CLB_ARATH
ID CLB_ARATH Reviewed; 510 AA.
AC Q9LEX1; P92940;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Calcium-dependent lipid-binding protein {ECO:0000303|PubMed:21252258};
DE Short=AtCLB {ECO:0000303|PubMed:21252258};
DE Short=CaLB protein {ECO:0000303|PubMed:15238157};
DE AltName: Full=Protein NTMC 2 TYPE 4;
DE Short=NTMC2TYPE4;
GN Name=CLB {ECO:0000303|PubMed:21252258}; Synonyms=NTMC2T4;
GN OrderedLocusNames=At3g61050 {ECO:0000312|Araport:AT3G61050};
GN ORFNames=T27I15.140 {ECO:0000312|EMBL:CAB94141.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
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 [MRNA] OF 13-510.
RA Kopka J., Pical C., Gray J.E., Mueller-Roeber B.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15238157; DOI=10.1186/1471-2164-5-43;
RA Craxton M.A.;
RT "Synaptotagmin gene content of the sequenced genomes.";
RL BMC Genomics 5:43-43(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21252258; DOI=10.1093/jxb/erq468;
RA de Silva K., Laska B., Brown C., Sederoff H.W., Khodakovskaya M.;
RT "Arabidopsis thaliana calcium-dependent lipid-binding protein (AtCLB): a
RT novel repressor of abiotic stress response.";
RL J. Exp. Bot. 62:2679-2689(2011).
RN [9]
RP INTERACTION WITH THE MICROBOTRYUM VIOLACEUM EFFECTOR MVLG_01732.
RX PubMed=29165363; DOI=10.3390/ijms18112489;
RA Kuppireddy V.S., Uversky V.N., Toh S.S., Tsai M.C., Beckerson W.C.,
RA Cahill C., Carman B., Perlin M.H.;
RT "Identification and initial characterization of the effectors of an anther
RT smut fungus and potential host target proteins.";
RL Int. J. Mol. Sci. 18:0-0(2017).
CC -!- FUNCTION: May be involved in membrane trafficking (By similarity). Acts
CC as a repressor of abiotic stress (e.g. drought and salt) responses by
CC binding specifically to the promoter of THAS1 to regulate its
CC transcription (PubMed:21252258). Binds to membrane lipid ceramides
CC (PubMed:21252258). {ECO:0000250|UniProtKB:B6ETT4,
CC ECO:0000269|PubMed:21252258}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:A0FGR8};
CC -!- SUBUNIT: Interacts with the biotrophic pathogenic fungi Microbotryum
CC violaceum effector MVLG_01732. {ECO:0000269|PubMed:29165363}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:21252258};
CC Single-pass membrane protein {ECO:0000255}. Note=Localized in the
CC nucleus membrane of root tips cells. {ECO:0000269|PubMed:21252258}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in rosette leaves and flowers, to
CC lower extent, in cauline leaves, roots and stems, and, at low levels,
CC in siliques. {ECO:0000269|PubMed:21252258}.
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind
CC various types of glycerophospholipids in its interior and mediate their
CC transfer between two adjacent bilayers. {ECO:0000255|PROSITE-
CC ProRule:PRU01194}.
CC -!- DISRUPTION PHENOTYPE: Enhanced drought and salt tolerance and modified
CC gravitropic response associated with an increased expression of THAS1
CC (PubMed:21252258). Higher root lengths (PubMed:21252258).
CC {ECO:0000269|PubMed:21252258}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA65416.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AL358732; CAB94141.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80144.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80145.1; -; Genomic_DNA.
DR EMBL; BT004564; AAO42810.1; -; mRNA.
DR EMBL; AK227322; BAE99336.1; -; mRNA.
DR EMBL; X96598; CAA65416.1; ALT_INIT; mRNA.
DR PIR; T50526; T50526.
DR RefSeq; NP_001030908.1; NM_001035831.2.
DR RefSeq; NP_191664.1; NM_115969.3.
DR AlphaFoldDB; Q9LEX1; -.
DR SMR; Q9LEX1; -.
DR STRING; 3702.AT3G61050.2; -.
DR PaxDb; Q9LEX1; -.
DR PRIDE; Q9LEX1; -.
DR ProteomicsDB; 181262; -.
DR EnsemblPlants; AT3G61050.1; AT3G61050.1; AT3G61050.
DR EnsemblPlants; AT3G61050.2; AT3G61050.2; AT3G61050.
DR GeneID; 825277; -.
DR Gramene; AT3G61050.1; AT3G61050.1; AT3G61050.
DR Gramene; AT3G61050.2; AT3G61050.2; AT3G61050.
DR KEGG; ath:AT3G61050; -.
DR Araport; AT3G61050; -.
DR TAIR; locus:2100992; AT3G61050.
DR eggNOG; KOG1012; Eukaryota.
DR HOGENOM; CLU_042212_1_0_1; -.
DR InParanoid; Q9LEX1; -.
DR OMA; WSRMMTH; -.
DR OrthoDB; 52746at2759; -.
DR PhylomeDB; Q9LEX1; -.
DR PRO; PR:Q9LEX1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LEX1; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0097001; F:ceramide binding; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR031069; CLB_plant.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR045050; Synaptotagmin_plant.
DR InterPro; IPR039010; Synaptotagmin_SMP.
DR PANTHER; PTHR10774; PTHR10774; 1.
DR PANTHER; PTHR10774:SF201; PTHR10774:SF201; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF17047; SMP_LBD; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Calcium; Coiled coil; Lipid transport; Lipid-binding; Membrane;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Stress response; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..510
FT /note="Calcium-dependent lipid-binding protein"
FT /id="PRO_0000450279"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 66..250
FT /note="SMP-LTD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 66..248
FT /note="SMP-LTD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 242..362
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 246..364
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 461..500
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 226..488
FT /note="Phospholipid binding"
FT /evidence="ECO:0000250|UniProtKB:P48018"
FT REGION 484..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 390..417
FT /evidence="ECO:0000255"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0FGR8"
FT CONFLICT 118
FT /note="L -> S (in Ref. 5; CAA65416)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="V -> F (in Ref. 5; CAA65416)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..304
FT /note="KAIE -> NAID (in Ref. 5; CAA65416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 55095 MW; 5AA0254953E166F6 CRC64;
MGLISGILFG IIFGVALMAG WSRMMTHRSS KRVAKAVDMK LLGSLSRDDL KKICGDNFPQ
WISFPAFEQV KWLNKLLSKM WPYIAEAATM VIRDSVEPLL EDYRPPGITS LKFSKLTLGN
VAPKIEGIRV QSFKEGQVTM DVDLRWGGDP NIVLGVTALV ASIPIQLKDL QVFTVARVIF
QLADEIPCIS AVVVALLAEP KPRIDYTLKA VGGSLTAIPG LSDMIDDTVD TIVKDMLQWP
HRIVVPIGGI PVDLSDLELK PQGKLIVTVV KATNLKNKEL IGKSDPYATI YIRPVFKYKT
KAIENNLNPV WDQTFELIAE DKETQSLTVE VFDKDVGQDE RLGLVKLPLS SLEAGVTKEL
ELNLLSSLDT LKVKDKKDRG SITLKVHYHE FNKEEQMAAL EDEKKIMEER KRLKEAGVIG
STMDAVGMVG SGLGAGVGMV GTGIGTGVGL VGSGVSSGVG MVGSGFGAVG SGLSKAGRFM
GRTITGQSSK RSGSSTPVNT VPENDGAKQQ
