AIP11_ARATH
ID AIP11_ARATH Reviewed; 611 AA.
AC Q9ZU34;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Actin-interacting protein 1-1 {ECO:0000303|PubMed:12417710};
GN Name=AIP1-1 {ECO:0000303|PubMed:12417710};
GN OrderedLocusNames=At2g01330 {ECO:0000312|Araport:AT2G01330};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, INTERACTION WITH ADF2, AND TISSUE SPECIFICITY.
RX PubMed=12417710; DOI=10.1105/tpc.005363;
RA Allwood E.G., Anthony R.G., Smertenko A.P., Reichelt S., Drobak B.K.,
RA Doonan J.H., Weeds A.G., Hussey P.J.;
RT "Regulation of the pollen-specific actin-depolymerizing factor LlADF1.";
RL Plant Cell 14:2915-2927(2002).
CC -!- FUNCTION: Binds actin. Enhances the F-actin depolymerization activity
CC of actin-depolymerizing factor (ADF) proteins.
CC {ECO:0000269|PubMed:12417710}.
CC -!- SUBUNIT: Interacts with ADF2. {ECO:0000269|PubMed:12417710}.
CC -!- TISSUE SPECIFICITY: Expressed in flower buds and flowers.
CC {ECO:0000269|PubMed:12417710}.
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DR EMBL; AC006200; AAD14533.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05436.1; -; Genomic_DNA.
DR PIR; D84423; D84423.
DR RefSeq; NP_178242.3; NM_126194.6.
DR AlphaFoldDB; Q9ZU34; -.
DR SMR; Q9ZU34; -.
DR STRING; 3702.AT2G01330.2; -.
DR PaxDb; Q9ZU34; -.
DR PRIDE; Q9ZU34; -.
DR ProteomicsDB; 244864; -.
DR EnsemblPlants; AT2G01330.1; AT2G01330.1; AT2G01330.
DR GeneID; 814661; -.
DR Gramene; AT2G01330.1; AT2G01330.1; AT2G01330.
DR KEGG; ath:AT2G01330; -.
DR Araport; AT2G01330; -.
DR TAIR; locus:2038761; AT2G01330.
DR eggNOG; KOG0318; Eukaryota.
DR HOGENOM; CLU_015246_2_0_1; -.
DR InParanoid; Q9ZU34; -.
DR OMA; HSSHREH; -.
DR OrthoDB; 325552at2759; -.
DR PhylomeDB; Q9ZU34; -.
DR PRO; PR:Q9ZU34; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU34; baseline and differential.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..611
FT /note="Actin-interacting protein 1-1"
FT /id="PRO_0000436135"
FT REPEAT 3..43
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 55..94
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 98..142
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 143..183
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 186..225
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 231..270
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 282..319
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 323..363
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REPEAT 446..485
FT /note="WD 9"
FT /evidence="ECO:0000255"
FT REPEAT 491..530
FT /note="WD 10"
FT /evidence="ECO:0000255"
FT REPEAT 534..573
FT /note="WD 11"
FT /evidence="ECO:0000255"
FT REPEAT 578..611
FT /note="WD 12"
FT /evidence="ECO:0000255"
SQ SEQUENCE 611 AA; 66387 MW; 4AD416BBAA423321 CRC64;
MAKLLETFPC VPSTERGRGI LISGDSKSDT ILYCNGRSVF IRSLRQLQDV QVYGEHGYAV
TVARYSPNGE WIASADVSGT VRVWGTHNGF VLKNEFRVLA GRVDDLQWSF DGLRIVASGD
GKGKSLVRSF AWDSGNTMGD FDGHSRRVLS CAFKPTRPFR IATCGEDFLV NFYDGPPFKF
HSSHREHSNF VNCIRYSPDG TKFITVSSDK KGMIYDGKTG DKVGELASED GHKGSIYAVS
WSPDSKRVLT VSADKSAKVW EVAEDGTIGS VIKTLSFMES GGAEDMLVGC LWQNDHLITV
SLGGTMSLFS ADDMDKPPLL LSGHIKNVTS LAVLGENQKT ILSCSYDGLI VKWLKGVGYS
CKLQMKDTKI KRLAATESSI FISGYDNMVW RIPLTDNGYG AAEHVDIGHQ PLDISIAVDS
PEATALVSFD SGVVLLNGLN ILSKIDLGFA VAASVISPDG KEAIVGGQDG KLHIYSVSGD
NNLKEEAVLE KHRGALTVIR YSPDLTMFAS GDANREAVVW DRETKQVKLN NMLFHTARIN
SLAWSPNNKM VATGSIDTCV IVYEVDKPAS SRITARNAHL GGVNAVAFID DCTVASSGED
ASVRLWHIEP Q
