WIH1_ARATH
ID WIH1_ARATH Reviewed; 82 AA.
AC Q9FJW3; Q8L8M2;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 13 {ECO:0000303|PubMed:29272523};
DE Short=AthCYSTM13 {ECO:0000303|PubMed:29272523};
DE AltName: Full=Cysteine-rich and transmembrane domain-containing protein WIH1 {ECO:0000305};
DE AltName: Full=Protein WINDHOSE 1 {ECO:0000303|PubMed:21658947};
GN Name=WIH1 {ECO:0000303|PubMed:21658947};
GN Synonyms=CYSTM13 {ECO:0000303|PubMed:29272523};
GN OrderedLocusNames=At5g67600 {ECO:0000312|Araport:AT5G67600};
GN ORFNames=K9I9.17 {ECO:0000312|EMBL:BAB08468.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21658947; DOI=10.1016/j.cub.2011.05.015;
RA Lieber D., Lora J., Schrempp S., Lenhard M., Laux T.;
RT "Arabidopsis WIH1 and WIH2 genes act in the transition from somatic to
RT reproductive cell fate.";
RL Curr. Biol. 21:1009-1017(2011).
RN [6]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH CYSTM7; CYTSM3; CYTSM4;
RP CYTSM5; CYTSM6; CYTSM9; CYTSM10; CYTSM11; CYSTM1 AND CYSTM2, TISSUE
RP SPECIFICITY, INDUCTION BY HEAT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=29272523; DOI=10.1093/pcp/pcx202;
RA Xu Y., Yu Z., Zhang D., Huang J., Wu C., Yang G., Yan K., Zhang S.,
RA Zheng C.;
RT "CYSTM, a novel non-secreted cysteine-rich peptide family, involved in
RT environmental stresses in Arabidopsis thaliana.";
RL Plant Cell Physiol. 59:423-438(2018).
CC -!- FUNCTION: Required for the promotion of megasporogenesis, or promotion
CC of germ cell formation from somatic precursor cells. Acts redundantly
CC with WIH2. Functions in a genetic pathway downstream of SPL/NZZ and WUS
CC and together with TRN2 in promoting megasporogenesis (PubMed:21658947).
CC Involved in resistance to abiotic stress (PubMed:29272523).
CC {ECO:0000269|PubMed:21658947, ECO:0000303|PubMed:29272523}.
CC -!- SUBUNIT: Homodimer and heterodimers (PubMed:29272523). Interacts with
CC CYSTM7, CYTSM3, CYTSM4, CYTSM5, CYTSM6, CYTSM9, CYTSM10 and CYTSM11
CC (PubMed:29272523). Binds weakly to CYSTM1 and CYSTM2 (PubMed:29272523).
CC {ECO:0000269|PubMed:29272523}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29272523};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in root meristem, root vasculature, leaf
CC vasculature and floral organ primordia (PubMed:21658947). Mostly
CC expressed in roots and flowers and, to a lower extent, in stems,
CC siliques and leaves (PubMed:29272523). {ECO:0000269|PubMed:21658947,
CC ECO:0000269|PubMed:29272523}.
CC -!- DEVELOPMENTAL STAGE: During ovule development, expressed in the
CC nucellus from early stage until embryo sac maturity.
CC {ECO:0000269|PubMed:21658947}.
CC -!- INDUCTION: Induced by heat in roots. {ECO:0000269|PubMed:29272523}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but flowers of the double mutants wih1-1 and wih2-1 have
CC defect in megasporgogenesis. Doubl mutant plants display retarded
CC growth, and twisted leaves, siliques and roots.
CC {ECO:0000269|PubMed:21658947}.
CC -!- SIMILARITY: Belongs to the CYSTM1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB013390; BAB08468.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98365.1; -; Genomic_DNA.
DR EMBL; AY040021; AAK64178.1; -; mRNA.
DR EMBL; AY114014; AAM45062.1; -; mRNA.
DR EMBL; AY088911; AAM67217.1; -; mRNA.
DR RefSeq; NP_569052.1; NM_126160.4.
DR AlphaFoldDB; Q9FJW3; -.
DR STRING; 3702.AT5G67600.1; -.
DR PaxDb; Q9FJW3; -.
DR PRIDE; Q9FJW3; -.
DR ProteomicsDB; 242549; -.
DR EnsemblPlants; AT5G67600.1; AT5G67600.1; AT5G67600.
DR GeneID; 836896; -.
DR Gramene; AT5G67600.1; AT5G67600.1; AT5G67600.
DR KEGG; ath:AT5G67600; -.
DR Araport; AT5G67600; -.
DR TAIR; locus:2158631; AT5G67600.
DR eggNOG; ENOG502S205; Eukaryota.
DR HOGENOM; CLU_128451_1_0_1; -.
DR InParanoid; Q9FJW3; -.
DR OMA; WRRRTKP; -.
DR PRO; PR:Q9FJW3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJW3; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0009554; P:megasporogenesis; IGI:TAIR.
DR InterPro; IPR044850; WIH2-like.
DR PANTHER; PTHR31568; PTHR31568; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..82
FT /note="Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 13"
FT /id="PRO_0000440182"
FT TRANSMEM 59..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 75
FT /note="C -> F (in Ref. 4; AAM67217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 82 AA; 8711 MW; A0E43CC24E8762A2 CRC64;
MYHQEQHPVG APPPQGYPPK DGYPPAGYPP AGYPPPGYAQ GYPAQGYPPP QYSQAPQQKQ
NAGMLEGCLA ALCCCCLLDA CF
