ID A0A7J8A177_MYOMY Unreviewed; 1039 AA.
AC A0A7J8A177;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 15.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=mMyoMyo1_015323 {ECO:0000313|EMBL:KAF6379876.1};
OS Myotis myotis (Greater mouse-eared bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6379876.1, ECO:0000313|Proteomes:UP000527355};
RN [1] {ECO:0000313|EMBL:KAF6379876.1, ECO:0000313|Proteomes:UP000527355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6379876.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6379876.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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 -!- SUBUNIT: Interacts with PIP5K1B. {ECO:0000256|ARBA:ARBA00065403}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00037811}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00037811}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00037811}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004444}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004444}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004444}. Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004577}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004577}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004577}.
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6379876.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JABWUV010000002; KAF6379876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8A177; -.
DR VEuPathDB; HostDB:GeneID_118675412; -.
DR Proteomes; UP000527355; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
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:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR GO; GO:0032534; P:regulation of microvillus assembly; IEA:TreeGrafter.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:TreeGrafter.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09844; PLDc_vPLD1_2; 1.
DR FunFam; 2.30.29.30:FF:000114; Phospholipase; 1.
DR FunFam; 3.30.1520.10:FF:000021; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000005; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000009; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000018; Phospholipase; 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; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
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:ARBA00023098};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000527355};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 81..212
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 219..328
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 459..486
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 856..883
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 152..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1039 AA; 119922 MW; 56C4A84DB94B7FB9 CRC64;
MSLKTEPIVN ISALQKIAAD MSNLIENLDT RELHFEGEEV DYDVSPSDPK TQEVYIPFSA
IYKTQGFKEP NVQTYLSGCP IKAQVLEVER FTSTTRARSI NLYTIELTHG EFKWQVKRKF
KHFEEFHREL LKYKAFIRIP IPTRRHTFRR QNVKEEPREM PSLPRSSENT MKEEQFLGRR
KQLEDYLTKL LKMPMYRNYH ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC
CGQGRVCYRW SRRWLIVKDS FLLYMKPDNG AIAFVLLVDK EFRIKVGKKE TDTKYGLRID
NLSRTLILKC NSYRHARLWA GAIEEFIQKY GSNFLKDHRF GSYATLQENI LAKWYVNAKG
YFEDIANAME EAKEEIFITD WWLSPEIFLK RPVVEGNRWR LDYILKRKAQ EGVRIFIILY
KEVELALGIN SEYSKRTLMR LHPNIKVMRH PDHVSSAVYL WAHHEKLVII DQSVAFVGGI
DLAYGRWDDN EHRLTDVGSV KRVISGPSLC SLPSSQAEIT DSMESLSLKD KKESAKNLLS
LKTADDMDSK LKGIGKPSKF SKFSLYRQLH RHHLHGSDSL SSIDSASNTG SVRSLQTGVG
ELHGETRFWH GKDYCNFVFK DWIQLDKPFA DFIDRYSTPR MPWHDIGSVV HGKAARDVAR
HFIQRWNFTK IMKPKYRSLS YPFLLPKSHT TAHELKYQVP GSVRANVQLL RSATDWSAGI
KYHEESIHTA YVHVIENSKH YIYIENQFFI SCADDKVVFN KIGDAIAQRI LRAYREGRRY
RVYVVIPLLP GFEGDIKTGG GNALQAIMHF NFRTMCRGEN SILGQLKVEL GNQWINYISF
CGLRTHAELE GNLVTELIYV HSKLLIADDN TVIIGSANIN DRSMLGKRDS EMAVIVEDTE
TVPSVMDGEE YQAGRFAHGL RLQCFRVVLG YLSDSSEDIQ DPVSDKFFKE VWVSTAARNA
TIYDKVFRCL PNDEVHTLIQ LRDFITKPIL AKEDPIRAEE ELKKIRGFLV QFPFNFLSGE
CLLPSVGTKE AMVPMEVWT
//
