ID A0A452I0U2_9SAUR Unreviewed; 1036 AA.
AC A0A452I0U2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000021076.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000021076.1}
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|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR STRING; 38772.ENSGAGP00000021076; -.
DR Ensembl; ENSGAGT00000024004.1; ENSGAGP00000021076.1; ENSGAGG00000015480.1.
DR Ensembl; ENSGAGT00000024008.1; ENSGAGP00000021080.1; ENSGAGG00000015480.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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; 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; 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; 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:UP000291020}.
FT DOMAIN 79..211
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 458..485
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 853..880
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 1036 AA; 119015 MW; 349E7A2F1A6D352C CRC64;
MSLSRERRVN TSTLEKVAAD MSNLIENLDT RELHFEGDEV DADMLNDPKT TVGIPFSAIY
NTQGFKEPHI QTYLTGCPIK VRVLEVERFT STKKVPSPNV YTVEFTHGDF TWQVKRKFKN
FQEFHRELLR YKAFIRIPIP TRSHTVRRQT IKRGEARQMP SLPRTSENMV REEHFSSRRK
QLEDYLTKIL KMPMYRNYHG TMEFIGVSQL SFIHDLGPKG IEGMIMKRSG GHRIPGLNCC
GQGRVCYRWS KRWLVVKDSF LMYMKTDSGA ISFVLLVDKE FSIKIGKKET ETEYGLRIDN
LSRSLILKCN SYRHARWWGQ GIEEFIQKNG KNFLTHHRFG SYAAIQENTL AKWYVNAKGY
FEDVANAMEA AKEEIFITDW WLSPEIFMKR PVVEGNRWRL DCILKRKAQQ GVRIFVMLYK
EVELALGINS EYSKRTLMRL HPNIKVMRHP DHVSSSVYLW AHHEKLVVID QSVAFVGGID
LAYGRWDDDE HRLTDVGSVK RIAGTKSTST VNLIPTAEST EALALKTQPL GNLPQHRNSD
DILDSSRMKG IGKPKKFSRF SIYKHLQKHG LHHADSVSSI DGESDKGSIR SLKTGVGELF
GETRFWHGKD YCNFVFKDWV QLDKPFADFI DRYTTPRMPW HDISSVVHGK AARDVARHFI
QRWNFTKIMK PKYRSLSYPF LLPKSQRTAG EMKYQVPESV CANVQVLRSA ADWSAGIKYH
EESIHNAYVS VIENSKHYIY IENQFFISCA DDKVVSNKIG DTIARRILKA HRDNKRYRVY
VVIPLLPGFE GDISTGGGNA LQAIMHFNYR TMCRGDNSIL GQLKAEIGDQ WINYISFCGL
RTYAELDGNL VTELIYVHSK LLIADDNTVI IGSANINDRS MLGKRDSEMA IVVQDTETVP
SVMDGKDYKA GRFAQSLRLR CFRVVLGCST DLSADLQDPV SDRFFKEVWV ATAARNATIF
DKVFRCLPSD EVTNLAQLRD FIAKSKLVTQ DAAKAAEELK KIHGFLVQFP FHFLYEENLL
PSVGTKESMV PMEVWT
//
