位置:首页 > 蛋白库 > CCA23_ARATH
CCA23_ARATH
ID   CCA23_ARATH             Reviewed;         450 AA.
AC   Q38819; Q8VYG1; Q9M9D7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 146.
DE   RecName: Full=Cyclin-A2-3;
DE   AltName: Full=Cyc3c-At;
DE   AltName: Full=Cyclin-3c;
DE   AltName: Full=G2/mitotic-specific cyclin-A2-3;
DE            Short=CycA2;3;
GN   Name=CYCA2-3; Synonyms=CYC3C; OrderedLocusNames=At1g15570;
GN   ORFNames=T16N11.8;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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 [MRNA] OF 224-450.
RC   STRAIN=cv. Columbia;
RA   Lu G., Ferl R.J.;
RT   "An Arabidopsis cDNA clone encoding cyclin.";
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15208425; DOI=10.1104/pp.104.040436;
RA   Wang G., Kong H., Sun Y., Zhang X., Zhang W., Altman N., dePamphilis C.W.,
RA   Ma H.;
RT   "Genome-wide analysis of the cyclin family in Arabidopsis and comparative
RT   phylogenetic analysis of plant cyclin-like proteins.";
RL   Plant Physiol. 135:1084-1099(2004).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDKA-1.
RX   PubMed=16415207; DOI=10.1105/tpc.105.037309;
RA   Imai K.K., Ohashi Y., Tsuge T., Yoshizumi T., Matsui M., Oka A., Aoyama T.;
RT   "The A-type cyclin CYCA2;3 is a key regulator of ploidy levels in
RT   Arabidopsis endoreduplication.";
RL   Plant Cell 18:382-396(2006).
RN   [7]
RP   REGULATION BY MYB88 AND MYB124.
RX   PubMed=21772250; DOI=10.1038/emboj.2011.240;
RA   Vanneste S., Coppens F., Lee E., Donner T.J., Xie Z., Van Isterdael G.,
RA   Dhondt S., De Winter F., De Rybel B., Vuylsteke M., De Veylder L.,
RA   Friml J., Inze D., Grotewold E., Scarpella E., Sack F., Beemster G.T.,
RA   Beeckman T.;
RT   "Developmental regulation of CYCA2s contributes to tissue-specific
RT   proliferation in Arabidopsis.";
RL   EMBO J. 30:3430-3441(2011).
RN   [8]
RP   INTERACTION WITH SAMBA.
RX   PubMed=22869741; DOI=10.1073/pnas.1211418109;
RA   Eloy N.B., Gonzalez N., Van Leene J., Maleux K., Vanhaeren H., De Milde L.,
RA   Dhondt S., Vercruysse L., Witters E., Mercier R., Cromer L., Beemster G.T.,
RA   Remaut H., Van Montagu M.C., De Jaeger G., Ferreira P.C., Inze D.;
RT   "SAMBA, a plant-specific anaphase-promoting complex/cyclosome regulator is
RT   involved in early development and A-type cyclin stabilization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:13853-13858(2012).
RN   [9]
RP   FUNCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=24687979; DOI=10.1093/jxb/eru139;
RA   Yang K., Wang H., Xue S., Qu X., Zou J., Le J.;
RT   "Requirement for A-type cyclin-dependent kinase and cyclins for the
RT   terminal division in the stomatal lineage of Arabidopsis.";
RL   J. Exp. Bot. 65:2449-2461(2014).
CC   -!- FUNCTION: Negatively regulates endocycles and acts as a regulator of
CC       ploidy levels in endoreduplication (PubMed:16415207). Promotes
CC       divisions in the guard cells (GCs) after the guard mother cells (GMC)
CC       symmetric division (PubMed:24687979). {ECO:0000269|PubMed:16415207,
CC       ECO:0000269|PubMed:24687979}.
CC   -!- SUBUNIT: Interacts with CDKA-1 (PubMed:16415207). Interacts with SAMBA
CC       (PubMed:22869741). {ECO:0000269|PubMed:16415207,
CC       ECO:0000269|PubMed:22869741}.
CC   -!- INTERACTION:
CC       Q38819; A0A384L704: At3g12720; NbExp=3; IntAct=EBI-1781564, EBI-25519283;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16415207}.
CC   -!- INDUCTION: Repressed by MYB88 and MYB124 in newly formed guard cells.
CC       {ECO:0000269|PubMed:21772250}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF71982.1; Type=Erroneous gene model prediction; 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; AC013453; AAF71982.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29336.1; -; Genomic_DNA.
DR   EMBL; AY072105; AAL59927.1; -; mRNA.
DR   EMBL; AY096733; AAM20367.1; -; mRNA.
DR   EMBL; U17890; AAA90946.1; -; mRNA.
DR   PIR; F86289; F86289.
DR   PIR; S71193; S71193.
DR   RefSeq; NP_173010.1; NM_101426.5.
DR   AlphaFoldDB; Q38819; -.
DR   SMR; Q38819; -.
DR   BioGRID; 23367; 32.
DR   IntAct; Q38819; 26.
DR   STRING; 3702.AT1G15570.1; -.
DR   PaxDb; Q38819; -.
DR   PRIDE; Q38819; -.
DR   EnsemblPlants; AT1G15570.1; AT1G15570.1; AT1G15570.
DR   GeneID; 838127; -.
DR   Gramene; AT1G15570.1; AT1G15570.1; AT1G15570.
DR   KEGG; ath:AT1G15570; -.
DR   Araport; AT1G15570; -.
DR   TAIR; locus:2196563; AT1G15570.
DR   eggNOG; KOG0654; Eukaryota.
DR   HOGENOM; CLU_020695_13_3_1; -.
DR   InParanoid; Q38819; -.
DR   OMA; AKWTMDQ; -.
DR   OrthoDB; 993640at2759; -.
DR   PhylomeDB; Q38819; -.
DR   PRO; PR:Q38819; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q38819; baseline and differential.
DR   Genevisible; Q38819; AT.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0044839; P:cell cycle G2/M phase transition; IGI:TAIR.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
DR   GO; GO:0010444; P:guard mother cell differentiation; IMP:UniProtKB.
DR   GO; GO:0010311; P:lateral root formation; IGI:TAIR.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:2000123; P:positive regulation of stomatal complex development; IGI:TAIR.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IGI:TAIR.
DR   CDD; cd00043; CYCLIN; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; SSF47954; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Nucleus; Reference proteome.
FT   CHAIN           1..450
FT                   /note="Cyclin-A2-3"
FT                   /id="PRO_0000286995"
FT   REGION          18..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        299
FT                   /note="R -> E (in Ref. 4; AAA90946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="F -> S (in Ref. 4; AAA90946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="E -> G (in Ref. 4; AAA90946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        355
FT                   /note="T -> A (in Ref. 4; AAA90946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="Y -> C (in Ref. 4; AAA90946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="N -> T (in Ref. 4; AAA90946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="E -> D (in Ref. 4; AAA90946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="A -> P (in Ref. 4; AAA90946)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  50642 MW;  8EF3B638843CD478 CRC64;
     MGKENAVSRP FTRSLASALR ASEVTSTTQN QQRVNTKRPA LEDTRATGPN KRKKRAVLGE
     ITNVNSNTAI LEAKNSKQIK KGRGHGLAST SQLATSVTSE VTDLQSRTDA KVEVASNTAG
     NLSVSKGTDN TADNCIEIWN SRLPPRPLGR SASTAEKSAV IGSSTVPDIP KFVDIDSDDK
     DPLLCCLYAP EIHYNLRVSE LKRRPLPDFM ERIQKDVTQS MRGILVDWLV EVSEEYTLAS
     DTLYLTVYLI DWFLHGNYVQ RQQLQLLGIT CMLIASKYEE ISAPRIEEFC FITDNTYTRD
     QVLEMENQVL KHFSFQIYTP TPKTFLRRFL RAAQASRLSP SLEVEFLASY LTELTLIDYH
     FLKFLPSVVA ASAVFLAKWT MDQSNHPWNP TLEHYTTYKA SDLKASVHAL QDLQLNTKGC
     PLSAIRMKYR QEKYKSVAVL TSPKLLDTLF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024