ID A0A0D2UVB8_GOSRA Unreviewed; 1032 AA.
AC A0A0D2UVB8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=B456_011G193900 {ECO:0000313|EMBL:KJB72739.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB72739.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB72739.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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|ARBA:ARBA00000798,
CC ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; CM001750; KJB72739.1; -; Genomic_DNA.
DR RefSeq; XP_012455684.1; XM_012600230.1.
DR AlphaFoldDB; A0A0D2UVB8; -.
DR EnsemblPlants; KJB72739; KJB72739; B456_011G193900.
DR Gramene; KJB72739; KJB72739; B456_011G193900.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000032304; Chromosome 11.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
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; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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 PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 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; 2.
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:UP000032304}.
FT DOMAIN 470..497
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 895..922
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 1032 AA; 116990 MW; A0C36EEA678CA20D CRC64;
MESEQSMLVG GARYYQMQSE PLSSTISSSA ESTRIFDELP KATIVSVSRP DAGDISPMLL
SYTIEFRYKQ FKWRLMKKAS QVFYLHFALK RRLFIEEIHE KQEQVKEWLQ NLGIGEHAPV
VQDDDEPDDD ALLLQQDESV KNRDVPSSAA LPVIRPALGK QSSMSDRAKV AMQEYLNHFL
GNMDIVNSRE VCKFLEVSKL SFSPEYGPKL KEDYVMAKHL PKLAKDDDSD KCCACHWFNC
CNDNWQKVWA VLKPGFLALL ADPLDTKPLD IIVFDVLPAL AGNTEGRASL AAEVKERNPL
RHAFKVTCGS RSVRLRTKSS GKAKDWVAAI NDAGLRPPEG WCHPHRFGSF APQRGLTEDG
SQAQWFVDGR AAFDAIASSI EDAKSEIFIC GWWLCPELYL RRPFHEQASS RLDALLEAKA
KQGVQIYILL YKELALALKI NSVYSKRKLL SIHENVRVLR YPDHFSTGVY LWSHHEKIVI
VDYQICFIGG LDLCFGRYDT HEHKVGDNPP SVWPGKDYYN PRESEPNSWE DTVKDELDRG
KYPRMPWHDV HCALWGPSCR DVARHFVQRW NYAKRNKAPY EEAIPLLMPQ QHMVIPHYMG
RSKEIEFESK NVEENNKGIK RRDSFSSGSS LQDIPLLLSQ EAKELDSCTL SPKSNGLDTT
ASKSVSFAFG KSKIEPAVAD TPMKGFVDDL GSLDLYNEKS SDVKWQPEAE LSDSDWWEMQ
ERAAQGGFVD EAGQVGPRTS CRCQIIRSVS QWSAGTSQIE ESIHCGYCSL IDKAEHFVYI
ENQFFISGLS GDEIIRNRVL EALYRRIMQA YNDKKCFRVI IVIPLLPGFQ GGLDDAGAAS
VRAIMHWQYR TICRGQNSIL HNLYDLLGPK AHDYISFYGL RAHGKLFDGG PVATSPVYVH
SKVMIIDDRA ALIGSANIND RSLLGSRDSE IGVLIEDKEF VDSWMGGNPW KAGKFALSLR
LALWSEHLGL HRGEINQIID PIIDSSYKDI WVGTAKACAP TKHCVLERKT RSHYNRFRNS
PYKIRIISQR RG
//
