SCAB1_ARATH
ID SCAB1_ARATH Reviewed; 496 AA.
AC O48791;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Stomatal closure-related actin-binding protein 1 {ECO:0000303|PubMed:21719691};
GN Name=SCAB1 {ECO:0000303|PubMed:21719691};
GN OrderedLocusNames=At2g26770 {ECO:0000312|Araport:AT2G26770};
GN ORFNames=F18A8.14 {ECO:0000312|EMBL:AAB95312.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP DOMAIN, AND GENE FAMILY.
RX PubMed=21719691; DOI=10.1105/tpc.111.086546;
RA Zhao Y., Zhao S., Mao T., Qu X., Cao W., Zhang L., Zhang W., He L., Li S.,
RA Ren S., Zhao J., Zhu G., Huang S., Ye K., Yuan M., Guo Y.;
RT "The plant-specific actin binding protein SCAB1 stabilizes actin filaments
RT and regulates stomatal movement in Arabidopsis.";
RL Plant Cell 23:2314-2330(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 272-496, SUBUNIT, FUNCTION, AND
RP MUTAGENESIS OF VAL-74; ARG-75; LEU-77; PHE-81; ALA-88; LEU-91; VAL-131;
RP VAL-138; LEU-141; ARG-410; LYS-412 AND LYS-422.
RX PubMed=22356912; DOI=10.1074/jbc.m111.338525;
RA Zhang W., Zhao Y., Guo Y., Ye K.;
RT "Plant actin-binding protein SCAB1 is dimeric actin cross-linker with
RT atypical pleckstrin homology domain.";
RL J. Biol. Chem. 287:11981-11990(2012).
CC -!- FUNCTION: Plant-specific actin binding protein that bundles and
CC stabilizes microfilaments (MFs). Has no nucleation or capping activity.
CC Regulates MF reorganization during stomatal closure. The binding to F-
CC actin is insensitive to Ca(2+) and pH. Binds weakly to inositol
CC phosphates (PubMed:22356912). {ECO:0000269|PubMed:21719691,
CC ECO:0000269|PubMed:22356912}.
CC -!- SUBUNIT: Dimer. Dimerization is required for actin-binding activity.
CC {ECO:0000269|PubMed:22356912}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21719691}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers,
CC siliques and guard cells. {ECO:0000269|PubMed:21719691}.
CC -!- DOMAIN: The NT5 region (73-100) is required for actin-binding activity.
CC {ECO:0000269|PubMed:21719691}.
CC -!- DISRUPTION PHENOTYPE: Defect in stomatal movment and hypersensitivity
CC to drought stress. {ECO:0000269|PubMed:21719691}.
CC -!- SIMILARITY: Belongs to the SCAB family. {ECO:0000305}.
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DR EMBL; AC003105; AAB95312.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07884.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07885.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61588.1; -; Genomic_DNA.
DR EMBL; AY136349; AAM97015.1; -; mRNA.
DR EMBL; BT000193; AAN15512.1; -; mRNA.
DR EMBL; AK118842; BAC43431.1; -; mRNA.
DR PIR; F84664; F84664.
DR RefSeq; NP_001323795.1; NM_001336082.1.
DR RefSeq; NP_180245.1; NM_128234.4.
DR RefSeq; NP_850085.1; NM_179754.2.
DR PDB; 4DIX; X-ray; 1.70 A; A/B=272-496.
DR PDB; 4DJG; X-ray; 1.90 A; A/B=100-151.
DR PDBsum; 4DIX; -.
DR PDBsum; 4DJG; -.
DR AlphaFoldDB; O48791; -.
DR SMR; O48791; -.
DR IntAct; O48791; 3.
DR STRING; 3702.AT2G26770.1; -.
DR iPTMnet; O48791; -.
DR PaxDb; O48791; -.
DR PRIDE; O48791; -.
DR ProteomicsDB; 232902; -.
DR EnsemblPlants; AT2G26770.1; AT2G26770.1; AT2G26770.
DR EnsemblPlants; AT2G26770.2; AT2G26770.2; AT2G26770.
DR EnsemblPlants; AT2G26770.3; AT2G26770.3; AT2G26770.
DR GeneID; 817218; -.
DR Gramene; AT2G26770.1; AT2G26770.1; AT2G26770.
DR Gramene; AT2G26770.2; AT2G26770.2; AT2G26770.
DR Gramene; AT2G26770.3; AT2G26770.3; AT2G26770.
DR KEGG; ath:AT2G26770; -.
DR Araport; AT2G26770; -.
DR TAIR; locus:2043828; AT2G26770.
DR eggNOG; ENOG502QQJ6; Eukaryota.
DR HOGENOM; CLU_026412_2_0_1; -.
DR InParanoid; O48791; -.
DR OMA; VRKHDIE; -.
DR OrthoDB; 552427at2759; -.
DR PhylomeDB; O48791; -.
DR PRO; PR:O48791; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48791; baseline and differential.
DR Genevisible; O48791; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:TAIR.
DR GO; GO:0007015; P:actin filament organization; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR InterPro; IPR039640; SCAB.
DR InterPro; IPR032012; SCAB-ABD.
DR InterPro; IPR041144; SCAB-PH.
DR InterPro; IPR032009; SCAB_CC.
DR PANTHER; PTHR31172; PTHR31172; 1.
DR Pfam; PF16711; SCAB-ABD; 1.
DR Pfam; PF17684; SCAB-PH; 1.
DR Pfam; PF16712; SCAB_CC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..496
FT /note="Stomatal closure-related actin-binding protein 1"
FT /id="PRO_0000431807"
FT COILED 126..269
FT /evidence="ECO:0000255"
FT MUTAGEN 74
FT /note="V->A: Loss of actin-binding activity."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 75
FT /note="R->E: Loss of actin-binding activity."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 77
FT /note="L->A: No effect on actin-binding activity."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 81
FT /note="F->A: Loss of actin-binding activity."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 88
FT /note="A->S: No effect on actin-binding activity."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 91
FT /note="L->A: No effect on actin-binding activity."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 131
FT /note="V->D: Loss of dimerization and loss of actin-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 138
FT /note="V->D: Loss of dimerization and loss of actin-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 141
FT /note="L->E: Loss of dimerization and loss of actin-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 410
FT /note="R->N: Loss of inositol phosphates binding."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 412
FT /note="K->N: Loss of inositol phosphates binding."
FT /evidence="ECO:0000269|PubMed:22356912"
FT MUTAGEN 422
FT /note="K->N: Loss of inositol phosphates binding."
FT /evidence="ECO:0000269|PubMed:22356912"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:4DJG"
FT HELIX 125..146
FT /evidence="ECO:0007829|PDB:4DJG"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:4DIX"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:4DIX"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:4DIX"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 380..391
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 401..415
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 418..424
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:4DIX"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:4DIX"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:4DIX"
FT HELIX 462..478
FT /evidence="ECO:0007829|PDB:4DIX"
SQ SEQUENCE 496 AA; 55418 MW; E76335520C2BDF8B CRC64;
MTRVTRDFRD SLQRDGVPAV SADVKFASSR FPNYRIGAND QIFDVKDDPK VMSMKEVVAR
ETAQLMDQQK RLSVRDLAHK FEKGLAAAAK LSEEAKLKEA TSLEKHVLLK KLRDALESLR
GRVAGRNKDD VEEAIAMVEA LAVQLTQREG ELFIEKAEVK KLASFLKQAS EDAKKLVDEE
RAFARAEIES ARAAVQRVEE ALREHEQMSR ASGKQDMEDL MKEVQEARRI KMLHQPSRVM
DMEYELRALR NQLAEKSKHF LQLQKKLAMC RKSEENISLV YEIDGTEALG SCLRVRPCSN
DAPDLSKCTI QWYRSSSDGS KKELISGATK SVYAPEPFDV GRVLHADIIY DGHSLSLSTV
GKIDPAAGLG SYVEALVRKH DVDFNVVVTQ MSGEDHTSES IHLFHVGKMR IKLCKGKTVI
AKEYYSSAMQ LCGVRGGGNA AAQALYWQAK KGVSFVIAFE SERERNAAIM LARRFACDCN
VTLAGPEDRT ETGQSP
