LCF2_SCHPO
ID LCF2_SCHPO Reviewed; 689 AA.
AC Q9P7D7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 2;
DE EC=6.2.1.3;
DE AltName: Full=Fatty acid activator 2;
DE AltName: Full=Long-chain acyl-CoA synthetase 2;
GN Name=lcf2; ORFNames=SPBP4H10.11c;
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).
RN [3]
RP FUNCTION.
RX PubMed=18071249; DOI=10.1271/bbb.70442;
RA Fujita Y., Mita S., Ohtsuka H., Aiba H.;
RT "Identification of a fatty acyl-CoA synthetase gene, lcf2+, which affects
RT viability after entry into the stationary phase in Schizosaccharomyces
RT pombe.";
RL Biosci. Biotechnol. Biochem. 71:3041-3047(2007).
CC -!- FUNCTION: Esterification, concomitant with transport, of endogenous
CC long-chain fatty acids into metabolically active CoA thioesters for
CC subsequent degradation or incorporation into phospholipids. Plays an
CC important role in the determination of viability in the stationary
CC phase. {ECO:0000269|PubMed:18071249}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16823372}.
CC Vacuole membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane
CC protein {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The FACS motif is required for catalytic activity and substrate
CC specificity. {ECO:0000250|UniProtKB:P30624}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB83169.1; -; Genomic_DNA.
DR RefSeq; NP_596185.1; NM_001022104.2.
DR AlphaFoldDB; Q9P7D7; -.
DR SMR; Q9P7D7; -.
DR BioGRID; 277861; 7.
DR IntAct; Q9P7D7; 1.
DR MINT; Q9P7D7; -.
DR STRING; 4896.SPBP4H10.11c.1; -.
DR iPTMnet; Q9P7D7; -.
DR MaxQB; Q9P7D7; -.
DR PaxDb; Q9P7D7; -.
DR PRIDE; Q9P7D7; -.
DR EnsemblFungi; SPBP4H10.11c.1; SPBP4H10.11c.1:pep; SPBP4H10.11c.
DR GeneID; 2541350; -.
DR KEGG; spo:SPBP4H10.11c; -.
DR PomBase; SPBP4H10.11c; lcf2.
DR VEuPathDB; FungiDB:SPBP4H10.11c; -.
DR eggNOG; KOG1180; Eukaryota.
DR HOGENOM; CLU_000022_45_2_1; -.
DR InParanoid; Q9P7D7; -.
DR OMA; HIFEFIF; -.
DR PhylomeDB; Q9P7D7; -.
DR Reactome; R-SPO-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR Reactome; R-SPO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR PRO; PR:Q9P7D7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0090432; F:myristoyl-CoA ligase activity; IMP:PomBase.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IGI:PomBase.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Fatty acid metabolism; Golgi apparatus; Ligase;
KW Lipid metabolism; Membrane; Nucleotide-binding; Reference proteome;
KW Vacuole.
FT CHAIN 1..689
FT /note="Long-chain-fatty-acid--CoA ligase 2"
FT /id="PRO_0000311761"
FT MOTIF 518..567
FT /note="FACS"
FT /evidence="ECO:0000250|UniProtKB:P30624"
FT BINDING 252..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69451"
SQ SEQUENCE 689 AA; 75791 MW; 5F80C06F6EA92F87 CRC64;
MDIKDYYCVE TKDSKQPGES YIYRSIHSAG KLLDTPEDGV STVYDLLCTA AKNHGEKQAM
GSRKLIKENR EEREIIRKVD NEEVVEKKLW TTYELGPYEY ISFNKVYEIA LALGSGLVAS
GITSETTMLF FAATSAKWFT TAQGCSSQAI PIVTAYETLG EDGIYTSLDE CKSRAIFTDP
NLIPKLLGPL KQSTWVKLIV CSSTPSEDLV ELVKSTAPDV EIITYDNLLS LGKEKPQPPH
PPKADDICCY MYTSGSTGKP KGVVLLHRNI IAALGGINRI LSQHINVKDY VLAYLPLAHI
FEFIFEMCCL YWGGVLGYAS PRTLTDASVV NCKGDLTEFR PTVLIGVPAV YELIKKGILA
KVSSMPAHRQ KVFSGSLSLK QYLIERNLPG SAALDAIVFN KVKAATGGRL RYCISGGAAL
AASTQAFLSS CICPVLPGYG LTETCAGSFV LSPEQWHLYA NTVGFPIPSI EFKLVDIPDL
GYYTDSSPPR GEVWIRGPAV CNGYLNRPED NKAAFTEDGW FKTGDVGEIA KGNTLRLIDR
KKNIVKSLNG EYIALEKIEA QFFTSPLVSN VCAYADVNHA KPVVIVNPDE NGLRTYLTKN
SGSSFNGNPN DTLTNLCKDS GVQHLILKEL INIGKQQRLA SIEIPEGVVL SDFEWTAENN
FLTASRKVKR QVIVAHYSDE IQKAYSKKH
