ID F6WA81_CIOIN Unreviewed; 1145 AA.
AC F6WA81;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000026201.2, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000026201.2}
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|ARBA:ARBA00000798,
CC ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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; EAAA01001234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EAAA01001235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6WA81; -.
DR STRING; 7719.ENSCINP00000026201; -.
DR Ensembl; ENSCINT00000026447.2; ENSCINP00000026201.2; ENSCING00000002858.3.
DR GeneTree; ENSGT00940000169500; -.
DR HOGENOM; CLU_000690_2_0_1; -.
DR InParanoid; F6WA81; -.
DR OMA; EWRLDQI; -.
DR TreeFam; TF300589; -.
DR Proteomes; UP000008144; Chromosome 14.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR CDD; cd06895; PX_PLD; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
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:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 2.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT DOMAIN 27..166
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 482..509
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 960..987
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 1145 AA; 131830 MW; AABA31597F01F71B CRC64;
IPYMSIYGSP SRLIVGVGSP YLAKTPLSVN ITCVKHDVTY RHPLNPNLYT IELAHGQFTW
TIYRRYKHFI ELHEKLWTYR ASLKIPLPSK KHRRRRLTTH GMPKKESKMP QFPKTPEILV
SSEDLDKRKG KVLVENMCDS IQIPVFDSTC YSHAILATLV NIKLLKFVCC GLPNQQSYIC
SPVEKNYIIN NIDQLCLYLQ AMLKSRMYRK HPATVSNYWV VQAFPNYCIV THREGVINKR
SGGHKEWGIM AWLCCQSGIY AHCININAYS FCLTFRIKWF VVKDTFIAYL DPSQDKIKGV
LLFDAVLNVL HQAPSSRLVI SNISRSLNVD CWTDRQALDW KRAIEHSFNN LSYGLTAPDI
RHQSFAPPRE DSYAYWFVDG RSYFDAVADA IEEAREEIYI TDWWLSPEIY MKRPIVHGDH
WRLDKLLKRK AVEGVKIYVQ LYKEVEMAVG LDSAYTKRTL NEMHPTNIRV MRHPDLTPGE
TLLWAHHEKI VVIDQSIAFV GGIDLCYGRW DDQDHKLTDT GGVCSTDFLP RTLKTMVLFF
EFEIIEQGKF SLCYHYHIYQ LPRAPSPVEP EEPAATGFKK RLRSLRPRKK VRDQSFIIST
QGCKPFGSGR FLFGLRVSVA TMSRMIDRLR FNERSRAPFT ADTHSPINDK NESYSFYTYF
IIHYKCVTND CFMVHKIRVN LNAAPLQASS VLTQYKDMVN QVEYAAQSKL WIGKDYNNFI
LKDLTQLDDP FGDVMDRLKT PRMPWHDIAC VTYGKAARDA ARHFIQRWNY TKIQKAKKGE
HISFLLPKSY SDDAFNLPKE LMRPEAVQAK ILRSSCEWSA GLSEVDRSIQ NAYIAAIDNS
QHFIYIENQF FISCLRNAQV GNQICTTLVR RIIRAHKNKK AFRVYVVMPL LPGFEGDISK
SGKSQAIRTV LHWQYKSINR GSASMFEELD KEIGPGNAWR YISFCGLRTH SKLMGKPITE
IIYVHSKMMI VDDRLVIIGS ANINDRSMSG TRDSEVAMLV EDSQLVDSTM DGKPCKVGVY
ASSLRRRCFA EHLGLLPDDY DGRYILEDVA SEAFFKDVWM KTAAVNTTSY EKVFCCVPSD
YVRKLTDIES FQKTPLVESD PEAAETTLQK IKGYLVLLPL LFLIDEDLTP DVMTKEAMAP
TDLWT
//
