ID A0A158NN69_ATTCE Unreviewed; 1099 AA.
AC A0A158NN69;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=phospholipase A1 {ECO:0000256|ARBA:ARBA00013179};
DE EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
GN Name=105622157 {ECO:0000313|EnsemblMetazoa:XP_012058977.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012058977.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012058977.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000256|ARBA:ARBA00000111};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
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DR EMBL; ADTU01021058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012058977.1; XM_012203587.1.
DR AlphaFoldDB; A0A158NN69; -.
DR EnsemblMetazoa; XM_012203587.1; XP_012058977.1; LOC105622157.
DR GeneID; 105622157; -.
DR KEGG; acep:105622157; -.
DR eggNOG; ENOG502SHK7; Eukaryota.
DR InParanoid; A0A158NN69; -.
DR OrthoDB; 3669154at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610:SF178; FI22312P1; 1.
DR PANTHER; PTHR11610; LIPASE; 1.
DR Pfam; PF00151; Lipase; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1099
FT /note="phospholipase A1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007629461"
FT DOMAIN 69..394
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT REGION 831..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 123576 MW; 036CCE3C6081E815 CRC64;
MIGKLLLTLW ILRWTSFIAE PIAGQVFSSF DESLDEKNDA EIFRAVVESM RQWMLHKRVN
HRGKREVSKV CYEDIGCFED TGPFSYLEML PSPPKDVGTR FIVYGSRKAR SIPMEVPADN
INDNVRRAID PNLPTKVIVH GFGSDCNHLW VYDMRSALMS IHDCNIVCVD WGPGSAVPNY
VRAAANTRLV GRQLAKLIRS LNVPLEKVHL IGFSLGAHVA GFAGAELGNV SRITGLDPAG
PLFESHDPRV RLDATDANFV DVIHSNGEQL ILGGLGSWQP MGDVDYYPNG GKMQSGCSNI
FVGAVSDIIW SSAVEGRSLC NHRRAYKFFT DSVSPKCRFP AFPCEQGYDG LLKGDCFPCG
MDGTDRPCGD MGYYSNESPA RGQLYLVTRD EEPFCAHQYQ IKVYNSRSER STKTYGKLQI
TLVGKSSYND TFAMTRKDEE LLVGAILQKI VVPHPAVTHL EAIEIKYTAY SGWISSGLVS
WTIDKVAIID SFGKILSVCK KGLILESARS VYLPLYPGEC NIPLDTDNST VSSSVPILEH
VEVENRQGGI GPFTKEQNYD TKDPPRYSME ILPTERTSQR RNLGPFTKEQ NRRVSEIETV
TSFEDAEKRR NVANPWIILD ISGDGDSNSL ENAESEQGRS FSGATNLIYH ASTVSERVVE
TTVTTVATTT EYLSEIREPV LRPSKKDAGR SLKLPEITEP ILRPRATRHN TRNEVISHEK
QHDEIQETSS TSTRAFTVQF LPERLAGILA QAERYARQTL LPLISQYTPS FVTGIRHEEP
KYFPLLNDIV RPRSIDNTAE ISRTTSRSWN RDQILRVEIG QRKSEKFNLD DKRYEESSSA
QTEKNKNEHT ISRIEESPMI VEAVYPEKSV STNSTSLETK AASKDSDWQP IGEPISESTL
KNSLSRRDSN VSRSLDWSLD HSHNWTLQKA NANVETEVKP DNDWIPIMIK SDIISTTARI
ASELSSEETV TTTIPTMEID TVENSQKSAE VNIFDEAKKE TTIANTYERK FIPLIDFEET
TSDLSSLTDI NDVSSSTTVA THIQKIPRYK TTKSARNIIH PTMMFPYAYE RKNDPRTRYI
PLIPEEDMGR AYPMLERER
//
