CSP1_ARATH
ID CSP1_ARATH Reviewed; 299 AA.
AC O65639;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Cold shock protein 1;
DE Short=AtCSP1;
DE AltName: Full=Cold shock domain-containing protein 1;
GN Name=CSP1; Synonyms=CSDP1; OrderedLocusNames=At4g36020; ORFNames=T19K4.150;
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=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 [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 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 [5]
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 [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 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).
RN [8]
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).
CC -!- FUNCTION: Chaperone that binds to RNA, single- (ssDNA) and double-
CC stranded (dsDNA) DNA, and unwinds nucleic acid duplex. Exhibits a DNA
CC melting activity. May be involved in cold resistance. Prevents seed
CC germination under dehydration or salt stress conditions.
CC {ECO:0000269|PubMed:17169986, ECO:0000269|PubMed:19258348,
CC ECO:0000269|PubMed:19269998}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in shoot apices and siliques, and,
CC to a lower extent, in roots, cotyledons, stems, shoots, leaves, floral
CC buds and flowers. {ECO:0000269|PubMed:19269998}.
CC -!- DEVELOPMENTAL STAGE: High expression in the earliest stage of silique
CC development, with a decrease during the middle stages of silique
CC development and subsequently an increase during the later stages.
CC {ECO:0000269|PubMed:19269998}.
CC -!- INDUCTION: Accumulates during cold acclimation, but down-regulated by
CC dehydration and salt stresses. {ECO:0000269|PubMed:12529510,
CC ECO:0000269|PubMed:17169986}.
CC -!- SIMILARITY: Belongs to the cold shock protein (CSP) family.
CC {ECO:0000305}.
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DR EMBL; AL022373; CAA18496.1; -; Genomic_DNA.
DR EMBL; AL161588; CAB81511.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86603.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67851.1; -; Genomic_DNA.
DR EMBL; AK226815; BAE98911.1; -; mRNA.
DR PIR; T05494; T05494.
DR RefSeq; NP_001320149.1; NM_001342395.1.
DR RefSeq; NP_195326.1; NM_119769.4.
DR AlphaFoldDB; O65639; -.
DR SMR; O65639; -.
DR BioGRID; 15040; 6.
DR IntAct; O65639; 4.
DR STRING; 3702.AT4G36020.1; -.
DR iPTMnet; O65639; -.
DR PaxDb; O65639; -.
DR PRIDE; O65639; -.
DR ProteomicsDB; 222624; -.
DR EnsemblPlants; AT4G36020.1; AT4G36020.1; AT4G36020.
DR EnsemblPlants; AT4G36020.3; AT4G36020.3; AT4G36020.
DR GeneID; 829758; -.
DR Gramene; AT4G36020.1; AT4G36020.1; AT4G36020.
DR Gramene; AT4G36020.3; AT4G36020.3; AT4G36020.
DR KEGG; ath:AT4G36020; -.
DR Araport; AT4G36020; -.
DR TAIR; locus:2135139; AT4G36020.
DR eggNOG; KOG3070; Eukaryota.
DR HOGENOM; CLU_089169_3_0_1; -.
DR InParanoid; O65639; -.
DR OMA; RECRRDA; -.
DR OrthoDB; 1604809at2759; -.
DR PhylomeDB; O65639; -.
DR PRO; PR:O65639; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65639; baseline and differential.
DR Genevisible; O65639; AT.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA: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:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IDA: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; 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; 5.
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..299
FT /note="Cold shock protein 1"
FT /id="PRO_0000418158"
FT DOMAIN 12..76
FT /note="CSD"
FT ZN_FING 100..117
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 132..149
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 164..181
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 198..215
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 230..247
FT /note="CCHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 253..270
FT /note="CCHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 280..297
FT /note="CCHC-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 76..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 299 AA; 30088 MW; B40DFCC8493F66F8 CRC64;
MASEDQSAAR STGKVNWFNA SKGYGFITPD DGSVELFVHQ SSIVSEGYRS LTVGDAVEFA
ITQGSDGKTK AVNVTAPGGG SLKKENNSRG NGARRGGGGS GCYNCGELGH ISKDCGIGGG
GGGGERRSRG GEGCYNCGDT GHFARDCTSA GNGDQRGATK GGNDGCYTCG DVGHVARDCT
QKSVGNGDQR GAVKGGNDGC YTCGDVGHFA RDCTQKVAAG NVRSGGGGSG TCYSCGGVGH
IARDCATKRQ PSRGCYQCGG SGHLARDCDQ RGSGGGGNDN ACYKCGKEGH FARECSSVA
