CID12_ARATH
ID CID12_ARATH Reviewed; 336 AA.
AC Q9S7N9; Q38915;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=Polyadenylate-binding protein-interacting protein 12;
DE Short=PABP-interacting protein 12;
DE Short=Poly(A)-binding protein-interacting protein 12;
DE AltName: Full=PAM2-containing protein CID12;
DE AltName: Full=Protein CTC-INTERACTING DOMAIN 12;
DE AltName: Full=RNA-binding protein 37;
DE Short=AtRBP37;
GN Name=CID12; Synonyms=RBP37; OrderedLocusNames=At4g10610;
GN ORFNames=F3H7.12, T4F9.70;
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 [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia; TISSUE=Silique;
RX PubMed=9177318; DOI=10.1023/a:1005834402536;
RA Hecht V., Stiefel V., Delseny M., Gallois P.;
RT "A new Arabidopsis nucleic-acid-binding protein gene is highly expressed in
RT dividing cells during development.";
RL Plant Mol. Biol. 34:119-124(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
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 [6]
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 [7]
RP INTERACTION WITH MPC.
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).
CC -!- FUNCTION: Binds nucleotic acids in vitro. {ECO:0000269|PubMed:9177318}.
CC -!- SUBUNIT: Interacts with MPC. {ECO:0000269|PubMed:18796636}.
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=Q9S7N9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. Detected in flowers only in growing organs: gynoecium,
CC petals, stamenal filaments, anther walls and ovules.
CC {ECO:0000269|PubMed:15650869, ECO:0000269|PubMed:9177318}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early-embryogenesis in the embryo
CC proper and the suspensor up to late heart stage. Expression is not
CC detected in the embryo during maturation. {ECO:0000269|PubMed:9177318}.
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; U44134; AAA86641.1; -; mRNA.
DR EMBL; AF109721; AAD34325.1; -; Genomic_DNA.
DR EMBL; AF118222; AAD03436.1; -; Genomic_DNA.
DR EMBL; AL049523; CAB40027.1; -; Genomic_DNA.
DR EMBL; AL161517; CAB78184.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82907.1; -; Genomic_DNA.
DR EMBL; AY039599; AAK62654.1; -; mRNA.
DR EMBL; AY078011; AAL77712.1; -; mRNA.
DR EMBL; AY086286; AAM64358.1; -; mRNA.
DR PIR; T04196; T04196.
DR RefSeq; NP_192799.1; NM_117129.3. [Q9S7N9-1]
DR AlphaFoldDB; Q9S7N9; -.
DR SMR; Q9S7N9; -.
DR BioGRID; 11952; 2.
DR STRING; 3702.AT4G10610.1; -.
DR iPTMnet; Q9S7N9; -.
DR PaxDb; Q9S7N9; -.
DR PRIDE; Q9S7N9; -.
DR ProteomicsDB; 246939; -. [Q9S7N9-1]
DR EnsemblPlants; AT4G10610.1; AT4G10610.1; AT4G10610. [Q9S7N9-1]
DR GeneID; 826653; -.
DR Gramene; AT4G10610.1; AT4G10610.1; AT4G10610. [Q9S7N9-1]
DR KEGG; ath:AT4G10610; -.
DR Araport; AT4G10610; -.
DR TAIR; locus:2139242; AT4G10610.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_042473_2_0_1; -.
DR InParanoid; Q9S7N9; -.
DR OMA; GYNHGKR; -.
DR PhylomeDB; Q9S7N9; -.
DR PRO; PR:Q9S7N9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S7N9; baseline and differential.
DR Genevisible; Q9S7N9; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Nucleotide-binding; Nucleus; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..336
FT /note="Polyadenylate-binding protein-interacting protein
FT 12"
FT /id="PRO_0000428902"
FT DOMAIN 150..225
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 247..323
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 14..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 75..85
FT /note="PAM2-like"
FT MOTIF 122..134
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 14..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 158
FT /note="D -> Y (in Ref. 1; AAA86641)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="A -> G (in Ref. 1; AAA86641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 36780 MW; 6DA47D27FA3BABF2 CRC64;
MAVIESVGAN TTVEAGGLIS PSPPSSVTSQ ESGASSNNDH GGNGIHDEIG VHVARSDGGE
SFKRDMRELH ELLSKLNPMA KEFIPPSLTK PVVNGFNGGF FAVNNGFVAA GNFPVNEDGS
FRRKKSFGQQ GKRRMNPRTS LAQREEIIRR TVYVSDIDQQ VTEEQLAGLF IGFGQVVDCR
ICGDPNSVLR FAFIEFTDEV GARTALNLSG TMLGFYPVKV MPSKTAIAPV NPTFLPRTED
EREMCARTIY CTNIDKKLTQ TDIKLFFESV CGEVYRLRLL GDYHHPTRIG FVEFVMAESA
IAALNCSGVL LGSLPIRVSP SKTPVRSRAI PRHQMH
