ID K1RH25_CRAGI Unreviewed; 807 AA.
AC K1RH25;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D {ECO:0000256|ARBA:ARBA00015988};
DE EC=3.1.4.50 {ECO:0000256|ARBA:ARBA00012284};
DE AltName: Full=Glycosyl-phosphatidylinositol-specific phospholipase D {ECO:0000256|ARBA:ARBA00029753};
GN ORFNames=CGI_10021256 {ECO:0000313|EMBL:EKC40765.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC40765.1};
RN [1] {ECO:0000313|EMBL:EKC40765.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC40765.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-
CC myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a
CC 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:10832,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57997,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:58700; EC=3.1.4.50;
CC Evidence={ECO:0000256|ARBA:ARBA00034002};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the GPLD1 family.
CC {ECO:0000256|ARBA:ARBA00008652}.
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DR EMBL; JH818314; EKC40765.1; -; Genomic_DNA.
DR AlphaFoldDB; K1RH25; -.
DR HOGENOM; CLU_011756_0_0_1; -.
DR InParanoid; K1RH25; -.
DR OMA; CGMTTHN; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; IEA:UniProtKB-EC.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 2.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR001028; Gprt_PLipase_D.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR029002; PLPC/GPLD1.
DR PANTHER; PTHR23221; GLYCOSYLPHOSPHATIDYLINOSITOL PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR23221:SF7; PHOSPHATIDYLINOSITOL-GLYCAN-SPECIFIC PHOSPHOLIPASE D; 1.
DR Pfam; PF01839; FG-GAP; 3.
DR Pfam; PF00882; Zn_dep_PLPC; 1.
DR PRINTS; PR00718; PHPHLIPASED.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 2.
DR PROSITE; PS51470; FG_GAP; 3.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 27..127
FT /note="Phospholipase C/D"
FT /evidence="ECO:0000259|Pfam:PF00882"
SQ SEQUENCE 807 AA; 89132 MW; 0224D186C26018AE CRC64;
MKALSIVCFA CFLFFYDTEG AGIVTQLTLA EHALRYFDPE PEKNYSQIIN QHKTAFFGGT
PYPDAYYNEL CEFGMFSNIS DDTKSGPFLN ATINYINKRP KPWDKATEQL FSFMMGMMSN
QVSDSLWTSL GVEQGFLSTM GYTNFHGSVH KARKAGNFGM TTENSIAIGG DIVVVYLLSV
FDEIDEWYVP TDDLYEIYKE FYGSVQIDKS LIESCSALAL VTAYAEITGN AELFTVVADT
TDFLVDNLMD YFQGGLMDMA AWTNRKWHDA ITMIENGTRR KHDTAGSHSP ILPRPTTTPY
TGDLTIKDFR IEKSDRGISI RPGQKLKTRL KELKSHASAV KDAKSESNKL KDDYHWRVFF
EDQNYGSLLG KSLAAADVDG DGNVDVAIGA PGFSHKENIM AGRAYILYNS KNGYPKGYYY
DSVNINNATL GYNEIFDGEK EKHSRFGSSV ALLDVNLDGN VDLAVGASSY GDSGPLDYNG
KVYIYFGTGK DRKWTQKPDI ILTCQSKYCN LGYSLTAVDV NQDGHPDLVM GTPHYSQGNL
TQNGKVAILQ SKAISSGTTI PVESLARKIY GDQSYGWFGQ RLSGKNGVLL VNEPYFRICE
DPSCPGFSET DKQSVGRLHV YSFDTSSPMT NMSIAGRDAN DLAGQSTDFG DPFGNGSLVL
AVGVPGADVE GEIFTLPNEL TQAGKVILLK VEKGQLTEIA SYESDRRYSR FGFRVNFADV
NSDKIDDLLI GSPYRNDDPS NLFSLDRTYA SFLSDKNYFG DNFVTLPSLN VTQLIVSASI
CADVLEDFGT YSSFVYVFDT GSKPGDG
//
