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Database: UniProt
Entry: A0A3P8SVX4_AMPPE
LinkDB: A0A3P8SVX4_AMPPE
Original site: A0A3P8SVX4_AMPPE 
ID   A0A3P8SVX4_AMPPE        Unreviewed;      1008 AA.
AC   A0A3P8SVX4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000016470.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000016470.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000016470.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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|PIRNR:PIRNR009376}.
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DR   AlphaFoldDB; A0A3P8SVX4; -.
DR   Ensembl; ENSAPET00000016916.1; ENSAPEP00000016470.1; ENSAPEG00000011649.1.
DR   GeneTree; ENSGT00940000155015; -.
DR   Proteomes; UP000265080; Chromosome 18.
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   Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
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; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF57; PHOSPHOLIPASE D1; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 3.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50035; PLD; 2.
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:UP000265080}.
FT   DOMAIN          201..310
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          441..468
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          825..852
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1008 AA;  115610 MW;  A27A87A19A66E4C8 CRC64;
     MLDKPQPTTS RLDLVNSDFS DATSASDEHD GIDMADLVES LDARELDLGE GEEIDYDGNW
     DSRIPFSAVY ATVGFKEANA KVYLPTVPIT ARILEVERFT TAQDRFNLSH HRSIELKHGE
     FTWVVKRKEK HFLELHRELR TYKTFMRIPL PSRRLAFAHT QTCTETKNTS LHVHIHTCFC
     YIVPMEFIDV SQLSFIHDLG PKGLEGMIHK RSGGHRIPGM NCCGHSQACY RWSKRWLVVK
     DSFLLYMKPD SGAISFVLLV DKEFSIKMDS KDTETKHGVR IDSLSRTLVF KCSSYRHARW
     WGQSIESFVR SHGKAFLRDH RFGSFAQEQE NIPAKWYVNG KTYMEDVADA LEEAKEEIFI
     TDWWLSPEIF LKRPVVEGNR WRLDCILKRK AQQGVRIFVM LYKEVELALG INSGYSKRTL
     MHLHPNIKVM RHPDHVSSSV YLWAHHEKIV VIDQSVAFVG GIDLAYGRWD DREHRLTDVG
     SVTRSVALEQ VRNTHSVSSA DGVSQSNGRG TPPSEPTDLP KLKGIGRNRM VRFSIYRHLH
     KHNLQHVDSV SSVDSAGSGS VRSLKTGVGE LQGNTRFWHG KDYCNFVYKD WIQLEKPFDD
     FIDRYTTPRM PWHDIASVVH GRGARDVARH FIQRWNFTKI MKPKYRSLFY PFLLPKSHSG
     ANEIRYQVPG CVNAKVQALR SASDWSAGIK YHEESIHTAY IQVIAKSKHY IYIENQFFIS
     CADNRTVYNK IGDAIIERVI RAHKEGKKYR VYVVTPLLPG FEGDITTGGG NAIQAVMHFN
     YRTMIRGEYS IISQLKKEMD DHWMNYISFA GLRTHAELEG RLVTELIYVH SKMLIADDNT
     VIIGSANIND RSMLGKRDSE VAVIVEDSEK VPSVMDGQEY EAGPYALQLR LECFRTILGG
     HTDTTIDISD PISDRFYKEV WMTTAGRNAT IYEKVFRCLP SSLVRNMSEL EQYQSKPGLA
     QTDLSRAQEE LRKIRGFLVQ FPLDFLSEHN LMPSVGTKEA MVPTEIWT
//
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