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CASP2_ARATH
ID   CASP2_ARATH             Reviewed;         204 AA.
AC   Q9CAX3;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Casparian strip membrane protein 2;
DE            Short=AtCASP2;
GN   Name=CASP2; OrderedLocusNames=At3g11550; ORFNames=F24K9.22;
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;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, DIMERIZATION, AND INTERACTION WITH CASP1;
RP   CASP3 AND CASP4.
RC   STRAIN=cv. Columbia;
RX   PubMed=21593871; DOI=10.1038/nature10070;
RA   Roppolo D., De Rybel B., Denervaud Tendon V., Pfister A., Alassimone J.,
RA   Vermeer J.E.M., Yamazaki M., Stierhof Y.-D., Beeckman T., Geldner N.;
RT   "A novel protein family directs Casparian strip formation in the
RT   endodermis.";
RL   Nature 473:380-383(2011).
RN   [5]
RP   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   -!- FUNCTION: Regulates membrane-cell wall junctions and localized cell
CC       wall deposition. Required for establishment of the Casparian strip
CC       membrane domain (CSD) and the subsequent formation of Casparian strips,
CC       a cell wall modification of the root endodermis that determines an
CC       apoplastic barrier between the intraorganismal apoplasm and the
CC       extraorganismal apoplasm and prevents lateral diffusion.
CC       {ECO:0000269|PubMed:21593871}.
CC   -!- SUBUNIT: Homodimer and heterodimers with other CASP proteins. Interacts
CC       with CASP1, CASP3 and CASP4. {ECO:0000269|PubMed:21593871}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21593871};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:21593871}. Note=Very
CC       restricted localization following a belt shape within the plasma
CC       membrane which coincides with the position of the Casparian strip
CC       membrane domain.
CC   -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC       family. {ECO:0000305}.
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DR   EMBL; AC008153; AAG51441.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75062.1; -; Genomic_DNA.
DR   EMBL; BT010843; AAR24210.1; -; mRNA.
DR   EMBL; BT012612; AAT06431.1; -; mRNA.
DR   RefSeq; NP_187762.1; NM_111988.3.
DR   AlphaFoldDB; Q9CAX3; -.
DR   SMR; Q9CAX3; -.
DR   DIP; DIP-59178N; -.
DR   IntAct; Q9CAX3; 3.
DR   STRING; 3702.AT3G11550.1; -.
DR   PaxDb; Q9CAX3; -.
DR   PRIDE; Q9CAX3; -.
DR   ProteomicsDB; 223866; -.
DR   EnsemblPlants; AT3G11550.1; AT3G11550.1; AT3G11550.
DR   GeneID; 820328; -.
DR   Gramene; AT3G11550.1; AT3G11550.1; AT3G11550.
DR   KEGG; ath:AT3G11550; -.
DR   Araport; AT3G11550; -.
DR   TAIR; locus:2080742; AT3G11550.
DR   eggNOG; ENOG502QZV7; Eukaryota.
DR   HOGENOM; CLU_066104_3_1_1; -.
DR   InParanoid; Q9CAX3; -.
DR   OMA; MPRRTHH; -.
DR   OrthoDB; 1230007at2759; -.
DR   PhylomeDB; Q9CAX3; -.
DR   PRO; PR:Q9CAX3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9CAX3; baseline and differential.
DR   Genevisible; Q9CAX3; AT.
DR   GO; GO:0048226; C:Casparian strip; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042545; P:cell wall modification; IMP:UniProtKB.
DR   GO; GO:0007043; P:cell-cell junction assembly; IDA: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; Cell wall biogenesis/degradation; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..204
FT                   /note="Casparian strip membrane protein 2"
FT                   /id="PRO_0000308666"
FT   TOPO_DOM        1..42
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..92
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..204
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   204 AA;  21482 MW;  7EA15EF1A95E289E CRC64;
     MKNESTFIDV PAESSSAMKG KAPLIGVARD HTTSGSGGYN RGLAIFDFLL RLAAIVAALA
     AAATMGTSDE TLPFFTQFLQ FEASYDDLPT FQFFVIAMAL VGGYLVLSLP ISVVTILRPL
     ATAPRLLLLV LDTGVLALNT AAASSAAAIS YLAHSGNQNT NWLPICQQFG DFCQKSSGAV
     VSAFVSVVFF TILVVISGVA LKRH
 
 
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