AIP12_ARATH
ID AIP12_ARATH Reviewed; 609 AA.
AC Q9LV35;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Actin-interacting protein 1-2 {ECO:0000303|PubMed:12417710};
GN Name=AIP1-2 {ECO:0000303|PubMed:12417710};
GN OrderedLocusNames=At3g18060 {ECO:0000312|Araport:AT3G18060};
GN ORFNames=MRC8.4 {ECO:0000312|EMBL:BAB02018.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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:0000250|UniProtKB:Q9ZU34}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flower buds and
CC flowers. {ECO:0000269|PubMed:12417710}.
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DR EMBL; AB020749; BAB02018.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76041.1; -; Genomic_DNA.
DR EMBL; AY062436; AAL32514.1; -; mRNA.
DR EMBL; AY114624; AAM47943.1; -; mRNA.
DR RefSeq; NP_188434.2; NM_112688.6.
DR AlphaFoldDB; Q9LV35; -.
DR SMR; Q9LV35; -.
DR IntAct; Q9LV35; 4.
DR STRING; 3702.AT3G18060.1; -.
DR PaxDb; Q9LV35; -.
DR PRIDE; Q9LV35; -.
DR ProteomicsDB; 244888; -.
DR EnsemblPlants; AT3G18060.1; AT3G18060.1; AT3G18060.
DR GeneID; 821331; -.
DR Gramene; AT3G18060.1; AT3G18060.1; AT3G18060.
DR KEGG; ath:AT3G18060; -.
DR Araport; AT3G18060; -.
DR TAIR; locus:2092742; AT3G18060.
DR eggNOG; KOG0318; Eukaryota.
DR HOGENOM; CLU_015246_2_0_1; -.
DR InParanoid; Q9LV35; -.
DR OMA; TNPAKHT; -.
DR OrthoDB; 325552at2759; -.
DR PhylomeDB; Q9LV35; -.
DR PRO; PR:Q9LV35; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LV35; 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:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011045; N2O_reductase_N.
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; 6.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50974; SSF50974; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..609
FT /note="Actin-interacting protein 1-2"
FT /id="PRO_0000436136"
FT REPEAT 2..42
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 54..93
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 97..141
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 142..182
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 185..224
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 230..269
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 277..318
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 322..362
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REPEAT 445..484
FT /note="WD 9"
FT /evidence="ECO:0000255"
FT REPEAT 489..528
FT /note="WD 10"
FT /evidence="ECO:0000255"
FT REPEAT 532..571
FT /note="WD 11"
FT /evidence="ECO:0000255"
FT REPEAT 576..609
FT /note="WD 12"
FT /evidence="ECO:0000255"
SQ SEQUENCE 609 AA; 66041 MW; B3E0676D739664A8 CRC64;
MELSETYACV PSTERGRGIL ISGNSKSDTI LYTNGRSVVT LDLNNPLKVS IYGEHAYPAT
VARYSPNGEW IASGDVSGTV RIWGAYNDHV LKNEFKVLAG RIDDLQWSAD GMRIVASGDG
KGKSLVRAFM WDSGSNVGEF DGHSRRVLSC AIKPTRPFRI VTCGEDFLVN FYEGPPFKFK
LSSREHSNFV NCVRFAPDGS KFITVSSDKK GIIYDGKTCE ILGELSSDDG HKGSIYAVSW
SPDGKQVLTV SADKSAKIWD ISDNGSGSLN TTLNCPGSSG GVDDMLVGCL WQNDHIVTVS
LGGTISIFSA SDLDKSPFQF SGHMKNVSSL AVLKGNADYI LSGSYDGLIC KWMLGRGFCG
KLQRTQNSQI KCFAAHEEEI VTSGYDNKIS RISYKDDQCT NEESIDIGNQ PKDLSLAPLS
PDLLLVTFES GVVFLRDGKV VSTINLGFIV TALAVTPDGT EAVIGGQDGK LHLYSINGDS
LTEEAVLERH RGAISVIRYS PDLSMFASAD LNREAVVWDR VSREMKLKNM LYHSARINCL
AWSPNSTMVA TGSLDTCVIV YEVDKPASSR MTIKGAHLGG VYGLGFADDS HVVSSGEDAC
IRVWSFTPQ
