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Database: UniProt
Entry: A8J056_CHLRE
LinkDB: A8J056_CHLRE
Original site: A8J056_CHLRE 
ID   A8J056_CHLRE            Unreviewed;       557 AA.
AC   A8J056;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Phospholipase A1 {ECO:0000256|RuleBase:RU367093};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU367093};
GN   ORFNames=CHLRE_09g391986v5 {ECO:0000313|EMBL:PNW78843.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW78843.1, ECO:0000313|Proteomes:UP000006906};
RN   [1] {ECO:0000313|EMBL:PNW78843.1, ECO:0000313|Proteomes:UP000006906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
CC   -!- FUNCTION: Acylhydrolase that catalyzes the hydrolysis of phospholipids
CC       at the sn-1 position. {ECO:0000256|RuleBase:RU367093}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU367093}.
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DR   EMBL; CM008970; PNW78843.1; -; Genomic_DNA.
DR   RefSeq; XP_001694655.1; XM_001694603.1.
DR   AlphaFoldDB; A8J056; -.
DR   PaxDb; 3055-EDP02239; -.
DR   EnsemblPlants; PNW78843; PNW78843; CHLRE_09g391986v5.
DR   GeneID; 5720240; -.
DR   Gramene; PNW78843; PNW78843; CHLRE_09g391986v5.
DR   KEGG; cre:CHLRE_09g391986v5; -.
DR   eggNOG; KOG4569; Eukaryota.
DR   HOGENOM; CLU_489507_0_0_1; -.
DR   InParanoid; A8J056; -.
DR   OrthoDB; 1210884at2759; -.
DR   Proteomes; UP000006906; Chromosome 9.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00519; Lipase_3; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   InterPro; IPR033556; PLA.
DR   PANTHER; PTHR31828; PHOSPHOLIPASE A1-IIGAMMA; 1.
DR   PANTHER; PTHR31828:SF1; PHOSPHOLIPASE A1-IIGAMMA; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU367093};
KW   Lipid degradation {ECO:0000256|RuleBase:RU367093};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU367093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006906}.
FT   DOMAIN          226..406
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   557 AA;  60385 MW;  F3C01C251C75461E CRC64;
     MGLQAPAKAT PGQTLRGHGA NGWKDAGWDY KQPKELSPQL RELLMHYGQL SQATYDNLGL
     NPCDAATWGY TTTKPGTSLI DYLTADYPLD PEARVTSKAP GTGDVYHLPL SDRLSPVIYA
     QAGGDDPDAA VAAVTAGAGS VAGVTAHSAT MARSVKSPWG LLDGGVDGVF GFLAGIPTAI
     IGGARPLFKQ NPATGRGTVP RPAFMGYVAI SPSAGAGSGG EVDVAFVWRG TIFKEEWAAN
     FGADQLVRWG DMSADGHALP WQVGVHRGFQ DLYLRAAPQP DAKTMTGAPP EGAKSVAPRE
     VVHNWIVELC RNHNVTTIST TGHSLGAALS TVSAFDIGEE VERLWAPANE KERAGWKTTA
     KPTVTAFAFA PPRVGNWNFV RTFRDKYNVR QLRICNVHDF VPKVPGGWVQ LLTTLLAKVG
     IDVYSDMDSA AARAFAGFYT WVSAATALLW RSRWGYFHAG TILEVDSNSD PAFQKVGTTP
     LSGFMQLPSG KHHNLEVYLY LLSLKGVKTD TTTRNKLFLN KGDDILNDTK TYTADWWRAP
     ADRHYRLRPQ DGRWEHY
//
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