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CAPZA_ARATH
ID   CAPZA_ARATH             Reviewed;         308 AA.
AC   O82631; Q9MA66;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=F-actin-capping protein subunit alpha;
DE   AltName: Full=CapZ alpha;
GN   OrderedLocusNames=At3g05520; ORFNames=F22F7.3;
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].
RC   STRAIN=cv. Columbia;
RA   Klein M., Mueller-Roeber B.;
RT   "Characterization of Arabidopsis thaliana CapZ proteins.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [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).
CC   -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner
CC       to the fast growing ends of actin filaments (barbed end) thereby
CC       blocking the exchange of subunits at these ends. Unlike other capping
CC       proteins (such as gelsolin and severin), these proteins do not sever
CC       actin filaments (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O82631-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AJ001855; CAA05054.1; -; mRNA.
DR   EMBL; AC009606; AAF64531.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74252.1; -; Genomic_DNA.
DR   PIR; T51820; T51820.
DR   RefSeq; NP_187203.1; NM_111425.5. [O82631-1]
DR   AlphaFoldDB; O82631; -.
DR   SMR; O82631; -.
DR   STRING; 3702.AT3G05520.2; -.
DR   iPTMnet; O82631; -.
DR   PaxDb; O82631; -.
DR   PRIDE; O82631; -.
DR   EnsemblPlants; AT3G05520.1; AT3G05520.1; AT3G05520. [O82631-1]
DR   GeneID; 819717; -.
DR   Gramene; AT3G05520.1; AT3G05520.1; AT3G05520. [O82631-1]
DR   KEGG; ath:AT3G05520; -.
DR   Araport; AT3G05520; -.
DR   eggNOG; KOG0836; Eukaryota.
DR   InParanoid; O82631; -.
DR   PhylomeDB; O82631; -.
DR   PRO; PR:O82631; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; O82631; baseline and differential.
DR   Genevisible; O82631; AT.
DR   GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   Gene3D; 3.30.1140.60; -; 1.
DR   Gene3D; 3.90.1150.210; -; 1.
DR   InterPro; IPR002189; CapZ_alpha.
DR   InterPro; IPR037282; CapZ_alpha/beta.
DR   InterPro; IPR042276; CapZ_alpha/beta_2.
DR   InterPro; IPR042489; CapZ_alpha_1.
DR   InterPro; IPR017865; F-actin_cap_asu_CS.
DR   PANTHER; PTHR10653; PTHR10653; 1.
DR   Pfam; PF01267; F-actin_cap_A; 1.
DR   PRINTS; PR00191; FACTINCAPA.
DR   SUPFAM; SSF90096; SSF90096; 1.
DR   PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR   PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE   2: Evidence at transcript level;
KW   Actin capping; Actin-binding; Alternative splicing; Reference proteome.
FT   CHAIN           1..308
FT                   /note="F-actin-capping protein subunit alpha"
FT                   /id="PRO_0000208640"
FT   CONFLICT        160
FT                   /note="N -> T (in Ref. 1; CAA05054)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   308 AA;  35038 MW;  81BA92AE0DF39B41 CRC64;
     MADEEDELLE TELSYDQKKE IAKWFFLNAP AGEINYVAKD LKAVLSDEEV YNEAAMEAFP
     VYNKTHMICL EMPSGAGDVI VSSYSEINEN EYLDPRTAQV AIVDHVKQIC TKVRPANDEE
     LPSLYIEEYR YALDAEIQRY VSESYPKGMS AVNCVKGKDN EGPGSDFELV VIITAMRLSP
     QNFCNGSWRS VWNIDFQDES QVLDIKGKLQ VGAHYFEEGN VELDAKKDFQ DSTIFQSADD
     CAIAIANIIR HHETEYLASL EVAYSKLPDN TFKDLRRKLP VTRTLFPWQN TLQFSLTREV
     EKELGLGK
 
 
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