SHW1_ARATH
ID SHW1_ARATH Reviewed; 192 AA.
AC F4I3V6; Q0WTQ6; Q8LGA9;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein SHORT HYPOCOTYL IN WHITE LIGHT 1 {ECO:0000303|PubMed:18375596};
GN Name=SHW1 {ECO:0000303|PubMed:18375596};
GN OrderedLocusNames=At1g69935 {ECO:0000312|Araport:AT1G69935};
GN ORFNames=T17F3 {ECO:0000305};
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] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION BY WHITE LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=18375596; DOI=10.1104/pp.108.118174;
RA Bhatia S., Gangappa S.N., Kushwaha R., Kundu S., Chattopadhyay S.;
RT "SHORT HYPOCOTYL IN WHITE LIGHT1, a serine-arginine-aspartate-rich protein
RT in Arabidopsis, acts as a negative regulator of photomorphogenic growth.";
RL Plant Physiol. 147:169-178(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=19704523; DOI=10.4161/psb.3.10.6038;
RA Bhatia S., Gangappa S.N., Chattopadhyay S.;
RT "SHW1, a common regulator of abscisic acid (ABA) and light signaling
RT pathways.";
RL Plant Signal. Behav. 3:862-864(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH HY5 AND COP1, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26474641; DOI=10.1104/pp.15.01184;
RA Srivastava A.K., Senapati D., Srivastava A., Chakraborty M., Gangappa S.N.,
RA Chattopadhyay S.;
RT "SHORT HYPOCOTYL IN WHITE LIGHT1 interacts with ELONGATED HYPOCOTYL5 (HY5)
RT and CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1) and promotes COP1-mediated
RT degradation of HY5 during Arabidopsis seedling development.";
RL Plant Physiol. 169:2922-2934(2015).
CC -!- FUNCTION: Negative regulator of photomorphogenesis modulating both
CC light and abscisic acid (ABA) signaling pathways (PubMed:19704523,
CC PubMed:18375596, PubMed:26474641). Regulates negatively the light-
CC mediated inhibition of hypocotyl elongation, probably in a PHYB-
CC mediated signaling pathway, but promotes flowering time (especially in
CC long days) and lateral root formation (PubMed:18375596,
CC PubMed:19704523). Enhances light-regulated gene expression
CC (PubMed:18375596). Promotes COP1-mediated degradation of HY5 during
CC seedling development (e.g. hypocotyl growth) through enhanced
CC ubiquitination in the darkness. Also involved in root gravitropism
CC (PubMed:26474641, PubMed:18375596). {ECO:0000269|PubMed:18375596,
CC ECO:0000269|PubMed:19704523, ECO:0000269|PubMed:26474641}.
CC -!- SUBUNIT: Interacts with HY5 and COP1 in the nucleus.
CC {ECO:0000269|PubMed:26474641}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00768, ECO:0000269|PubMed:18375596,
CC ECO:0000269|PubMed:26474641}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Constitutively localized in the nucleus of
CC hypocotyl cells. {ECO:0000269|PubMed:18375596}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000312|Araport:AT1G69935};
CC Name=1;
CC IsoId=F4I3V6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4I3V6-2; Sequence=VSP_058839, VSP_058840;
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings (e.g. hypocotyl and
CC cotyledons) and in green tissues (e.g. leaves, stems, sepals, and young
CC siliques). {ECO:0000269|PubMed:18375596}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, expressed in hypocotyl and
CC cotyledons up to the fifth day after germination. Levels decrease
CC gradually in hypocotyl to become undetectable in 8 days old seedlings.
CC In cotyledons, repartition becomes later patchy. In adult plants,
CC observed in green tissues, with a gradual decrease during aging leading
CC to patchy distribution. Also detected in seeds still partly green but
CC disappear in dry seeds. {ECO:0000269|PubMed:18375596}.
CC -!- INDUCTION: Induced by white light (WL). Barely detectable in dark and
CC in various wavelengths of light such as red light (RL), far red light
CC (FR), and blue light (BL).
CC -!- DISRUPTION PHENOTYPE: Short hypocotyl in dark with drastic reduction in
CC apical hook curvature. Enhanced inhibition in hypocotyl elongation in
CC white light (WL), especially at lower fluence rates (PubMed:18375596,
CC PubMed:26474641). Delayed flowering under long-day conditions
CC (PubMed:18375596). Reduced lateral roots formation (PubMed:18375596,
CC PubMed:26474641). Reduced chlorophyll accumulation and expression of
CC light-regulated genes. Increase in the anthocyanin level in the dark
CC (PubMed:18375596). Reduced sensitivity to abscisic acid (ABA) leading
CC to impaired ABA-mediated reduction of seed germination
CC (PubMed:19704523, PubMed:26474641). The double mutant shw1 phyB
CC exhibits a strongly reduced hypocotyl length in WL (PubMed:19704523).
CC The double mutant shw1 cop1 displays an enhanced photomorphogenic
CC growth in the darkness as well as abnormal accumulation of HY5
CC (PubMed:26474641, PubMed:18375596). The double mutant shw1 hy5 has
CC altered root growth, hypocotyl length and hook angle similar to the
CC single mutant shw1 in the darkness and far red light (FR), but shorter
CC hypocotyl in WL, red light (RL) and blue light (BL). In addition, shw1
CC hy5 is recued for gravitropic root growth defect observed in hy5 single
CC mutant (PubMed:26474641). {ECO:0000269|PubMed:18375596,
CC ECO:0000269|PubMed:19704523, ECO:0000269|PubMed:26474641}.
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DR EMBL; AM419013; CAL91513.1; -; mRNA.
DR EMBL; AC010675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE35000.1; -; Genomic_DNA.
DR EMBL; AK227492; BAE99492.1; -; mRNA.
DR EMBL; AY084370; AAM60951.1; -; mRNA.
DR RefSeq; NP_564981.1; NM_105662.2. [F4I3V6-1]
DR AlphaFoldDB; F4I3V6; -.
DR STRING; 3702.AT1G69935.1; -.
DR iPTMnet; F4I3V6; -.
DR PaxDb; F4I3V6; -.
DR PRIDE; F4I3V6; -.
DR ProteomicsDB; 234505; -. [F4I3V6-1]
DR EnsemblPlants; AT1G69935.1; AT1G69935.1; AT1G69935. [F4I3V6-1]
DR GeneID; 843330; -.
DR Gramene; AT1G69935.1; AT1G69935.1; AT1G69935. [F4I3V6-1]
DR KEGG; ath:AT1G69935; -.
DR Araport; AT1G69935; -.
DR TAIR; locus:505006215; AT1G69935.
DR eggNOG; ENOG502S0GF; Eukaryota.
DR HOGENOM; CLU_082534_0_0_1; -.
DR InParanoid; F4I3V6; -.
DR OMA; FLEVICN; -.
DR OrthoDB; 1538335at2759; -.
DR PRO; PR:F4I3V6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I3V6; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0010100; P:negative regulation of photomorphogenesis; IMP:UniProtKB.
DR GO; GO:0009958; P:positive gravitropism; IMP:UniProtKB.
DR GO; GO:1901333; P:positive regulation of lateral root development; IMP:UniProtKB.
DR GO; GO:0048578; P:positive regulation of long-day photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0031540; P:regulation of anthocyanin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IMP:UniProtKB.
DR GO; GO:0090227; P:regulation of red or far-red light signaling pathway; IMP:UniProtKB.
DR GO; GO:0009642; P:response to light intensity; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
DR InterPro; IPR039324; SHW1.
DR PANTHER; PTHR35474; PTHR35474; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Flowering; Membrane;
KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..192
FT /note="Protein SHORT HYPOCOTYL IN WHITE LIGHT 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439374"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 70..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..50
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 78..92
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 57..126
FT /note="SRRRYESDDRFFGGGDNYDVVPDDDGFSDDDDEEDERESSVDLLIRFLRSMF
FT KKVSKRTKKASRRILPAA -> VRSDYLLLIELCNPNPNPNLLNLFILSRVGDTNQTID
FT SSAVVTITMLFPMTTDLATMMMKKTKEKAVSIF (in isoform 2)"
FT /id="VSP_058839"
FT VAR_SEQ 127..192
FT /note="Missing (in isoform 2)"
FT /id="VSP_058840"
FT CONFLICT 115
FT /note="T -> A (in Ref. 1; CAL91513 and 5; AAM60951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21367 MW; 22A7ED004E89C403 CRC64;
MAAATTTLSS SSSSPSLTLI NASHRFVSVT PFSSNSIFLR RRFRRLNRSL ASSSSHSRRR
YESDDRFFGG GDNYDVVPDD DGFSDDDDEE DERESSVDLL IRFLRSMFKK VSKRTKKASR
RILPAAMSPR LVSFAVDGIL LLGSLSITRA FLEVICNLGG TVFTVILLIR LFWAAASFFQ
TYGNSFGPNP VN
