ACR11_ARATH
ID ACR11_ARATH Reviewed; 290 AA.
AC Q9FZ47;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=ACT domain-containing protein ACR11 {ECO:0000305};
DE AltName: Full=Protein ACT DOMAIN REPEATS 11 {ECO:0000303|PubMed:21861936};
DE Flags: Precursor;
GN Name=ACR11 {ECO:0000303|PubMed:21861936};
GN OrderedLocusNames=At1g16880 {ECO:0000312|Araport:AT1G16880};
GN ORFNames=F6I1.12 {ECO:0000312|EMBL:AAF99845.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY LIGHT.
RX PubMed=21861936; DOI=10.1186/1471-2229-11-118;
RA Sung T.Y., Chung T.Y., Hsu C.P., Hsieh M.H.;
RT "The ACR11 encodes a novel type of chloroplastic ACT domain repeat protein
RT that is coordinately expressed with GLN2 in Arabidopsis.";
RL BMC Plant Biol. 11:118-118(2011).
RN [2]
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 [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;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY LIGHT.
RX PubMed=16548064; DOI=10.1002/pmic.200500657;
RA Wang B.C., Wang H.X., Feng J.X., Meng D.Z., Qu L.J., Zhu Y.X.;
RT "Post-translational modifications, but not transcriptional regulation, of
RT major chloroplast RNA-binding proteins are related to Arabidopsis seedling
RT development.";
RL Proteomics 6:2555-2563(2006).
CC -!- FUNCTION: May be involved in feedback regulation of amino acid
CC metabolism. May be involved in the regulation of glutamine metabolism.
CC {ECO:0000303|PubMed:21861936}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21861936}.
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=Q9FZ47-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, rosette leaves, stems,
CC sepals, style, and tip of pedicel in mature siliques.
CC {ECO:0000269|PubMed:21861936}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:16548064,
CC ECO:0000269|PubMed:21861936}.
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DR EMBL; JF797176; AEP31952.1; -; mRNA.
DR EMBL; AC051629; AAF99845.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29513.1; -; Genomic_DNA.
DR EMBL; AF386988; AAK62433.1; -; mRNA.
DR EMBL; BT006317; AAP13425.1; -; mRNA.
DR PIR; B86304; B86304.
DR RefSeq; NP_564010.1; NM_101549.5. [Q9FZ47-1]
DR AlphaFoldDB; Q9FZ47; -.
DR STRING; 3702.AT1G16880.1; -.
DR iPTMnet; Q9FZ47; -.
DR PaxDb; Q9FZ47; -.
DR PRIDE; Q9FZ47; -.
DR ProteomicsDB; 244645; -. [Q9FZ47-1]
DR EnsemblPlants; AT1G16880.1; AT1G16880.1; AT1G16880. [Q9FZ47-1]
DR GeneID; 838259; -.
DR Gramene; AT1G16880.1; AT1G16880.1; AT1G16880. [Q9FZ47-1]
DR KEGG; ath:AT1G16880; -.
DR Araport; AT1G16880; -.
DR TAIR; locus:2015616; AT1G16880.
DR eggNOG; ENOG502QWKY; Eukaryota.
DR HOGENOM; CLU_066532_1_0_1; -.
DR InParanoid; Q9FZ47; -.
DR OMA; ITKANTG; -.
DR PhylomeDB; Q9FZ47; -.
DR PRO; PR:Q9FZ47; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ47; baseline and differential.
DR Genevisible; Q9FZ47; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR InterPro; IPR040217; ACR1-12.
DR InterPro; IPR002912; ACT_dom.
DR PANTHER; PTHR31096; PTHR31096; 1.
DR PROSITE; PS51671; ACT; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Plastid; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..290
FT /note="ACT domain-containing protein ACR11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431465"
FT DOMAIN 98..178
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 213..283
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 290 AA; 31295 MW; AE77BBE76D6138A0 CRC64;
MAMASASGSA LCFTDASSSL ALRRDCGALC LPPRTVTFGF VDKPLVNLER LRLSTLKIRA
SNATAVENGK QEGSAADSDK VPTPVVIIDQ DSDPDATVLE VTFGDRLGAL LDTMNALKNL
GLNVVKANVY LDSSGKHNKF AITRADSGRK VEDPELLEAI RLTVINNLLE FHPESSSQLA
MGAAFGVLPP TEPIDVDIAT HITIEDDGPD RSLLFIESAD RPGLLVELVK IISDISVAVE
SGEFDTEGLL AKVKFHVSYR NKALIKPLQQ VLANSLRYFL RRPSTDESSF
