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Database: UniProt
Entry: A0A2R9AP34_PANPA
LinkDB: A0A2R9AP34_PANPA
Original site: A0A2R9AP34_PANPA 
ID   A0A2R9AP34_PANPA        Unreviewed;      1074 AA.
AC   A0A2R9AP34;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   Name=PLD1 {ECO:0000313|Ensembl:ENSPPAP00000017470.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000017470.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000017470.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000017470.1}
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   EMBL; AJFE02113057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02113058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02113059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02113060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008955556.1; XM_008957308.1.
DR   AlphaFoldDB; A0A2R9AP34; -.
DR   STRING; 9597.ENSPPAP00000017470; -.
DR   Ensembl; ENSPPAT00000040174.1; ENSPPAP00000017470.1; ENSPPAG00000031781.1.
DR   GeneTree; ENSGT00940000155015; -.
DR   OMA; EWRLDQI; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000240080; Chromosome 3.
DR   Bgee; ENSPPAG00000031781; Expressed in liver and 6 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR   GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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:0031670; P:cellular response to nutrient; IEA:Ensembl.
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   GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR   GO; GO:0032534; P:regulation of microvillus assembly; IEA:Ensembl.
DR   GO; GO:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl.
DR   CDD; cd01254; PH_PLD; 1.
DR   CDD; cd09842; PLDc_vPLD1_1; 1.
DR   CDD; cd09844; PLDc_vPLD1_2; 1.
DR   CDD; cd07296; PX_PLD1; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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; IPR001683; PX_dom.
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   Pfam; PF00787; PX; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR   SMART; SM00233; PH; 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   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080}.
FT   DOMAIN          81..212
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          459..486
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          891..918
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   1074 AA;  124199 MW;  C65F423790A2C1F5 CRC64;
     MSLKNEPRVN TSALQKIAAD MSNIIENLDT RELHFEGEEV DYDVSPSDPK IQEVYIPFSA
     IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTTRVPSI NLYTIELTHG EFKWQVKRKF
     KHFQEFHREL LKYKAFIRIP IPTRRHTFRR QNVREEPREM PSLPRSSENM IREEQFLGRR
     KQLEDYLTKI LKMPMYRNYH ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC
     CGQGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFKIKVGKKE TETKYGIRID
     NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTNFLKDHRF GSYAAIQENA LAKWYVNAKG
     YFEDVANAME EANEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY
     KEVELALGIN SEYTKRTLMR LHPNIKVMRH PDHVSSTVYL WAHHEKLVII DQSVAFVGGI
     DLAYGRWDDN EHRLTDVGSV KRVTSGPSLG SLPPAAMESM ESLRLKDKNE PDQNLPIQKS
     IDDVDSKLKG IGKPRKFSKF SLYKQLHRHH LHNADSISSI DSTSSYFNHY RSHHNLIHGL
     KPHFKLFHPS SESEQGLTRP HADTGSIRSL QTGVGELHGE TRFWHGKDYC NFVFKDWVQL
     DKPFADFIDR YSTPRMPWHD IASAVHGKAA RDVARHFIQR WNFTKIMKSK YRSLSYPFLL
     PKSQTTAHEL RYQVPGSVHA NVQLLRSAAD WSAGIKYHEE SIHAAYVHVI ENSRHYIYIE
     NQFFISCADD KVVFNKIGDA IAQRILKAHR ENQKYRVYVV IPLLPGFEGD ISTGGGNALQ
     AIMHFNYRTM CRGENSILGQ LKAELGNQWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL
     IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FARGLRLQCF
     RVVLGYLDDP SEDIQDPVSD KFFKEVWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI
     NKPVLAKEDP IRAEEELKKI RGFLVQFPFY FLSEESLLPS VGTKEAIVPM EVWT
//
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