CSP2_ARATH
ID CSP2_ARATH Reviewed; 203 AA.
AC Q41188; C0Z2E8;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 176.
DE RecName: Full=Cold shock protein 2;
DE Short=AtCSP2;
DE AltName: Full=Cold shock domain-containing protein 2;
DE AltName: Full=Glycine-rich protein 2;
DE Short=AtGRP2;
GN Name=CSP2; Synonyms=CSDP2, GRP2; OrderedLocusNames=At4g38680;
GN ORFNames=F20M13.240;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION
RP BY ABSCISIC ACID AND DROUGHT.
RC STRAIN=cv. C24;
RX PubMed=2152168; DOI=10.1105/tpc.2.5.427;
RA de Oliveira D.E., Seurinck J., Inze D., Van Montagu M., Botterman J.;
RT "Differential expression of five Arabidopsis genes encoding glycine-rich
RT proteins.";
RL Plant Cell 2:427-436(1990).
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP INDUCTION BY COLD, AND GENE FAMILY.
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 [7]
RP FUNCTION, INDUCTION BY COLD, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=17963727; DOI=10.1016/j.bbrc.2007.10.059;
RA Sasaki K., Kim M.-H., Imai R.;
RT "Arabidopsis COLD SHOCK DOMAIN PROTEIN2 is a RNA chaperone that is
RT regulated by cold and developmental signals.";
RL Biochem. Biophys. Res. Commun. 364:633-638(2007).
RN [8]
RP FUNCTION, AND INDUCTION BY COLD.
RC STRAIN=cv. Columbia;
RX PubMed=17169986; DOI=10.1093/nar/gkl1076;
RA Kim J.S., Park S.J., Kwak K.J., Kim Y.O., Kim J.Y., Song J., Jang B.,
RA Jung C.-H., Kang H.;
RT "Cold shock domain proteins and glycine-rich RNA-binding proteins from
RT Arabidopsis thaliana can promote the cold adaptation process in Escherichia
RT coli.";
RL Nucleic Acids Res. 35:506-516(2007).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, AND INDUCTION BY COLD.
RC STRAIN=cv. C24;
RX PubMed=17123099; DOI=10.1007/s00425-006-0444-4;
RA Fusaro A.F., Bocca S.N., Ramos R.L., Barroco R.M., Magioli C., Jorge V.C.,
RA Coutinho T.C., Rangel-Lima C.M., De Rycke R., Inze D., Engler G.,
RA Sachetto-Martins G.;
RT "AtGRP2, a cold-induced nucleo-cytoplasmic RNA-binding protein, has a role
RT in flower and seed development.";
RL Planta 225:1339-1351(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17376161; DOI=10.1111/j.1365-313x.2007.03057.x;
RA Kim J.Y., Park S.J., Jang B., Jung C.-H., Ahn S.J., Goh C.-H., Cho K.,
RA Han O., Kang H.;
RT "Functional characterization of a glycine-rich RNA-binding protein 2 in
RT Arabidopsis thaliana under abiotic stress conditions.";
RL Plant J. 50:439-451(2007).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=19258348; DOI=10.1093/pcp/pcp037;
RA Park S.J., Kwak K.J., Oh T.R., Kim Y.O., Kang H.;
RT "Cold shock domain proteins affect seed germination and growth of
RT Arabidopsis thaliana under abiotic stress conditions.";
RL Plant Cell Physiol. 50:869-878(2009).
CC -!- FUNCTION: Chaperone that binds to RNA, single- (ssDNA) and double-
CC stranded (dsDNA) DNA, and unwinds nucleic acid duplex. Accelerates seed
CC germination and seedling growth under cold stress, and contributes to
CC enhancement of cold and freezing tolerance. Regulates flowering
CC transition, and flower and seed development. Promotes seed germination
CC under salt stress. May regulate respiratory oxygen uptake.
CC {ECO:0000269|PubMed:17123099, ECO:0000269|PubMed:17169986,
CC ECO:0000269|PubMed:17376161, ECO:0000269|PubMed:17963727,
CC ECO:0000269|PubMed:19258348, ECO:0000269|PubMed:19269998}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17123099,
CC ECO:0000269|PubMed:17963727}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:17123099, ECO:0000269|PubMed:17963727}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q41188-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q41188-2; Sequence=VSP_044000;
CC -!- TISSUE SPECIFICITY: Mostly expressed in shoot apices, seeds and
CC siliques, and, to a lower extent, in roots, cotyledons, stems, shoots,
CC leaves, floral buds and flowers. Present in shoot apical meristems and
CC siliques (at protein level). {ECO:0000269|PubMed:17123099,
CC ECO:0000269|PubMed:17963727, ECO:0000269|PubMed:19269998,
CC ECO:0000269|PubMed:2152168}.
CC -!- DEVELOPMENTAL STAGE: Active in meristematic tissues. During vegetative
CC growth, expressed in root and shoot apical regions, leaves and roots
CC primordia, root vascular cylinder and procambium. In reproductive
CC organs, present in developing floral meristem, meristematic tissues of
CC young flower buds, and placentae, pollen, ovules and seeds, mostly in
CC embryos. High expression in the earliest stage of silique development,
CC with a decrease during the middle stages of silique development and
CC subsequently an increase during the later stages. In mature seeds,
CC mostly localized in hypocotyl and radicule. During seed germination,
CC first observed in the tip of the radicule and, upon opening of the
CC cotyledons, expressed in the radicule and hypocotyl/radicule transition
CC zone. {ECO:0000269|PubMed:17123099, ECO:0000269|PubMed:17963727,
CC ECO:0000269|PubMed:19269998}.
CC -!- INDUCTION: Induced by abscisic acid (ABA), transiently by ethylene,
CC salicylic acid and water fload, but down-regulated by dehydration
CC stress. Accumulates during cold acclimation. Accumulation during
CC silique development is AGL15-dependent. {ECO:0000269|PubMed:12529510,
CC ECO:0000269|PubMed:17123099, ECO:0000269|PubMed:17169986,
CC ECO:0000269|PubMed:17963727, ECO:0000269|PubMed:2152168}.
CC -!- DISRUPTION PHENOTYPE: Early flowering, altered stamen number and
CC impaired seed development. {ECO:0000269|PubMed:17123099,
CC ECO:0000269|PubMed:17376161}.
CC -!- SIMILARITY: Belongs to the cold shock protein (CSP) family.
CC {ECO:0000305}.
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DR EMBL; S47408; AAB24074.1; -; mRNA.
DR EMBL; AL035540; CAB37524.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80532.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86964.1; -; Genomic_DNA.
DR EMBL; AF360202; AAK25912.1; -; mRNA.
DR EMBL; AF385696; AAK60289.1; -; mRNA.
DR EMBL; AY040049; AAK64107.1; -; mRNA.
DR EMBL; AY133591; AAM91421.1; -; mRNA.
DR EMBL; AK318762; BAH56877.1; -; mRNA.
DR PIR; JQ1061; JQ1061.
DR RefSeq; NP_195580.1; NM_120029.3. [Q41188-1]
DR AlphaFoldDB; Q41188; -.
DR SMR; Q41188; -.
DR BioGRID; 15304; 4.
DR IntAct; Q41188; 4.
DR STRING; 3702.AT4G38680.1; -.
DR iPTMnet; Q41188; -.
DR PaxDb; Q41188; -.
DR PRIDE; Q41188; -.
DR ProteomicsDB; 224429; -. [Q41188-1]
DR EnsemblPlants; AT4G38680.1; AT4G38680.1; AT4G38680. [Q41188-1]
DR GeneID; 830024; -.
DR Gramene; AT4G38680.1; AT4G38680.1; AT4G38680. [Q41188-1]
DR KEGG; ath:AT4G38680; -.
DR Araport; AT4G38680; -.
DR TAIR; locus:2121219; AT4G38680.
DR eggNOG; KOG3070; Eukaryota.
DR HOGENOM; CLU_089169_3_0_1; -.
DR InParanoid; Q41188; -.
DR OMA; WMSGRGF; -.
DR PhylomeDB; Q41188; -.
DR PRO; PR:Q41188; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q41188; baseline and differential.
DR Genevisible; Q41188; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0031982; C:vesicle; IDA:TAIR.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; ISS:TAIR.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009631; P:cold acclimation; IGI:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:TAIR.
DR GO; GO:0043457; P:regulation of cellular respiration; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009269; P:response to desiccation; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0048443; P:stamen development; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
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; 2.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; RNA-binding; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q38896"
FT CHAIN 2..203
FT /note="Cold shock protein 2"
FT /id="PRO_0000418159"
FT DOMAIN 12..76
FT /note="CSD"
FT ZN_FING 129..146
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 183..200
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 65..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q38896"
FT VAR_SEQ 177..203
FT /note="GGGGGGGSCYSCGESGHFARDCTSGGR -> LLSLYYPLFAYYDGSLSLLVG
FT FFLMVSD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_044000"
SQ SEQUENCE 203 AA; 19153 MW; 9310C89C1BC44F55 CRC64;
MSGDNGGGER RKGSVKWFDT QKGFGFITPD DGGDDLFVHQ SSIRSEGFRS LAAEEAVEFE
VEIDNNNRPK AIDVSGPDGA PVQGNSGGGS SGGRGGFGGG RGGGRGSGGG YGGGGGGYGG
RGGGGRGGSD CYKCGEPGHM ARDCSEGGGG YGGGGGGYGG GGGYGGGGGG YGGGGRGGGG
GGGSCYSCGE SGHFARDCTS GGR
