DHN1_MAIZE
ID DHN1_MAIZE Reviewed; 168 AA.
AC P12950; P16318;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Dehydrin DHN1;
DE AltName: Full=M3;
DE AltName: Full=RAB-17 protein;
GN Name=DHN1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2562763; DOI=10.1007/bf00027338;
RA Close T.J., Kortt A.A., Chandler P.M.;
RT "A cDNA-based comparison of dehydration-induced proteins (dehydrins) in
RT barley and corn.";
RL Plant Mol. Biol. 13:95-108(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. AC 1503;
RX PubMed=2151715; DOI=10.1007/bf00028778;
RA Vilardell J., Goday A., Freire M.A., Torrent M., Martinez M.C., Torne J.M.,
RA Pages M.;
RT "Gene sequence, developmental expression, and protein phosphorylation of
RT RAB-17 in maize.";
RL Plant Mol. Biol. 14:423-432(1990).
RN [3]
RP PHOSPHORYLATION BY CKII.
RX PubMed=1939268; DOI=10.1016/s0021-9258(18)54601-9;
RA Plana M., Itarte E., Eritja R., Goday A., Pages M., Martinez M.C.;
RT "Phosphorylation of maize RAB-17 protein by casein kinase 2.";
RL J. Biol. Chem. 266:22510-22514(1991).
CC -!- DEVELOPMENTAL STAGE: ABA treatment induced the synthesis of RAB-17 in
CC calli, however, the RAB-17 proteins were found to be highly
CC phosphorylated only in embryos.
CC -!- INDUCTION: By abscisic acid (ABA) and water stress.
CC -!- PTM: Phosphorylated on serines in the serine-cluster region (poly-Ser).
CC {ECO:0000269|PubMed:1939268}.
CC -!- SIMILARITY: Belongs to the plant dehydrin family. {ECO:0000305}.
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DR EMBL; X15290; CAA33364.1; -; mRNA.
DR EMBL; X15994; CAA34123.1; -; Genomic_DNA.
DR PIR; A39316; A39316.
DR PIR; S05545; S05545.
DR PIR; S08633; S08633.
DR AlphaFoldDB; P12950; -.
DR STRING; 4577.GRMZM2G079440_P01; -.
DR PaxDb; P12950; -.
DR PRIDE; P12950; -.
DR MaizeGDB; 24916; -.
DR eggNOG; ENOG502S4VW; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P12950; baseline and differential.
DR GO; GO:0012506; C:vesicle membrane; IDA:CAFA.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:CAFA.
DR GO; GO:1901611; F:phosphatidylglycerol binding; IDA:CAFA.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:CAFA.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:CAFA.
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 DisProt; DP00530; -.
DR InterPro; IPR000167; Dehydrin.
DR InterPro; IPR030513; Dehydrin_CS.
DR PANTHER; PTHR33346; PTHR33346; 1.
DR Pfam; PF00257; Dehydrin; 1.
DR PROSITE; PS00315; DEHYDRIN_1; 1.
DR PROSITE; PS00823; DEHYDRIN_2; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat;
KW Stress response.
FT CHAIN 1..168
FT /note="Dehydrin DHN1"
FT /id="PRO_0000100051"
FT REPEAT 2..10
FT /note="1-1"
FT REPEAT 94..107
FT /note="2-1"
FT REPEAT 122..130
FT /note="1-2"
FT REPEAT 132..140
FT /note="1-3"
FT REPEAT 153..166
FT /note="2-2"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..140
FT /note="3 X approximate repeats"
FT REGION 94..166
FT /note="2 X approximate repeats"
FT COMPBIAS 87..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 9
FT /note="R -> H (in Ref. 2; CAA33364)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="R -> A (in Ref. 2; CAA33364)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="Missing (in Ref. 2; CAA33364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 17161 MW; BE7758CAD37CFF39 CRC64;
MEYGQQGQRG HGRTGHVDQY GNPVGGVEHG TGGMRHGTGT TGGMGQLGEH GGAGMGGGQF
QPAREEHKTG GILHRSGSSS SSSSEDDGMG GRRKKGIKEK IKEKLPGGHK DDQHATATTG
GAYGQQGHTG SAYGQQGHTG GAYATGTEGT GEKKGIMDKI KEKLPGQH
