PIGM_ARATH
ID PIGM_ARATH Reviewed; 450 AA.
AC Q500W7; Q7XZS2; Q9C575;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=GPI mannosyltransferase 1;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase I;
DE Short=GPI-MT-I;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class M protein;
DE Short=PIG-M;
DE AltName: Full=Protein PEANUT 1;
GN Name=PIGM; Synonyms=PNT1; OrderedLocusNames=At5g22130; ORFNames=T6G21.34;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-450, FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15772281; DOI=10.1105/tpc.105.031815;
RA Gillmor C.S., Lukowitz W., Brininstool G., Sedbrook J.C., Hamann T.,
RA Poindexter P., Somerville C.;
RT "Glycosylphosphatidylinositol-anchored proteins are required for cell wall
RT synthesis and morphogenesis in Arabidopsis.";
RL Plant Cell 17:1128-1140(2005).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-
CC acyl-PI during GPI precursor assembly. {ECO:0000269|PubMed:15772281}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q500W7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in influorescence meristem. Present at
CC low level in roots, hypocotyls, leaves and stems.
CC {ECO:0000269|PubMed:15772281}.
CC -!- DISRUPTION PHENOTYPE: Plants display cell walls with decreased
CC crystalline cellulose, increased pectins and irregular and ectopic
CC deposition of pectins, xyloglucans and callose.
CC {ECO:0000269|PubMed:15772281}.
CC -!- SIMILARITY: Belongs to the PIGM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP59446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC34506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL589883; CAC34506.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92986.1; -; Genomic_DNA.
DR EMBL; BT022100; AAY34161.1; -; mRNA.
DR EMBL; AY302133; AAP59446.1; ALT_INIT; mRNA.
DR RefSeq; NP_001332623.1; NM_001343720.1.
DR RefSeq; NP_680199.1; NM_147894.4. [Q500W7-1]
DR AlphaFoldDB; Q500W7; -.
DR SMR; Q500W7; -.
DR BioGRID; 17549; 3.
DR STRING; 3702.AT5G22130.2; -.
DR CAZy; GT50; Glycosyltransferase Family 50.
DR PaxDb; Q500W7; -.
DR PRIDE; Q500W7; -.
DR EnsemblPlants; AT5G22130.1; AT5G22130.1; AT5G22130. [Q500W7-1]
DR GeneID; 832274; -.
DR Gramene; AT5G22130.1; AT5G22130.1; AT5G22130. [Q500W7-1]
DR KEGG; ath:AT5G22130; -.
DR Araport; AT5G22130; -.
DR eggNOG; KOG3893; Eukaryota.
DR InParanoid; Q500W7; -.
DR PhylomeDB; Q500W7; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q500W7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q500W7; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR InterPro; IPR007704; PIG-M.
DR PANTHER; PTHR12886; PTHR12886; 1.
DR Pfam; PF05007; Mannosyl_trans; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycosyltransferase;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..450
FT /note="GPI mannosyltransferase 1"
FT /id="PRO_0000246222"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..93
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..148
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..243
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..345
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..401
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 450 AA; 52946 MW; 4CD10F65C9CA8056 CRC64;
MSRESENTDD EPSKWMKFRS LLVFSMLLRV FLIVYGEWQD AHMEVRYTDV DYIVFSDAAS
LMASGESPYK RTTYRYSPLL ALLLTPNSFF HRSWGKFLFS ASDLLVGWFI HKILKQRKVP
EKICTYSVMV WLFNPFTFTI GTRGNCEPIV CAMILWIILC LMQGNLLQAA FWYGLVVHFR
VYPIIYALPI ILVLDTQVFR SGQKPALLYW NTGQAKTPAS NMERKTFLFN LLTTLKSLFS
RERIMFALIS GGVFLACNAV SFYFYGQEFL HEALLYHLTR TDPRHNFSIY FYHIYLHYER
QFSAVEKLIS FLPQFTVQFA LVFCFSQDLV FCIFLQTVAF VTFNKVITAQ YFVWFYCLLP
LILPWSHMKL KWEGLLCIIM WIGAQTHWLL WGYMLEFKGV NVFLPLWIAS LLFLAANTFV
LVRIIQRHRF SPLFRRYESS SSSNNVTKED
