGACHVSM VMVLALILAV VIGVGIVSLY
     VEKPVVVRDR LFFDYTEENP SAVFSFDKKK RSFSVPVGHS VHVSLVLWMP ESEINRRIGV
     FQLKVELLSL KGETIARSSQ PCMLRFRSKP IRLARTFVMS VPLIAGIANE AQTMRIDALK
     HQEKMPRTKA VRATLIPRAQ TRTLPQLYEA EIVINSKPPW IKRMAYNWKW TLCVWTSMYL
     YVAILTALLW CFRPVLFPYT SSRTISESEN LEIEVVEEEQ EQVMERRRRE RRNQPRRRNF
     ATTQKSYT
 
 
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