SCS3_SCHPO
ID SCS3_SCHPO Reviewed; 250 AA.
AC Q9HGM4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Acyl-coenzyme A diphosphatase fit1 {ECO:0000305};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_03231};
DE AltName: Full=Acyl-coenzyme A diphosphatase scs3 {ECO:0000255|HAMAP-Rule:MF_03231};
DE AltName: Full=FIT family protein scs3 {ECO:0000255|HAMAP-Rule:MF_03231};
GN Name=fit1 {ECO:0000312|PomBase:SPBC543.08};
GN Synonyms=fit2b {ECO:0000255|HAMAP-Rule:MF_03231},
GN scs3 {ECO:0000255|HAMAP-Rule:MF_03231}; ORFNames=SPBC543.08;
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 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: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes
CC fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-
CC bisphosphate (By similarity). Preferentially hydrolyzes unsaturated
CC long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen
CC (By similarity). This catalytic activity is required for maintaining ER
CC structure and for lipid droplets (LDs) biogenesis, which are lipid
CC storage organelles involved in maintaining lipid and energy homeostasis
CC (By similarity). May directly bind to diacylglycerol (DAGs) and
CC triacylglycerol, which is also important for LD biogenesis (By
CC similarity). May support directional budding of nacent LDs from the ER
CC into the cytosol by reducing DAG levels at sites of LD formation (By
CC similarity). May play a role in the regulation of cell morphology and
CC cytoskeletal organization (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_03231}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-
CC phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58342, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:132023; Evidence={ECO:0000255|HAMAP-Rule:MF_03231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2
CC H(+) + S-(9Z-octadecenoyl)-4'-phosphopantetheine;
CC Xref=Rhea:RHEA:65564, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:58343, ChEBI:CHEBI:156553;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65565;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = adenosine 3',5'-
CC bisphosphate + 2 H(+) + S-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-4'-
CC phosphopantetheine; Xref=Rhea:RHEA:65568, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57368, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:156554; Evidence={ECO:0000255|HAMAP-Rule:MF_03231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65569;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+)
CC + S-hexadecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50032,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132018; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03231};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03231, ECO:0000269|PubMed:16823372}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03231}. Note=Enriched
CC at sites of lipid droplet (LD) biogenesis.
CC {ECO:0000250|UniProtKB:P53012}.
CC -!- SIMILARITY: Belongs to the FIT family. Fungal FIT2B/SCS3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03231}.
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DR EMBL; CU329671; CAC05250.1; -; Genomic_DNA.
DR RefSeq; NP_596796.1; NM_001023816.2.
DR AlphaFoldDB; Q9HGM4; -.
DR BioGRID; 277389; 9.
DR STRING; 4896.SPBC543.08.1; -.
DR MaxQB; Q9HGM4; -.
DR PaxDb; Q9HGM4; -.
DR EnsemblFungi; SPBC543.08.1; SPBC543.08.1:pep; SPBC543.08.
DR GeneID; 2540872; -.
DR KEGG; spo:SPBC543.08; -.
DR PomBase; SPBC543.08; fit1.
DR VEuPathDB; FungiDB:SPBC543.08; -.
DR eggNOG; KOG3750; Eukaryota.
DR HOGENOM; CLU_048143_0_0_1; -.
DR InParanoid; Q9HGM4; -.
DR OMA; ERCAWFL; -.
DR PhylomeDB; Q9HGM4; -.
DR Reactome; R-SPO-8964572; Lipid particle organization.
DR PRO; PR:Q9HGM4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0106399; F:acyl-coenzyme A diphosphatase activity; ISO:PomBase.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; ISS:PomBase.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; ISS:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:1900481; P:negative regulation of diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:1900480; P:regulation of diacylglycerol biosynthetic process; ISS:UniProtKB.
DR HAMAP; MF_03231; SCS3; 1.
DR InterPro; IPR019388; FIT.
DR InterPro; IPR046400; SCS3.
DR PANTHER; PTHR23129; PTHR23129; 1.
DR Pfam; PF10261; Scs3p; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..250
FT /note="Acyl-coenzyme A diphosphatase fit1"
FT /id="PRO_0000374041"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..58
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..160
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 161
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03231"
FT ACT_SITE 212
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03231"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 250 AA; 28787 MW; ED485F5A03F29418 CRC64;
MTEKTASHYW NEETSILKLR RKDILLFEIY ATTLLLGSIY SIYVDKWSIT SYFGNSKNLI
NLIFVKRGWF WTSLVYFYHA WDQKRNKIDF KFISRYIVAT LWWMFVTQWF IGPGLIDRTF
ALSGGSCKNF DGDSSVFIPL TASTCKGLNG SWSGGHDLSG HVFLLTHSSL FMLSENFSFI
LNNGIKATST KVLFGLLGLW WWMLFVTASF YHTTFEKCTG FFSGILEWSI VYVFSSRMPA
VADLLGSSDY
