ID   CID7_ARATH              Reviewed;         567 AA.
AC   O64843; Q0WQS0;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Polyadenylate-binding protein-interacting protein 7;
DE            Short=PABP-interacting protein 7;
DE            Short=Poly(A)-binding protein-interacting protein 7;
DE   AltName: Full=PAM2-containing protein CID7;
DE   AltName: Full=Protein CTC-INTERACTING DOMAIN 7;
GN   Name=CID7; OrderedLocusNames=At2g26280; ORFNames=T1D16.8;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, PAM2 MOTIF, AND INTERACTION WITH PAB2.
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   [6]
RP   INTERACTION WITH MPC, AND TISSUE SPECIFICITY.
RX   PubMed=18796636; DOI=10.1105/tpc.108.061929;
RA   Tiwari S., Schulz R., Ikeda Y., Dytham L., Bravo J., Mathers L.,
RA   Spielman M., Guzman P., Oakey R.J., Kinoshita T., Scott R.J.;
RT   "MATERNALLY EXPRESSED PAB C-TERMINAL, a novel imprinted gene in
RT   Arabidopsis, encodes the conserved C-terminal domain of polyadenylate
RT   binding proteins.";
RL   Plant Cell 20:2387-2398(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- SUBUNIT: Interacts with MPC and PAB2. {ECO:0000269|PubMed:15650869,
CC       ECO:0000269|PubMed:18796636}.
CC   -!- TISSUE SPECIFICITY: Expressed in cauline leaves, stems, rosette leaves,
CC       immature siliques and primary inflorescences.
CC       {ECO:0000269|PubMed:18796636}.
CC   -!- DOMAIN: Contains a PAM2-like motif, which seems to be involved in the
CC       binding to the PABC/CTC domain of PAB proteins.
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DR   EMBL; AC004484; AAC14523.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07818.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62763.1; -; Genomic_DNA.
DR   EMBL; AK228618; BAF00529.1; -; mRNA.
DR   EMBL; BT030338; ABO38751.1; -; mRNA.
DR   PIR; E84658; E84658.
DR   RefSeq; NP_001324896.1; NM_001336050.1.
DR   RefSeq; NP_180196.1; NM_128185.3.
DR   AlphaFoldDB; O64843; -.
DR   SMR; O64843; -.
DR   BioGRID; 2520; 5.
DR   IntAct; O64843; 2.
DR   STRING; 3702.AT2G26280.1; -.
DR   iPTMnet; O64843; -.
DR   PaxDb; O64843; -.
DR   PRIDE; O64843; -.
DR   ProteomicsDB; 246941; -.
DR   EnsemblPlants; AT2G26280.1; AT2G26280.1; AT2G26280.
DR   EnsemblPlants; AT2G26280.3; AT2G26280.3; AT2G26280.
DR   GeneID; 817168; -.
DR   Gramene; AT2G26280.1; AT2G26280.1; AT2G26280.
DR   Gramene; AT2G26280.3; AT2G26280.3; AT2G26280.
DR   KEGG; ath:AT2G26280; -.
DR   Araport; AT2G26280; -.
DR   TAIR; locus:2057775; AT2G26280.
DR   eggNOG; KOG2401; Eukaryota.
DR   HOGENOM; CLU_040596_0_0_1; -.
DR   InParanoid; O64843; -.
DR   OMA; ANIREGP; -.
DR   OrthoDB; 521445at2759; -.
DR   PhylomeDB; O64843; -.
DR   PRO; PR:O64843; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O64843; baseline and differential.
DR   Genevisible; O64843; AT.
DR   GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR   CDD; cd14371; CUE_CID7_like; 1.
DR   Gene3D; 3.30.1370.110; -; 1.
DR   InterPro; IPR041806; CID5/6/7_CUE.
DR   InterPro; IPR013899; DUF1771.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   Pfam; PF08590; DUF1771; 1.
DR   Pfam; PF01713; Smr; 1.
DR   SMART; SM01162; DUF1771; 1.
DR   SMART; SM00463; SMR; 1.
DR   SUPFAM; SSF160443; SSF160443; 1.
DR   PROSITE; PS50828; SMR; 1.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..567
FT                   /note="Polyadenylate-binding protein-interacting protein 7"
FT                   /id="PRO_0000422641"
FT   DOMAIN          215..259
FT                   /note="CUE"
FT   DOMAIN          485..567
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00321"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           21..31
FT                   /note="PAM2-like"
FT   COMPBIAS        358..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        500
FT                   /note="K -> E (in Ref. 3; BAF00529)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   567 AA;  62147 MW;  85F888BE2D90F03E CRC64;
     MSLTKKASEP KLSGTSIKPT TLNPHAAEFV PFTLRSPSSG GTSTLDTRLL ASSSSVGKAV
     LDRTESSASH HSDEEARQFW SHQLPDDITP DFGLMTQDDN SYGSGSLSLA NLSLFDGNEA
     EKFPSASGGY GFSDQTGLAS HNANGNSLAD KSRYPISSFG EDPQRQSFMQ LSPKPWDKQI
     MNAEQLLGND RERNPFSGKS RHGFVNDMIT ESPGDMEVNP VDFLASQFPG FAAESLAEVY
     FANGCDLQLT IEMLTQLELQ VDGGLNQNIS PKTYAPPSLT PMDFPALSIS NSHGIPAQFG
     GDDLQQTGNH YQSPEKDNMF FFKSGPSVSQ PGAIDYVSAV RKLASQDSGM WKYERNDSAD
     SSIGSSRNSG AYKSGRGRSI YSDKLQSRAQ TRPAPVWVET GDAVGNMYSE LREEARDYAR
     LRNVYFEQAR QAYLVGNKAL AKELSVKGQL HNMQMKAAHG KAQEAIYRQR NPVGQGNSRG
     NERMIDLHGL HVSEALQVLK HELSVLRSTA RATQERLQIY ICVGTGHHTR GSRTPARLPV
     AVQRYLLEEE GLDYSEPQAG LLRVIIY