CID5_ARATH
ID CID5_ARATH Reviewed; 155 AA.
AC Q9LYE5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Polyadenylate-binding protein-interacting protein 5;
DE Short=PABP-interacting protein 5;
DE Short=Poly(A)-binding protein-interacting protein 5;
DE AltName: Full=PAM2-containing protein CID5;
DE AltName: Full=Protein CTC-INTERACTING DOMAIN 5;
DE AltName: Full=Protein INCREASED POLYPLOIDY LEVEL IN DARKNESS 1;
GN Name=CID5; Synonyms=IPD1; OrderedLocusNames=At5g11440; ORFNames=F15N18_30;
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].
RC STRAIN=cv. Columbia;
RA Xiao Y.-L., Underwood B.A., Moskal W.A. Jr., Wang W., Redman J.C., Wu H.C.,
RA Utterback T., Town C.D.;
RT "Reconstruction of cDNA sequences for hypothetical genes in Arabidopsis
RT thaliana from 5' and 3' RACE products.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, PAM2 MOTIF, AND TISSUE SPECIFICITY.
RX PubMed=15650869; DOI=10.1007/s00438-004-1090-9;
RA Bravo J., Aguilar-Henonin L., Olmedo G., Guzman P.;
RT "Four distinct classes of proteins as interaction partners of the PABC
RT domain of Arabidopsis thaliana Poly(A)-binding proteins.";
RL Mol. Genet. Genomics 272:651-665(2005).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16897495; DOI=10.1007/s11103-006-0053-4;
RA Tsumoto Y., Yoshizumi T., Kuroda H., Kawashima M., Ichikawa T.,
RA Nakazawa M., Yamamoto N., Matsui M.;
RT "Light-dependent polyploidy control by a CUE protein variant in
RT Arabidopsis.";
RL Plant Mol. Biol. 61:817-828(2006).
CC -!- FUNCTION: Promotes polyploidy in dark-grown seedlings. Regulates the
CC endocycle leading to hypocotyl elongation.
CC {ECO:0000269|PubMed:16897495}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in immature siliques.
CC {ECO:0000269|PubMed:15650869}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in mitotically dividing
CC cells of seedlings. {ECO:0000269|PubMed:16897495}.
CC -!- DOMAIN: Contains a PAM2-like motif, which seems to be involved in the
CC binding to the PABC/CTC domain of PAB proteins.
CC -!- MISCELLANEOUS: Overexpression of CID5/IPD1 leads to increased ploidy
CC levels and longer hypocotyls in dark-grown seedlings compared to wild-
CC type.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL163815; CAB87704.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91680.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69811.1; -; Genomic_DNA.
DR EMBL; AY735675; AAU44545.1; -; mRNA.
DR EMBL; AY773894; AAV63923.1; -; mRNA.
DR PIR; T48503; T48503.
DR RefSeq; NP_001331464.1; NM_001343191.1.
DR RefSeq; NP_196705.1; NM_121182.3.
DR AlphaFoldDB; Q9LYE5; -.
DR SMR; Q9LYE5; -.
DR BioGRID; 16293; 2.
DR IntAct; Q9LYE5; 2.
DR STRING; 3702.AT5G11440.1; -.
DR PaxDb; Q9LYE5; -.
DR PRIDE; Q9LYE5; -.
DR ProteomicsDB; 246907; -.
DR EnsemblPlants; AT5G11440.1; AT5G11440.1; AT5G11440.
DR EnsemblPlants; AT5G11440.2; AT5G11440.2; AT5G11440.
DR GeneID; 831015; -.
DR Gramene; AT5G11440.1; AT5G11440.1; AT5G11440.
DR Gramene; AT5G11440.2; AT5G11440.2; AT5G11440.
DR KEGG; ath:AT5G11440; -.
DR Araport; AT5G11440; -.
DR TAIR; locus:2144221; AT5G11440.
DR eggNOG; ENOG502S2Y2; Eukaryota.
DR HOGENOM; CLU_123587_0_0_1; -.
DR InParanoid; Q9LYE5; -.
DR OMA; KFDCDES; -.
DR OrthoDB; 1458065at2759; -.
DR PhylomeDB; Q9LYE5; -.
DR PRO; PR:Q9LYE5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYE5; baseline and differential.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR CDD; cd14371; CUE_CID7_like; 1.
DR InterPro; IPR041806; CID5/6/7_CUE.
DR InterPro; IPR038981; CID5/CID6.
DR InterPro; IPR003892; CUE.
DR PANTHER; PTHR37252; PTHR37252; 1.
DR PROSITE; PS51140; CUE; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..155
FT /note="Polyadenylate-binding protein-interacting protein 5"
FT /id="PRO_0000428896"
FT DOMAIN 66..109
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 114..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..17
FT /note="PAM2-like"
FT COMPBIAS 127..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 155 AA; 16560 MW; 05A9F8A4004B01A5 CRC64;
MKPGAFALNP HAASYVPISK RVDYGGGDDG LVFAAKSPTV EVSMPKKSSE MAYKQIRDDD
LDLEMDIDMD IEYLLVTFSG LSQESITDVY LANGGDLEAT IEMLNQLEIY STESEENLPE
TLDIGDISES GPSTSKSTEV AASTSSVIPN APVSA