BSCLH_SCHPO
ID BSCLH_SCHPO Reviewed; 249 AA.
AC O14119;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 4.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Seipin homolog {ECO:0000250|UniProtKB:Q06058};
GN ORFNames=SPAC3A11.04 {ECO:0000312|PomBase:SPAC3A11.04};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in lipid metabolism and lipid droplet (LD)
CC morphology, number, and size. Facilitates initiation of LD formation,
CC and ensures that vectorial budding of LDs from the ER is directed
CC towards the cytoplasm. {ECO:0000250|UniProtKB:Q06058}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Concentrates at endoplasmic reticulum lipid droplet
CC junctions. {ECO:0000250|UniProtKB:Q06058}.
CC -!- SIMILARITY: Belongs to the seipin family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16380.3; -; Genomic_DNA.
DR PIR; T11626; T11626.
DR RefSeq; NP_594199.2; NM_001019623.2.
DR AlphaFoldDB; O14119; -.
DR SMR; O14119; -.
DR BioGRID; 279490; 13.
DR STRING; 4896.SPAC3A11.04.1; -.
DR PaxDb; O14119; -.
DR EnsemblFungi; SPAC3A11.04.1; SPAC3A11.04.1:pep; SPAC3A11.04.
DR PomBase; SPAC3A11.04; -.
DR VEuPathDB; FungiDB:SPAC3A11.04; -.
DR eggNOG; KOG4200; Eukaryota.
DR HOGENOM; CLU_043048_0_1_1; -.
DR InParanoid; O14119; -.
DR OMA; RWFMYTH; -.
DR PRO; PR:O14119; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0140042; P:lipid droplet formation; ISO:PomBase.
DR GO; GO:0034389; P:lipid droplet organization; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR InterPro; IPR009617; Seipin.
DR PANTHER; PTHR21212; PTHR21212; 1.
DR Pfam; PF06775; Seipin; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..249
FT /note="Seipin homolog"
FT /id="PRO_0000341580"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06058"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..212
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q06058"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06058"
SQ SEQUENCE 249 AA; 28673 MW; 0CB0BE795BB14236 CRC64;
MGYLVKLFKL VVWMLVIGLF SIPSLVSYVI FYDTVIPHSV IQYPVYFNYT TGLNFPTAEV
RLDHFSIDPR LPGTSLLQIK MPHSPRNSAM GNFMVSVDFQ DRNQRSLKQV KRTVLLPHRS
PIHEYLKLIV CSPLYFMGIL EETDIVNVRL FESETFAKSF NSITTLSVRF SVKNTPAQAI
VKIYSKDIEF YEATLAFASK LHGMRWFMYT HKVSAFLVFT SLFWFTGITS TIITYLIVSS
TSETKATRR
