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PIGA_ARATH
ID   PIGA_ARATH              Reviewed;         447 AA.
AC   Q94BX4; Q9M1U9;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit A;
DE            EC=2.4.1.198;
DE   AltName: Full=GlcNAc-PI synthesis protein;
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class A protein;
GN   Name=PIGA {ECO:0000305}; Synonyms=SETH2 {ECO:0000303|PubMed:14671020};
GN   OrderedLocusNames=At3g45100 {ECO:0000312|Araport:AT3G45100};
GN   ORFNames=T14D3.40 {ECO:0000312|EMBL:CAB72148.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=24905498; DOI=10.1111/tpj.12577;
RA   Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA   Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA   Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA   Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA   Loque D., Scheller H.V., Heazlewood J.L.;
RT   "The plant glycosyltransferase clone collection for functional genomics.";
RL   Plant J. 79:517-529(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=14671020; DOI=10.1105/tpc.014407;
RA   Lalanne E., Honys D., Johnson A., Borner G.H.H., Lilley K.S., Dupree P.,
RA   Grossniklaus U., Twell D.;
RT   "SETH1 and SETH2, two components of the glycosylphosphatidylinositol anchor
RT   biosynthetic pathway, are required for pollen germination and tube growth
RT   in Arabidopsis.";
RL   Plant Cell 16:229-240(2004).
CC   -!- FUNCTION: Necessary for the synthesis of N-acetylglucosaminyl-
CC       phosphatidylinositol, the very early intermediate in GPI-anchor
CC       biosynthesis (Probable). Required for pollen germination and pollen
CC       tube growth (PubMed:14671020). {ECO:0000269|PubMed:14671020,
CC       ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-
CC         acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-
CC         phosphatidyl-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:14789,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57265, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58223; EC=2.4.1.198;
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       pollen grains. {ECO:0000269|PubMed:14671020}.
CC   -!- DISRUPTION PHENOTYPE: Defective in pollen germination and pollen tube
CC       growth. {ECO:0000269|PubMed:14671020}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB72148.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; KJ138805; AHL38745.1; -; mRNA.
DR   EMBL; AL138649; CAB72148.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE77993.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77994.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64654.1; -; Genomic_DNA.
DR   EMBL; AY039602; AAK62657.1; -; mRNA.
DR   EMBL; AY081726; AAL87379.1; -; mRNA.
DR   PIR; T47450; T47450.
DR   RefSeq; NP_001326667.1; NM_001339193.1.
DR   RefSeq; NP_566874.1; NM_114379.3.
DR   RefSeq; NP_850658.1; NM_180327.2.
DR   AlphaFoldDB; Q94BX4; -.
DR   SMR; Q94BX4; -.
DR   IntAct; Q94BX4; 1.
DR   STRING; 3702.AT3G45100.1; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PaxDb; Q94BX4; -.
DR   PRIDE; Q94BX4; -.
DR   ProteomicsDB; 236146; -.
DR   EnsemblPlants; AT3G45100.1; AT3G45100.1; AT3G45100.
DR   EnsemblPlants; AT3G45100.2; AT3G45100.2; AT3G45100.
DR   EnsemblPlants; AT3G45100.3; AT3G45100.3; AT3G45100.
DR   GeneID; 823646; -.
DR   Gramene; AT3G45100.1; AT3G45100.1; AT3G45100.
DR   Gramene; AT3G45100.2; AT3G45100.2; AT3G45100.
DR   Gramene; AT3G45100.3; AT3G45100.3; AT3G45100.
DR   KEGG; ath:AT3G45100; -.
DR   Araport; AT3G45100; -.
DR   TAIR; locus:2096875; AT3G45100.
DR   eggNOG; KOG1111; Eukaryota.
DR   HOGENOM; CLU_009583_19_0_1; -.
DR   InParanoid; Q94BX4; -.
DR   OMA; SHFWMSG; -.
DR   OrthoDB; 719531at2759; -.
DR   PhylomeDB; Q94BX4; -.
DR   BioCyc; ARA:AT3G45100-MON; -.
DR   UniPathway; UPA00196; -.
DR   PRO; PR:Q94BX4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q94BX4; baseline and differential.
DR   GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009846; P:pollen germination; IMP:UniProtKB.
DR   GO; GO:0009860; P:pollen tube growth; IMP:UniProtKB.
DR   CDD; cd03796; GT4_PIG-A-like; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR039507; PIG-A/GPI3.
DR   InterPro; IPR013234; PIGA_GPI_anchor_biosynthesis.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF08288; PIGA; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..447
FT                   /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT                   subunit A"
FT                   /id="PRO_0000438104"
FT   TOPO_DOM        1..387
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        409..447
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  50424 MW;  C7BD0E8821D4DFB1 CRC64;
     MAEPPKLRVL MVSDFFFPNF GGVENHIYYL SQCLLKLGHK VVVMTHAYGN RSGVRYMTGG
     LKVYYVPWRP FVMQTTFPTV YGTLPIVRTI LRREKITVVH GHQAFSTLCH EALMHARTMG
     YKVVFTDHSL YGFADVGSIH MNKVLQFSLA DIDQAICVSH TSKENTVLRS GLSPAKVFMI
     PNAVDTAMFK PASVRPSTDI ITIVVISRLV YRKGADLLVE VIPEVCRLYP NVRFVVGGDG
     PKHVRLEEMR EKHSLQDRVE MLGAVPHSRV RSVLVTGHIF LNSSLTEAFC IAILEAASCG
     LLTVSTRVGG VPEVLPDDMV VLAEPDPDDM VRAIEKAISI LPTINPEEMH NRMKKLYSWQ
     DVAKRTEIVY DRALKCSNRS LLERLMRFLS CGAWAGKLFC MVMILDYLLW RLLQLLQPDE
     DIEEAPDICL CHHRGVEVSE GLRKKIK
 
 
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