CSP3_ARATH
ID CSP3_ARATH Reviewed; 301 AA.
AC Q94C69;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Cold shock domain-containing protein 3;
DE Short=AtCSP3;
GN Name=CSP3; OrderedLocusNames=At2g17870; ORFNames=T13L16.11;
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 [MRNA], INDUCTION BY COLD, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12529510; DOI=10.1104/pp.014472;
RA Karlson D., Imai R.;
RT "Conservation of the cold shock domain protein family in plants.";
RL Plant Physiol. 131:12-15(2003).
RN [2]
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 [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 FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION BY COLD, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19556243; DOI=10.1074/jbc.m109.025791;
RA Kim M.-H., Sasaki K., Imai R.;
RT "Cold shock domain protein 3 regulates freezing tolerance in Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 284:23454-23460(2009).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=19269998; DOI=10.1093/jxb/ern351;
RA Nakaminami K., Hill K., Perry S.E., Sentoku N., Long J.A., Karlson D.T.;
RT "Arabidopsis cold shock domain proteins: relationships to floral and
RT silique development.";
RL J. Exp. Bot. 60:1047-1062(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP INTERACTION WITH PTAC16; PABN1; PABN2 AND PABN3.
RX PubMed=23334891; DOI=10.1007/s12192-012-0398-3;
RA Kim M.H., Sonoda Y., Sasaki K., Kaminaka H., Imai R.;
RT "Interactome analysis reveals versatile functions of Arabidopsis COLD SHOCK
RT DOMAIN PROTEIN 3 in RNA processing within the nucleus and cytoplasm.";
RL Cell Stress Chaperones 18:517-525(2013).
CC -!- FUNCTION: Chaperone that binds to RNA, single- (ssDNA) and double-
CC stranded (dsDNA) DNA, and unwinds nucleic acid duplex. Promotes
CC freezing tolerance. {ECO:0000269|PubMed:19269998,
CC ECO:0000269|PubMed:19556243}.
CC -!- SUBUNIT: Interacts with PTAC16, PABN1, PABN2 and PABN3.
CC {ECO:0000269|PubMed:23334891}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19556243}. Cytoplasm
CC {ECO:0000269|PubMed:19556243}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in shoot and root apices, and
CC siliques, and, to a lower extent, in roots, cotyledons, stems, shoots,
CC leaves, floral buds and flowers. {ECO:0000269|PubMed:19269998,
CC ECO:0000269|PubMed:19556243}.
CC -!- DEVELOPMENTAL STAGE: In flowers, present in pollen within anthers. High
CC expression in the earliest stage of silique development, with a
CC decrease during the middle stages of silique development and
CC subsequently an increase during the later stages.
CC {ECO:0000269|PubMed:19269998, ECO:0000269|PubMed:19556243}.
CC -!- INDUCTION: Accumulates during cold acclimation, especially in roots.
CC {ECO:0000269|PubMed:12529510, ECO:0000269|PubMed:19556243}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to freezing.
CC {ECO:0000269|PubMed:19556243}.
CC -!- SIMILARITY: Belongs to the cold shock protein (CSP) family.
CC {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; AB308041; BAF63841.1; -; mRNA.
DR EMBL; CP002685; AEC06697.1; -; Genomic_DNA.
DR EMBL; AY035133; AAK59638.1; -; mRNA.
DR EMBL; AY062985; AAL34159.1; -; mRNA.
DR PIR; T00837; T00837.
DR RefSeq; NP_565427.1; NM_127341.4.
DR AlphaFoldDB; Q94C69; -.
DR SMR; Q94C69; -.
DR BioGRID; 1654; 43.
DR IntAct; Q94C69; 5.
DR STRING; 3702.AT2G17870.1; -.
DR iPTMnet; Q94C69; -.
DR PaxDb; Q94C69; -.
DR PRIDE; Q94C69; -.
DR ProteomicsDB; 220371; -.
DR EnsemblPlants; AT2G17870.1; AT2G17870.1; AT2G17870.
DR GeneID; 816297; -.
DR Gramene; AT2G17870.1; AT2G17870.1; AT2G17870.
DR KEGG; ath:AT2G17870; -.
DR Araport; AT2G17870; -.
DR TAIR; locus:2827810; AT2G17870.
DR eggNOG; KOG3070; Eukaryota.
DR HOGENOM; CLU_089169_3_0_1; -.
DR InParanoid; Q94C69; -.
DR OMA; GDSCKCG; -.
DR OrthoDB; 1604809at2759; -.
DR PhylomeDB; Q94C69; -.
DR PRO; PR:Q94C69; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q94C69; baseline and differential.
DR Genevisible; Q94C69; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:CACAO.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00313; CSD; 1.
DR Pfam; PF00098; zf-CCHC; 7.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00343; ZnF_C2HC; 7.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF57756; SSF57756; 3.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
DR PROSITE; PS50158; ZF_CCHC; 7.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..301
FT /note="Cold shock domain-containing protein 3"
FT /id="PRO_0000418160"
FT DOMAIN 13..76
FT /note="CSD"
FT ZN_FING 94..111
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 130..147
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 161..178
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 196..213
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 224..241
FT /note="CCHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 252..269
FT /note="CCHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 282..299
FT /note="CCHC-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 301 AA; 29564 MW; 28F6A32F4C48CFBF CRC64;
MAMEDQSAAR SIGKVSWFSD GKGYGFITPD DGGEELFVHQ SSIVSDGFRS LTLGESVEYE
IALGSDGKTK AIEVTAPGGG SLNKKENSSR GSGGNCFNCG EVGHMAKDCD GGSGGKSFGG
GGGRRSGGEG ECYMCGDVGH FARDCRQSGG GNSGGGGGGG RPCYSCGEVG HLAKDCRGGS
GGNRYGGGGG RGSGGDGCYM CGGVGHFARD CRQNGGGNVG GGGSTCYTCG GVGHIAKVCT
SKIPSGGGGG GRACYECGGT GHLARDCDRR GSGSSGGGGG SNKCFICGKE GHFARECTSV
A
