GenomeNet

Database: UniProt
Entry: G3V8B1_RAT
LinkDB: G3V8B1_RAT
Original site: G3V8B1_RAT 
ID   G3V8B1_RAT              Unreviewed;       843 AA.
AC   G3V8B1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 89.
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   Name=Gpld1 {ECO:0000313|Ensembl:ENSRNOP00000024196.2,
GN   ECO:0000313|RGD:631371};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000024196.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000024196.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000024196.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000024196.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000024196.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; NP_001093982.1; NM_001100512.1.
DR   RefSeq; XP_006253985.1; XM_006253923.3.
DR   RefSeq; XP_008769848.1; XM_008771626.2.
DR   RefSeq; XP_008769850.1; XM_008771628.2.
DR   RefSeq; XP_008769851.1; XM_008771629.2.
DR   RefSeq; XP_008769853.1; XM_008771631.2.
DR   RefSeq; XP_017455969.1; XM_017600480.1.
DR   RefSeq; XP_017455970.1; XM_017600481.1.
DR   RefSeq; XP_017455971.1; XM_017600482.1.
DR   RefSeq; XP_017455972.1; XM_017600483.1.
DR   RefSeq; XP_017455973.1; XM_017600484.1.
DR   AlphaFoldDB; G3V8B1; -.
DR   Ensembl; ENSRNOT00000024196.4; ENSRNOP00000024196.2; ENSRNOG00000017702.4.
DR   GeneID; 291132; -.
DR   KEGG; rno:291132; -.
DR   CTD; 2822; -.
DR   RGD; 631371; Gpld1.
DR   GeneTree; ENSGT00390000013522; -.
DR   HOGENOM; CLU_011756_0_0_1; -.
DR   OMA; CGMTTHN; -.
DR   OrthoDB; 1332649at2759; -.
DR   TreeFam; TF335726; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000017702; Expressed in liver and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR   GO; GO:0004621; F:glycosylphosphatidylinositol phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR   GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
DR   GO; GO:0071467; P:cellular response to pH; IEA:Ensembl.
DR   GO; GO:0071401; P:cellular response to triglyceride; IEA:Ensembl.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0002430; P:complement receptor mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0006507; P:GPI anchor release; IEA:Ensembl.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
DR   GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0009749; P:response to glucose; IEA:Ensembl.
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; 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; 4.
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   PROSITE; PS51470; FG_GAP; 4.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          28..207
FT                   /note="Phospholipase C/D"
FT                   /evidence="ECO:0000259|Pfam:PF00882"
SQ   SEQUENCE   843 AA;  93667 MW;  A15C8DCB9EA2828F CRC64;
     MSVGRLWSGL LLLLLFFCSR SSSCGLSTHV EIGHRALQFL QLQDGRINYK ELLLEHQDAY
     QAGTVFPDAF YPSICKQGKF HEVSESTHWT PFLNASIHYI RENYPLPWEK DTEKLVAFLF
     GVTSHMVADV SWHSLGIEQG FLRTMGAIDF YDSYSEAHSA GDFGGDVLSQ FEFNFNYLSR
     RWYVPIQDLL RIYDNLYGRK VITKNVIVDC TYLQFLEMHG EMLAVSKLYS TYSTKSPFLV
     EQFQDYFLGG LDDMAFWSTN IYRLTSFMLE NGTSDCNLPE NPLFISCDGR KNHTLSSSKV
     QKNDFHRNLT MFISKDIRKN LNYTERGVFY STGSWAPESV TFMYQTLERN LRMMFTGNSQ
     TALKHVSSPS ASYTLSVPYA RLGWVMASAD LNQDGHGDLV VGAPGYSHPG RFQIGRVYII
     YGNDLGLPPI DLDLDKEAHG VLEGFQPSGR FGSALAVLDF NKDGLPDLAV GAPSVGSGQL
     TYNGSVYVYY GSQQGRLSSS PNITISCKDT YCNLGWALLA ADADGDGQHD LVISSPFAPG
     GGKQRGIVAA FYSHPRRNDK ESLTLDEADW KVNGEEDFSW FGYSLHGVTV ANRSLLLIGS
     PTWKNISRMA RSSHQKNQEK KSLGRVYGYF PPNRQREITI SGDKAMGKLG TSLSSGYVRV
     NGTLTQVLLV GAPTHDDVSK MAFLTMTLHQ GGATRMYELA PEKTQPALLS TFSGDRRFSR
     FGSVLHLTDL DDDGLDEIIM AAPLRITDVT SGLLGGEDGR VYIYNGMHTT LGDVTGKCKS
     WMTPCPEEKA QYVLISPEAS SRFGSSLVSV RSKERNQVVV AAGRSSWGAR LSGALHVYSF
     SSD
//
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