SRC1_SOYBN
ID SRC1_SOYBN Reviewed; 102 AA.
AC O04132; K7MMH0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein SRC1 {ECO:0000305};
DE AltName: Full=Protein SOYBEAN GENE REGULATED BY COLD 1 {ECO:0000303|Ref.1};
GN Name=SRC1 {ECO:0000303|Ref.1};
GN OrderedLocusNames=Glyma17g24193 {ECO:0000305};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Kitamusume; TISSUE=Leaf;
RX DOI=10.1016/S0168-9452(96)04568-2;
RA Takahashi R., Shimosaka E.;
RT "cDNA sequence analysis and expression of two cold-regulated genes in
RT soybean.";
RL Plant Sci. 123:93-104(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [3]
RP INDUCTION BY COLD STRESS.
RX PubMed=15020631; DOI=10.1093/jxb/erh125;
RA Kim K.Y., Park S.W., Chung Y.S., Chung C.H., Kim J.I., Lee J.H.;
RT "Molecular cloning of low-temperature-inducible ribosomal proteins from
RT soybean.";
RL J. Exp. Bot. 55:1153-1155(2004).
CC -!- FUNCTION: Intrinsically disordered and metal-binding protein that may
CC play a role in stress responses. {ECO:0000250|UniProtKB:Q9SLJ2}.
CC -!- INDUCTION: By cold stress (Ref.1, PubMed:15020631). Induced by heat
CC shock, drought, wounding and infection by soybean mosaic virus (SMV)
CC (Ref.1). {ECO:0000269|PubMed:15020631, ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the KS-type dehydrin family. {ECO:0000305}.
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DR EMBL; AB000129; BAA19768.1; -; mRNA.
DR EMBL; CM000850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T07078; T07078.
DR RefSeq; NP_001236644.1; NM_001249715.1.
DR RefSeq; XP_006600235.1; XM_006600172.2.
DR AlphaFoldDB; O04132; -.
DR STRING; 3847.GLYMA17G24193.1; -.
DR PRIDE; O04132; -.
DR EnsemblPlants; KRH04799; KRH04799; GLYMA_17G187600.
DR GeneID; 547450; -.
DR Gramene; KRH04799; KRH04799; GLYMA_17G187600.
DR KEGG; gmx:547450; -.
DR eggNOG; ENOG502S99J; Eukaryota.
DR OMA; HADEHKS; -.
DR Proteomes; UP000008827; Chromosome 17.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR039285; HIRD11-like.
DR PANTHER; PTHR34941; PTHR34941; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Repeat; Stress response.
FT CHAIN 1..102
FT /note="Protein SRC1"
FT /id="PRO_0000433972"
FT REPEAT 21..24
FT /note="1"
FT /evidence="ECO:0000305|Ref.1"
FT REPEAT 25..28
FT /note="2"
FT /evidence="ECO:0000305|Ref.1"
FT REPEAT 29..32
FT /note="3"
FT /evidence="ECO:0000305|Ref.1"
FT REPEAT 33..36
FT /note="4"
FT /evidence="ECO:0000305|Ref.1"
FT REPEAT 37..40
FT /note="5"
FT /evidence="ECO:0000305|Ref.1"
FT REPEAT 41..44
FT /note="6"
FT /evidence="ECO:0000305|Ref.1"
FT REPEAT 45..48
FT /note="7"
FT /evidence="ECO:0000305|Ref.1"
FT REPEAT 49..53
FT /note="8"
FT /evidence="ECO:0000305|Ref.1"
FT REPEAT 54..58
FT /note="9"
FT /evidence="ECO:0000305|Ref.1"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..58
FT /note="9 X approximate tandem repeats"
FT /evidence="ECO:0000305|Ref.1"
FT COMPBIAS 10..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 102 AA; 11556 MW; 3AC68756058B8E2D CRC64;
MSGIIHKIEE TLHVGGHKKE EHKGEHHGEH KGEHKGEHHG EHKGEHKGEQ HHGEHKEGLV
DKIKDKIHGD GHDKGEKKKK KDKKKKEHGH DHHGHSSSSD SD