CSP4_ARATH
ID CSP4_ARATH Reviewed; 201 AA.
AC Q38896; Q5BIT2;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Cold shock domain-containing protein 4;
DE Short=AtCSP4;
DE AltName: Full=Glycine-rich protein 2b;
DE Short=AtGRP2b;
GN Name=CSP4; Synonyms=GRP2B; OrderedLocusNames=At2g21060; ORFNames=F26H11.18;
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].
RC STRAIN=cv. Columbia;
RA van Nocker S., Vierstra R.D.;
RT "Arabidopsis AtGRP2b, a glycine-rich protein containing multiple nucleic
RT acid-binding motifs.";
RL (er) Plant Gene Register PGR95-128(1995).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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, 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 [8]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21282328; DOI=10.1093/jxb/erq400;
RA Yang Y., Karlson D.T.;
RT "Overexpression of AtCSP4 affects late stages of embryo development in
RT Arabidopsis.";
RL J. Exp. Bot. 62:2079-2091(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 and unwinds RNA and both single-
CC stranded DNA and double-stranded DNA (ssDNA and dsDNA DNA) (By
CC similarity). Regulates the flowering transition and flower and seed
CC development, particularly at late stages of embryo development, through
CC regulation of gene expression (including MEA, FIS2, AP1, CAL, AG and
CC SHP2). {ECO:0000250, ECO:0000269|PubMed:19269998,
CC ECO:0000269|PubMed:21282328}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21282328}. Nucleus,
CC nucleolus {ECO:0000250}. Nucleus {ECO:0000269|PubMed:21282328}.
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. Present in shoot apical meristems and siliques (at
CC protein level). Very low levels are observed in cv. Landsberg erecta
CC compared to cv. Columbia (PubMed:19269998).
CC {ECO:0000269|PubMed:19269998, ECO:0000269|PubMed:21282328}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in floral buds, flowers, developing
CC embryos during an early stage of silique development.
CC {ECO:0000269|PubMed:19269998}.
CC -!- INDUCTION: Down-regulated during cold acclimation. Accumulation during
CC silique development is AGL15-dependent. {ECO:0000269|PubMed:12529510}.
CC -!- SIMILARITY: Belongs to the cold shock protein (CSP) family.
CC {ECO:0000305}.
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DR EMBL; U39072; AAA91165.1; -; mRNA.
DR EMBL; AC006264; AAD29810.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07117.1; -; Genomic_DNA.
DR EMBL; AY057693; AAL15323.1; -; mRNA.
DR EMBL; BT021142; AAX22277.1; -; mRNA.
DR PIR; F84596; F84596.
DR RefSeq; NP_179702.1; NM_127676.3.
DR AlphaFoldDB; Q38896; -.
DR SMR; Q38896; -.
DR BioGRID; 1994; 8.
DR IntAct; Q38896; 6.
DR STRING; 3702.AT2G21060.1; -.
DR iPTMnet; Q38896; -.
DR PaxDb; Q38896; -.
DR PRIDE; Q38896; -.
DR ProteomicsDB; 224430; -.
DR EnsemblPlants; AT2G21060.1; AT2G21060.1; AT2G21060.
DR GeneID; 816641; -.
DR Gramene; AT2G21060.1; AT2G21060.1; AT2G21060.
DR KEGG; ath:AT2G21060; -.
DR Araport; AT2G21060; -.
DR TAIR; locus:2047092; AT2G21060.
DR eggNOG; KOG3070; Eukaryota.
DR HOGENOM; CLU_089169_3_0_1; -.
DR InParanoid; Q38896; -.
DR OMA; WIGSSWV; -.
DR OrthoDB; 1604809at2759; -.
DR PhylomeDB; Q38896; -.
DR PRO; PR:Q38896; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38896; baseline and differential.
DR Genevisible; Q38896; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
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; 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..201
FT /note="Cold shock domain-containing protein 4"
FT /id="PRO_0000100354"
FT DOMAIN 14..81
FT /note="CSD"
FT ZN_FING 136..153
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 180..197
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 66..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 201 AA; 19077 MW; 832411B7FD890E46 CRC64;
MSGGGDVNMS GGDRRKGTVK WFDTQKGFGF ITPSDGGDDL FVHQSSIRSE GFRSLAAEES
VEFDVEVDNS GRPKAIEVSG PDGAPVQGNS GGGGSSGGRG GFGGGGGRGG GRGGGSYGGG
YGGRGSGGRG GGGGDNSCFK CGEPGHMARE CSQGGGGYSG GGGGGRYGSG GGGGGGGGGL
SCYSCGESGH FARDCTSGGA R
