UGPI2_ARATH
ID UGPI2_ARATH Reviewed; 199 AA.
AC Q84VZ5; Q8H7A4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Uncharacterized GPI-anchored protein At5g19240;
DE Flags: Precursor;
GN OrderedLocusNames=At5g19240; ORFNames=T24G5.140;
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 MRNA].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UPF0277 family. {ECO:0000305}.
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DR EMBL; AF083770; AAN60328.1; -; mRNA.
DR EMBL; AC069326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92674.1; -; Genomic_DNA.
DR EMBL; BT004589; AAO42835.1; -; mRNA.
DR RefSeq; NP_197425.1; NM_121929.3.
DR AlphaFoldDB; Q84VZ5; -.
DR SMR; Q84VZ5; -.
DR BioGRID; 17320; 1.
DR STRING; 3702.AT5G19240.1; -.
DR PaxDb; Q84VZ5; -.
DR PRIDE; Q84VZ5; -.
DR ProteomicsDB; 246392; -.
DR EnsemblPlants; AT5G19240.1; AT5G19240.1; AT5G19240.
DR GeneID; 832044; -.
DR Gramene; AT5G19240.1; AT5G19240.1; AT5G19240.
DR KEGG; ath:AT5G19240; -.
DR Araport; AT5G19240; -.
DR TAIR; locus:2182152; AT5G19240.
DR eggNOG; ENOG502RYCU; Eukaryota.
DR HOGENOM; CLU_087436_1_0_1; -.
DR InParanoid; Q84VZ5; -.
DR OrthoDB; 1298341at2759; -.
DR PRO; PR:Q84VZ5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84VZ5; baseline and differential.
DR Genevisible; Q84VZ5; AT.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR InterPro; IPR045285; At5g19230-like.
DR PANTHER; PTHR33976; PTHR33976; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..169
FT /note="Uncharacterized GPI-anchored protein At5g19240"
FT /id="PRO_0000036269"
FT PROPEP 170..199
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036270"
FT LIPID 169
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 16
FT /note="F -> L (in Ref. 4; AAO42835)"
FT /evidence="ECO:0000305"
FT CONFLICT 17..18
FT /note="LS -> IF (in Ref. 1; AAN60328)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..199
FT /note="HVLSHNSLSLFS -> LFCFFMF (in Ref. 1; AAN60328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 21335 MW; 6D947B9F68DC946E CRC64;
MAISKLHLVL FLLSVFLSLH RPVLSNTDGE NLLFTVFNQY RESVNLTNLK KNKNAECLAD
EVVDQLQNQP CTNTTGSASV PGTDPGIPNF PNLLAKCRLN TNVTRDGLIL QVCAPKHHST
PDLSSFANVL TKNLNDSKFT GAGVGIDSDG IWLVTVLTTN TPGGSYSNSG AFAFGVNGLV
SSSLMFLHVL SHNSLSLFS
