ID   CS120_WHEAT             Reviewed;         391 AA.
AC   P46525;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Cold-shock protein CS120;
GN   Name=CS120;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Norstar; TISSUE=Shoot;
RX   PubMed=16669048; DOI=10.1104/pp.99.4.1381;
RA   Houde M., Danyluk J., Laliberte J.-F., Rassart E., Dhindsa R.S., Sarhan F.;
RT   "Cloning, characterization and expression of a cDNA encoding a 50-
RT   kiladalton protein specifically induced by cold acclimation in wheat.";
RL   Plant Physiol. 99:1381-1387(1992).
RN   [2]
RP   SEQUENCE REVISION TO 320-328.
RA   Houde M., Danyluk J., Laliberte J.-F., Rassart E., Dhindsa R.S., Sarhan F.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May reduce intracellular freezing damage during winter by
CC       hydrogen-bonding to the lattice of the nascent ice crystals, thus
CC       modifying the structure and/or propagation of ice crystals.
CC   -!- INDUCTION: Specifically induced by cold temperatures.
CC   -!- DOMAIN: Contains 6 A-type repeats and 11 B-type repeats similar to
CC       those found in maize, rice and barley dehydrin and rab proteins.
CC   -!- SIMILARITY: Belongs to the plant dehydrin family. {ECO:0000305}.
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DR   EMBL; M93342; AAA34261.2; -; mRNA.
DR   PIR; S27766; S27766.
DR   AlphaFoldDB; P46525; -.
DR   PRIDE; P46525; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P46525; baseline and differential.
DR   GO; GO:0009631; P:cold acclimation; IBA:GO_Central.
DR   GO; GO:0009737; P:response to abscisic acid; IBA:GO_Central.
DR   GO; GO:0009414; P:response to water deprivation; IBA:GO_Central.
DR   InterPro; IPR000167; Dehydrin.
DR   InterPro; IPR030513; Dehydrin_CS.
DR   PANTHER; PTHR33346; PTHR33346; 5.
DR   Pfam; PF00257; Dehydrin; 1.
DR   PROSITE; PS00823; DEHYDRIN_2; 2.
PE   2: Evidence at transcript level;
KW   Reference proteome; Repeat.
FT   CHAIN           1..391
FT                   /note="Cold-shock protein CS120"
FT                   /id="PRO_0000100063"
FT   REPEAT          9..31
FT                   /note="1-1"
FT   REPEAT          49..62
FT                   /note="2-1"
FT   REPEAT          72..94
FT                   /note="1-2"
FT   REPEAT          95..108
FT                   /note="2-2"
FT   REPEAT          115..128
FT                   /note="2-3"
FT   REPEAT          135..148
FT                   /note="2-4"
FT   REPEAT          156..178
FT                   /note="1-3"
FT   REPEAT          179..192
FT                   /note="2-5"
FT   REPEAT          199..212
FT                   /note="2-6"
FT   REPEAT          220..242
FT                   /note="1-4"
FT   REPEAT          243..256
FT                   /note="2-7"
FT   REPEAT          263..276
FT                   /note="2-8"
FT   REPEAT          284..306
FT                   /note="1-5"
FT   REPEAT          307..320
FT                   /note="2-9"
FT   REPEAT          327..340
FT                   /note="2-10"
FT   REPEAT          350..363
FT                   /note="2-11"
FT   REPEAT          374..391
FT                   /note="1-6"
FT   REGION          9..391
FT                   /note="6 X 23 AA approximate repeats"
FT   REGION          21..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..363
FT                   /note="11 X 14 AA approximate repeats"
FT   COMPBIAS        21..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..237
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  38898 MW;  E53CB63E80B1F43B CRC64;
     MENQAHIAGE KKGIMEKIKE KLPGGHGDHK ETAGTHGHPG TATHGAPATG GAYGQQGHAG
     TTGTGLHGAH AGEKKGVMEN IKDKLPGGHQ DHQQTGGTYG QQGHTGTATH GTPATGGTYG
     QQGHTGTATH GTPATGGTYG EQGHTGVTGT GTHGTGEKKG VMENIKEKLP GGHGDHQQTG
     GTYGQQGHTG TATHGTPAGG GTYEQHGHTG MTGTGTHGTG EKKGVMENIK DKLPGGHGDH
     QQTGGTYGQQ GHTGTATQGT PAGGGTYEQH GHTGMTGAGT HSTGEKKGVM ENIKEKLPGG
     HSDHQQTGGA YGQQGHTGTA THGTPAGGGT YGQHGHAGVI GTETHGTTAT GGTHGQHGHT
     GTTGTGTHGS DGIGEKKSLM DKIKDKLPGQ H