SPR1_ARATH
ID SPR1_ARATH Reviewed; 119 AA.
AC Q9SJW3; O49622;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Protein SPIRAL1;
DE AltName: Full=Protein NAP16kDa;
GN Name=SPR1; Synonyms=SKU6; OrderedLocusNames=At2g03680; ORFNames=F19B11.13;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15084720; DOI=10.1105/tpc.017830;
RA Nakajima K., Furutani I., Tachimoto H., Matsubara H., Hashimoto T.;
RT "SPIRAL1 encodes a plant-specific microtubule-localized protein required
RT for directional control of rapidly expanding Arabidopsis cells.";
RL Plant Cell 16:1178-1190(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RA Bartling D.;
RT "Two-hybrid screening in yeast and co-immunoprecipitation of a nitrilase
RT binding protein gives evidence of a plant plasma membrane bound complex of
RT IAA-biosynthesis in Arabidopsis.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11003843; DOI=10.1242/dev.127.20.4443;
RA Furutani I., Watanabe Y., Prieto R., Masukawa M., Suzuki K., Naoi K.,
RA Thitamadee S., Shikanai T., Hashimoto T.;
RT "The SPIRAL genes are required for directional control of cell elongation
RT in Aarabidopsis thaliana.";
RL Development 127:4443-4453(2000).
RN [8]
RP GENE FAMILY.
RA Nakajima K., Kawamura T., Furutani I., Hashimoto T.;
RT "Functional analysis of SPIRAL1-LIKE genes.";
RL (In) Proceedings of the 13th international conference on Arabidopsis
RL research, abstract#7-28, Seville (2002).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15155883; DOI=10.1105/tpc.020644;
RA Sedbrook J.C., Ehrhardt D.W., Fisher S.E., Scheible W.R., Somerville C.R.;
RT "The Arabidopsis sku6/spiral1 gene encodes a plus end-localized
RT microtubule-interacting protein involved in directional cell expansion.";
RL Plant Cell 16:1506-1520(2004).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND GENE FAMILY.
RX PubMed=16478750; DOI=10.1093/pcp/pcj020;
RA Nakajima K., Kawamura T., Hashimoto T.;
RT "Role of the SPIRAL1 gene family in anisotropic growth of Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 47:513-522(2006).
RN [11]
RP FUNCTION, AND DEGRADATION BY PROTEASOME.
RX PubMed=21954463; DOI=10.1105/tpc.111.089920;
RA Wang S., Kurepa J., Hashimoto T., Smalle J.A.;
RT "Salt stress-induced disassembly of Arabidopsis cortical microtubule arrays
RT involves 26S proteasome-dependent degradation of SPIRAL1.";
RL Plant Cell 23:3412-3427(2011).
CC -!- FUNCTION: Required for directional control of cell elongation.
CC Stabilizes growing ends of cortical microtubules and influences their
CC dynamic properties. Acts redundantly with SP1Ls in maintaining the
CC cortical microtubules organization essential for anisotropic cell
CC growth. Plays a key role in salt stress-induced microtubules
CC disassembly. {ECO:0000269|PubMed:11003843, ECO:0000269|PubMed:15084720,
CC ECO:0000269|PubMed:15155883, ECO:0000269|PubMed:16478750,
CC ECO:0000269|PubMed:21954463}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:15155883}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:15155883}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. High expression was associated with
CC tissues undergoing rapid cell expansion, including the root elongation
CC zone, hypocotyls of dark grown-seedlings, and cotyledons of light-grown
CC seedlings. {ECO:0000269|PubMed:15084720, ECO:0000269|PubMed:15155883,
CC ECO:0000269|PubMed:16478750}.
CC -!- PTM: Ubiquitinated (Probable). Upon salt-stress induction, it is
CC subject to proteasome-dependent degradation. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Isotropic expansion of endodermal and cortical
CC cells in root, etiolated hypocotyl, and dark-grown influorescent stem,
CC and induce right-handed spiral in epidermal cell files of these organs.
CC {ECO:0000269|PubMed:11003843, ECO:0000269|PubMed:15155883}.
CC -!- SIMILARITY: Belongs to the SPIRAL1 family. {ECO:0000305}.
CC -!- CAUTION: Was originally (Ref.2) erroneously thought to be a nitrilase
CC associated protein NAP16kDa. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB09665.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY464947; AAS38571.1; -; mRNA.
DR EMBL; Z96936; CAB09665.1; ALT_FRAME; mRNA.
DR EMBL; AC006836; AAD20083.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05735.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05736.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61758.1; -; Genomic_DNA.
DR EMBL; AF412118; AAL06570.1; -; mRNA.
DR EMBL; AY045933; AAK76607.1; -; mRNA.
DR EMBL; AY113867; AAM44915.1; -; mRNA.
DR EMBL; AY084847; AAM61412.1; -; mRNA.
DR PIR; B84451; B84451.
DR RefSeq; NP_001154491.1; NM_001161019.2.
DR RefSeq; NP_001323957.1; NM_001335199.1.
DR RefSeq; NP_178464.1; NM_126416.3.
DR AlphaFoldDB; Q9SJW3; -.
DR BioGRID; 297; 3.
DR IntAct; Q9SJW3; 1.
DR STRING; 3702.AT2G03680.2; -.
DR iPTMnet; Q9SJW3; -.
DR PaxDb; Q9SJW3; -.
DR PRIDE; Q9SJW3; -.
DR ProteomicsDB; 245346; -.
DR EnsemblPlants; AT2G03680.1; AT2G03680.1; AT2G03680.
DR EnsemblPlants; AT2G03680.2; AT2G03680.2; AT2G03680.
DR EnsemblPlants; AT2G03680.3; AT2G03680.3; AT2G03680.
DR GeneID; 814896; -.
DR Gramene; AT2G03680.1; AT2G03680.1; AT2G03680.
DR Gramene; AT2G03680.2; AT2G03680.2; AT2G03680.
DR Gramene; AT2G03680.3; AT2G03680.3; AT2G03680.
DR KEGG; ath:AT2G03680; -.
DR Araport; AT2G03680; -.
DR TAIR; locus:2044224; AT2G03680.
DR eggNOG; ENOG502S4KK; Eukaryota.
DR HOGENOM; CLU_129558_0_0_1; -.
DR InParanoid; Q9SJW3; -.
DR OMA; PCNSEPI; -.
DR OrthoDB; 1632388at2759; -.
DR PhylomeDB; Q9SJW3; -.
DR PRO; PR:Q9SJW3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJW3; baseline and differential.
DR Genevisible; Q9SJW3; AT.
DR GO; GO:0010005; C:cortical microtubule, transverse to long axis; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0009574; C:preprophase band; IDA:TAIR.
DR GO; GO:0005876; C:spindle microtubule; IDA:TAIR.
DR GO; GO:0051211; P:anisotropic cell growth; IMP:TAIR.
DR GO; GO:0071472; P:cellular response to salt stress; IGI:TAIR.
DR GO; GO:0043622; P:cortical microtubule organization; IGI:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR InterPro; IPR039613; SPR1/2/3/4/5.
DR PANTHER; PTHR33403; PTHR33403; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Microtubule; Reference proteome; Ubl conjugation.
FT CHAIN 1..119
FT /note="Protein SPIRAL1"
FT /id="PRO_0000417952"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 119 AA; 11920 MW; 5D2281B17D942FD6 CRC64;
MGRGNSCGGG QSSLDYLFGG DAPAPKPVPA PRPAPTESNN GPAPPVTAVT ATALTTATTS
VEPAELNKQI PAGIKTPVNN YARAEGQNTG NFLTDRPSTK VHAAPGGGSS LDYLFTGGK
