CID11_ARATH
ID CID11_ARATH Reviewed; 358 AA.
AC Q9LPI5; Q94JR0;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Polyadenylate-binding protein-interacting protein 11;
DE Short=PABP-interacting protein 11;
DE Short=Poly(A)-binding protein-interacting protein 11;
DE AltName: Full=PAM2-containing protein CID11;
DE AltName: Full=Protein CTC-INTERACTING DOMAIN 11;
GN Name=CID11; OrderedLocusNames=At1g32790; ORFNames=F6N18.17;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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=Q9LPI5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in cauline leaves, stems, immature
CC siliques and primary inflorescences. {ECO:0000269|PubMed:15650869}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAK53018.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AY089165; Type=Frameshift; Evidence={ECO:0000305};
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; AC017118; AAF25974.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31529.1; -; Genomic_DNA.
DR EMBL; AF375434; AAK53018.1; ALT_FRAME; mRNA.
DR EMBL; BT002225; AAN72236.1; -; mRNA.
DR EMBL; AY089165; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; F86452; F86452.
DR RefSeq; NP_174556.1; NM_103013.3. [Q9LPI5-1]
DR AlphaFoldDB; Q9LPI5; -.
DR SMR; Q9LPI5; -.
DR STRING; 3702.AT1G32790.2; -.
DR iPTMnet; Q9LPI5; -.
DR PaxDb; Q9LPI5; -.
DR PRIDE; Q9LPI5; -.
DR ProteomicsDB; 246904; -. [Q9LPI5-1]
DR EnsemblPlants; AT1G32790.1; AT1G32790.1; AT1G32790. [Q9LPI5-1]
DR GeneID; 840173; -.
DR Gramene; AT1G32790.1; AT1G32790.1; AT1G32790. [Q9LPI5-1]
DR KEGG; ath:AT1G32790; -.
DR Araport; AT1G32790; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_042473_2_0_1; -.
DR OMA; QDQSKHN; -.
DR PhylomeDB; Q9LPI5; -.
DR PRO; PR:Q9LPI5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPI5; baseline and differential.
DR Genevisible; Q9LPI5; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR CDD; cd12459; RRM1_CID8_like; 1.
DR CDD; cd12460; RRM2_CID8_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR034823; CID8-like_RRM1.
DR InterPro; IPR034825; CID8-like_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..358
FT /note="Polyadenylate-binding protein-interacting protein
FT 11"
FT /id="PRO_0000428901"
FT DOMAIN 173..248
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 270..346
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 92..102
FT /note="PAM2-like"
FT MOTIF 146..157
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT CONFLICT 265
FT /note="R -> S (in Ref. 3; AAK53018/AAN72236)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="S -> Y (in Ref. 3; AAK53018/AAN72236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38952 MW; 73EB080D795F436E CRC64;
MAVVETGAAA TAADAGGVVI QPPPSSPPSS MTSQDSGVSS DDQNHHSRID QVLRHDQGLY
SKIGSHVARS DGVDGGESFK RDMRELQELF SKLNPMAEEF VPPSLNKQGG NGVNGGFFTS
AGSFFRNNGF AGTGNGGYGN ENGGFRRKKS FGQGKRRMNA RTSMAQREDV IRRTVYVSDL
DQQVTEEQLA GLFVSCGQVV DCRICGDPNS VLRFAFIEFT DEEGAMTALN LSGTMLGFYP
VKVLPSKTAI APVNPTFLPR TEDEREMCAR TIYCTNIDKK VTQSDVKIFF ESFCGEVYRL
RLLGDYQHST RIAFVEFVMA ESAIAALNCS GVVLGSLPIR VSPSKTPVRP RSPRHPMH