ID W5K453_ASTMX Unreviewed; 1076 AA.
AC W5K453;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000002364.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000002364.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR AlphaFoldDB; W5K453; -.
DR STRING; 7994.ENSAMXP00000002364; -.
DR Ensembl; ENSAMXT00000002364.2; ENSAMXP00000002364.2; ENSAMXG00000002297.2.
DR eggNOG; KOG1329; Eukaryota.
DR GeneTree; ENSGT00940000155015; -.
DR HOGENOM; CLU_000690_2_0_1; -.
DR InParanoid; W5K453; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000002297; Expressed in bone element and 2 other cell types or tissues.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd06895; PX_PLD; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF202; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 3.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467}.
FT DOMAIN 74..209
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 456..483
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 893..920
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 493..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 123017 MW; 2B895EC988D426C7 CRC64;
MAQRVRQRPL RLERLDSSLD HYDLQDDAEE LDVSSSPDCC DGKQLESRNI PFQAIYSFVP
FKSVDCAVFL ENSPILVQVT EVERFTSTRV LNPNLYTIEL SHGNFSWKIK RRFKHFQALH
QELLKFKALL KIPLPSRIHS VKRRSFKGHK RSQGGHMPTL PRRPDALVKE EQLISRKMQL
EDYLKNILKR SLYRNHPATL EFLEVSQISF IQELGPKGIE GLILKKSGGN TFPVCYWCGS
NSVCYRWSKR WLVVKDSFVL YMRPEDGQVG TVILYDKGFH IKIGTQETGV RHGVTIENLC
RALTIKCSTY RQARWWGHSI DEFAQRFGQD FLRENRHGSF APVRENTTAQ WFVNAAGYFD
AIADALEGAK EEIFITAWWL SPEIFLKRPV VDGNTWRLDH VLKRKAEQGV KICVLLYKEV
EVVLGLNSEY TKKTLMGLHS NIMVIRHPDH VPSTALLWAH HEKSVVIDQS LAFLGGIDLA
YGRWDDSQHR LTDVGSVRRS PQPSPALSPS LTRQSATTVL EEDEEMKFSV VVEEDLLGGD
GAGELVEEPG ENSSSLTLPI TKLHTSPTEQ EKSRRSSETT ESKQCSSRNS VSSRTLPARE
WYTKSLSLRS SDSYSLGLHH SLLLPHDTSS LRSHISSTEL CGETRFWHGK DYCNFILKDW
VKLNKPFDDF IDRYKTPRMP WHDIGVAVHG KAARDIARHF IQRWNFTKLV KKRSGATGYP
CLMPKSLSTP SELPETRGKH TQANVQVLRS VCQWSIGTKV HEESIHLAYI SAIQNSKHFI
YIENQFFISC ADKSIHNSIG DALTERILRA YREKKKFRVY VVMPLLPGFE GDISSGGGQA
IKAIMYFNYR TMCRGDHSII ERLKRVMSDC WINYISFCGL RTHADLDGRL VTELIYVHSK
LMIVDDCTVI IGSANINDRS MLGKRDSEMA VVVEDTEFQD SLMDGGIYQA GRFALSLREE
CFRIVLGLMG DSSVDISDPM SDRFYKEVWM VTAAKNASVY DKVFRCLPTD AVLNYKILRE
YMSRSCMATE DPIQACAELR KVHGFLVQFP FYFLSEENLF PSLNSKEGIM PMELWT
//
