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CSPLO_ARATH
ID   CSPLO_ARATH             Reviewed;         190 AA.
AC   Q8L8Z1; O23414; Q570K0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=CASP-like protein 1E1;
DE            Short=AtCASPL1E1;
GN   OrderedLocusNames=At4g15630; ORFNames=Dl3855w, FCAALL.230;
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=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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].
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].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA   Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA   Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT   "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT   proteome.";
RL   Mol. Cell. Proteomics 3:675-691(2004).
RN   [8]
RP   INTERACTION WITH AHK4.
RX   PubMed=18642946; DOI=10.1021/pr0703831;
RA   Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT   "Toward an interaction map of the two-component signaling pathway of
RT   Arabidopsis thaliana.";
RL   J. Proteome Res. 7:3649-3660(2008).
RN   [9]
RP   SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=24920445; DOI=10.1104/pp.114.239137;
RA   Roppolo D., Boeckmann B., Pfister A., Boutet E., Rubio M.C.,
RA   Denervaud-Tendon V., Vermeer J.E., Gheyselinck J., Xenarios I., Geldner N.;
RT   "Functional and evolutionary analysis of the CASPARIAN STRIP MEMBRANE
RT   DOMAIN PROTEIN family.";
RL   Plant Physiol. 165:1709-1722(2014).
CC   -!- SUBUNIT: Homodimer and heterodimers. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8L8Z1; Q9C5U0: AHK4; NbExp=2; IntAct=EBI-1807704, EBI-1100775;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130,
CC       ECO:0000269|PubMed:24920445}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:24920445}.
CC   -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC       family. {ECO:0000305}.
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DR   EMBL; Z97339; CAB10341.1; -; Genomic_DNA.
DR   EMBL; AL161542; CAB78605.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83630.1; -; Genomic_DNA.
DR   EMBL; AK220708; BAD93816.1; -; mRNA.
DR   EMBL; AK229320; BAF01183.1; -; mRNA.
DR   EMBL; BT028921; ABI49468.1; -; mRNA.
DR   EMBL; AY088726; AAM67044.1; -; mRNA.
DR   PIR; C71421; C71421.
DR   RefSeq; NP_567473.1; NM_117654.3.
DR   AlphaFoldDB; Q8L8Z1; -.
DR   SMR; Q8L8Z1; -.
DR   BioGRID; 12534; 1.
DR   IntAct; Q8L8Z1; 1.
DR   STRING; 3702.AT4G15630.1; -.
DR   PaxDb; Q8L8Z1; -.
DR   PRIDE; Q8L8Z1; -.
DR   ProteomicsDB; 224439; -.
DR   EnsemblPlants; AT4G15630.1; AT4G15630.1; AT4G15630.
DR   GeneID; 827240; -.
DR   Gramene; AT4G15630.1; AT4G15630.1; AT4G15630.
DR   KEGG; ath:AT4G15630; -.
DR   Araport; AT4G15630; -.
DR   TAIR; locus:2130509; AT4G15630.
DR   eggNOG; ENOG502RZNK; Eukaryota.
DR   HOGENOM; CLU_066104_1_0_1; -.
DR   InParanoid; Q8L8Z1; -.
DR   OMA; IGLMGYQ; -.
DR   OrthoDB; 1468357at2759; -.
DR   PhylomeDB; Q8L8Z1; -.
DR   PRO; PR:Q8L8Z1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8L8Z1; baseline and differential.
DR   Genevisible; Q8L8Z1; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR   InterPro; IPR006459; CASP/CASPL.
DR   InterPro; IPR006702; CASP_dom.
DR   Pfam; PF04535; DUF588; 1.
DR   TIGRFAMs; TIGR01569; A_tha_TIGR01569; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..190
FT                   /note="CASP-like protein 1E1"
FT                   /id="PRO_0000308677"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..83
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..111
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..163
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..190
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        10
FT                   /note="D -> N (in Ref. 5; AAM67044)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="A -> T (in Ref. 5; AAM67044)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124
FT                   /note="V -> M (in Ref. 5; AAM67044)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   190 AA;  20109 MW;  0B70658CC8B3806E CRC64;
     MEHESKNKVD GMEMEKGKKE SGSRKGLELT MRVLALVLTM VAATVLGVAK QTKVVPIKLI
     PTLPPLNVST TAKASYLSAF VYNISANAIA CGYTAISIVI VMISKGKRSK SLLMAVLIGD
     LMMVALLFSS TGAAGAIGLM GRHGNKHVMW KKVCGVFGKF CNQAAVSVAI TLIASVVFML
     LVVLDALKLP
 
 
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