AIP1_YEAST
ID AIP1_YEAST Reviewed; 615 AA.
AC P46680; D6VZR5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Actin-interacting protein 1;
GN Name=AIP1; OrderedLocusNames=YMR092C; ORFNames=YM9582.17C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Amberg D.C., Botstein D.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP INTERACTION WITH COFILIN, AND FUNCTION.
RX PubMed=10366597; DOI=10.1083/jcb.145.6.1251;
RA Rodal A.A., Tetreault J.W., Lappalainen P., Drubin D.G., Amberg D.C.;
RT "Aip1p interacts with cofilin to disassemble actin filaments.";
RL J. Cell Biol. 145:1251-1264(1999).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND WD REPEATS.
RX PubMed=12807914; DOI=10.1074/jbc.m302773200;
RA Voegtli W.C., Madrona A.Y., Wilson D.K.;
RT "The structure of Aip1p, a WD repeat protein that regulates Cofilin-
RT mediated actin depolymerization.";
RL J. Biol. Chem. 278:34373-34379(2003).
CC -!- FUNCTION: Involved in the depolymerization of actin filaments. Enhances
CC the filament disassembly activity of cofilin and restricts cofilin
CC localization to cortical actin patches. {ECO:0000269|PubMed:10366597}.
CC -!- SUBUNIT: Interacts with actin and cofilin in a ternary complex.
CC {ECO:0000269|PubMed:10366597}.
CC -!- INTERACTION:
CC P46680; P60010: ACT1; NbExp=3; IntAct=EBI-2406, EBI-2169;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC actin patch.
CC -!- MISCELLANEOUS: Present with 11100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family. {ECO:0000305}.
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DR EMBL; U35666; AAA79141.1; -; Genomic_DNA.
DR EMBL; Z49259; CAA89239.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09989.1; -; Genomic_DNA.
DR PIR; S54468; S54468.
DR RefSeq; NP_013810.1; NM_001182592.1.
DR PDB; 1PGU; X-ray; 2.30 A; A/B=1-615.
DR PDB; 1PI6; X-ray; 2.50 A; A=1-615.
DR PDBsum; 1PGU; -.
DR PDBsum; 1PI6; -.
DR AlphaFoldDB; P46680; -.
DR SMR; P46680; -.
DR BioGRID; 35267; 71.
DR DIP; DIP-890N; -.
DR IntAct; P46680; 9.
DR MINT; P46680; -.
DR STRING; 4932.YMR092C; -.
DR iPTMnet; P46680; -.
DR MaxQB; P46680; -.
DR PaxDb; P46680; -.
DR PRIDE; P46680; -.
DR EnsemblFungi; YMR092C_mRNA; YMR092C; YMR092C.
DR GeneID; 855117; -.
DR KEGG; sce:YMR092C; -.
DR SGD; S000004698; AIP1.
DR VEuPathDB; FungiDB:YMR092C; -.
DR eggNOG; KOG0318; Eukaryota.
DR GeneTree; ENSGT00390000009416; -.
DR HOGENOM; CLU_015246_1_0_1; -.
DR InParanoid; P46680; -.
DR OMA; TNPAKHT; -.
DR BioCyc; YEAST:G3O-32792-MON; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR EvolutionaryTrace; P46680; -.
DR PRO; PR:P46680; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P46680; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005884; C:actin filament; IDA:SGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003779; F:actin binding; IPI:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IGI:SGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; IMP:SGD.
DR GO; GO:0032466; P:negative regulation of cytokinesis; IGI:SGD.
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; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..615
FT /note="Actin-interacting protein 1"
FT /id="PRO_0000050841"
FT REPEAT 2..45
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 46..94
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 95..146
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 147..189
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 190..235
FT /note="WD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 236..280
FT /note="WD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 281..325
FT /note="WD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 326..363
FT /note="WD 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 364..399
FT /note="WD 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 400..433
FT /note="WD 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 434..473
FT /note="WD 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 474..516
FT /note="WD 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 517..569
FT /note="WD 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT REPEAT 570..611
FT /note="WD 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12807914"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 103..113
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 256..271
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:1PGU"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 347..350
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 416..424
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 476..482
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:1PGU"
FT TURN 517..520
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 587..594
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 597..602
FT /evidence="ECO:0007829|PDB:1PGU"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:1PGU"
SQ SEQUENCE 615 AA; 67326 MW; B8340BF68DD08257 CRC64;
MSSISLKEII PPQPSTQRNF TTHLSYDPTT NAIAYPCGKS AFVRCLDDGD SKVPPVVQFT
GHGSSVVTTV KFSPIKGSQY LCSGDESGKV IVWGWTFDKE SNSVEVNVKS EFQVLAGPIS
DISWDFEGRR LCVVGEGRDN FGVFISWDSG NSLGEVSGHS QRINACHLKQ SRPMRSMTVG
DDGSVVFYQG PPFKFSASDR THHKQGSFVR DVEFSPDSGE FVITVGSDRK ISCFDGKSGE
FLKYIEDDQE PVQGGIFALS WLDSQKFATV GADATIRVWD VTTSKCVQKW TLDKQQLGNQ
QVGVVATGNG RIISLSLDGT LNFYELGHDE VLKTISGHNK GITALTVNPL ISGSYDGRIM
EWSSSSMHQD HSNLIVSLDN SKAQEYSSIS WDDTLKVNGI TKHEFGSQPK VASANNDGFT
AVLTNDDDLL ILQSFTGDII KSVRLNSPGS AVSLSQNYVA VGLEEGNTIQ VFKLSDLEVS
FDLKTPLRAK PSYISISPSE TYIAAGDVMG KILLYDLQSR EVKTSRWAFH TSKINAISWK
PAEKGANEEE IEEDLVATGS LDTNIFIYSV KRPMKIIKAL NAHKDGVNNL LWETPSTLVS
SGADACIKRW NVVLE
