ID A0A091N8K0_9PASS Unreviewed; 830 AA.
AC A0A091N8K0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=N310_03118 {ECO:0000313|EMBL:KFP85776.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP85776.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP85776.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP85776.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK843828; KFP85776.1; -; Genomic_DNA.
DR RefSeq; XP_009078276.1; XM_009080028.1.
DR AlphaFoldDB; A0A091N8K0; -.
DR GeneID; 103807301; -.
DR KEGG; achl:103807301; -.
DR CTD; 2822; -.
DR OrthoDB; 1332649at2759; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
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; 3.
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; IPR008947; PLipase_C/P1_nuclease_dom_sf.
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; 1.
DR SUPFAM; SSF48537; Phospholipase C/P1 nuclease; 1.
DR PROSITE; PS51470; FG_GAP; 3.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..830
FT /note="Phosphatidylinositol-glycan-specific phospholipase
FT D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001878743"
FT DOMAIN 28..210
FT /note="Phospholipase C/D"
FT /evidence="ECO:0000259|Pfam:PF00882"
FT REPEAT 363..424
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 432..493
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 495..555
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 830 AA; 91734 MW; 22417A42ABF80EAA CRC64;
MAGAKIHSLL LLILYHCCQR CIPCGISTHV EIAHRALEFF IKHEGSVNYR QLLLNHQDAF
QAGSIYPDAF YSPICKRGIF HGVSEDTHWS PFLKASIDYI RRNYPQPWEG ATEKLVAFLF
GIASHMVADI SWHSLGIDQG FLKAMGEIDF HGSYSEAHSA GDFGGDVVSQ FELDFSYLAS
NWYVPVKDLA SIYKEFYGEE IITESTITDC TYLLFLELHG ERLAVGKLFP TYASKSPFLV
ENLHEYFLGG VDDMAFWTNN IFELTSHMLE NGTSGCYLPE NPLFINCKEE HKDNHINKQS
KHGHHKNRTS LLTETLEKNI NYTERGVHFN IQSWATNSLR LINRIVWRAL AATQQKSSKN
IFKPAASYFL TSPYARLGWA MISADLNQDG YEDLVVGAPG YSTMGHVQIG RVYVVYGNQS
GLPPEDMDLD RKADQVLQGH QLSGRFGSAL AVLDFNEDGV PDLAIGAPSV GSQFLTYKGA
VYVYFGTEGR GLASQPNVTI TCQYSYCNLG WSLLAADVDG DGNADLVVGS PYAPGGGQQR
GFVVAFYSYF NRSDQGTLSV QDANWMVEGE ENYAWFGFSL DSCQLENITL LLIGSPTWKS
CASCNPFSSD VRQSVGKVYG YNPPSTERWF AVTGEKEMGR MGLSLASGVM SVAGTARRVL
VVGAPTADSL SRMSFMSSVL HQAGLALVYD LTDSTKPALL STFSGDRRFS RFGGDVYLSD
LDNDGLDEMI VTSPLRTNGI MMLFGGAAGR VYIYNGKQAS WGNVTGHCKS WVSPCPEDWA
QYVLISPEEQ SRFGSSVITV KSERKKEVVV AAERSSAKAR LGGRLFVYSL
//