WDR1_CAEEL
ID WDR1_CAEEL Reviewed; 611 AA.
AC Q11176; Q86GT5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Actin-interacting protein 1;
DE Short=AIP1;
DE AltName: Full=Uncoordinated protein 78;
GN Name=unc-78; ORFNames=C04F6.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2; TISSUE=Embryo;
RX PubMed=11257131; DOI=10.1083/jcb.152.6.1313;
RA Ono S.;
RT "The Caenorhabditis elegans unc-78 gene encodes a homologue of actin-
RT interacting protein 1 required for organized assembly of muscle actin
RT filaments.";
RL J. Cell Biol. 152:1313-1320(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Induces disassembly of actin filaments in conjunction with
CC ADF/cofilin family proteins. Regulator of actin organization in
CC myofibrils.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q11176-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q11176-2; Sequence=VSP_020108;
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family. {ECO:0000305}.
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DR EMBL; AF324437; AAK11613.1; -; mRNA.
DR EMBL; FO080344; CCD63029.1; -; Genomic_DNA.
DR EMBL; FO080344; CCD63030.1; -; Genomic_DNA.
DR PIR; T15410; T15410.
DR RefSeq; NP_001024356.1; NM_001029185.2. [Q11176-1]
DR PDB; 1NR0; X-ray; 1.70 A; A=1-611.
DR PDB; 1PEV; X-ray; 2.00 A; A=1-611.
DR PDBsum; 1NR0; -.
DR PDBsum; 1PEV; -.
DR AlphaFoldDB; Q11176; -.
DR SMR; Q11176; -.
DR BioGRID; 45571; 23.
DR STRING; 6239.C04F6.4a.1; -.
DR World-2DPAGE; 0011:Q11176; -.
DR EPD; Q11176; -.
DR PaxDb; Q11176; -.
DR PeptideAtlas; Q11176; -.
DR EnsemblMetazoa; C04F6.4a.1; C04F6.4a.1; WBGene00006810. [Q11176-1]
DR GeneID; 180631; -.
DR KEGG; cel:CELE_C04F6.4; -.
DR UCSC; C04F6.4a; c. elegans. [Q11176-1]
DR CTD; 180631; -.
DR WormBase; C04F6.4a; CE03924; WBGene00006810; unc-78. [Q11176-1]
DR eggNOG; KOG0318; Eukaryota.
DR GeneTree; ENSGT00390000009416; -.
DR InParanoid; Q11176; -.
DR OMA; TNPAKHT; -.
DR OrthoDB; 325552at2759; -.
DR PhylomeDB; Q11176; -.
DR EvolutionaryTrace; Q11176; -.
DR PRO; PR:Q11176; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006810; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; IDA:WormBase.
DR GO; GO:0016528; C:sarcoplasm; IDA:WormBase.
DR GO; GO:0003779; F:actin binding; ISS:WormBase.
DR GO; GO:0051015; F:actin filament binding; IDA:WormBase.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0071689; P:muscle thin filament assembly; IMP:WormBase.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:WormBase.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IDA:WormBase.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:WormBase.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
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; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..611
FT /note="Actin-interacting protein 1"
FT /id="PRO_0000051345"
FT REPEAT 57..96
FT /note="WD 1"
FT REPEAT 145..185
FT /note="WD 2"
FT REPEAT 188..227
FT /note="WD 3"
FT REPEAT 237..276
FT /note="WD 4"
FT REPEAT 322..361
FT /note="WD 5"
FT REPEAT 446..485
FT /note="WD 6"
FT REPEAT 489..528
FT /note="WD 7"
FT REPEAT 534..573
FT /note="WD 8"
FT REPEAT 579..610
FT /note="WD 9"
FT VAR_SEQ 516..611
FT /note="IPYSVANNFELAHTNSWTFHTAKVACVSWSPDNVRLATGSLDNSVIVWNMNK
FT PSDHPIIIKGAHAMSSVNSVIWLNETTIVSAGQDSNIKFWNVPF -> SF (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020108"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1NR0"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1NR0"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1NR0"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:1NR0"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:1NR0"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:1NR0"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:1NR0"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:1NR0"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:1NR0"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:1PEV"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 426..438
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 462..467
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 503..510
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 515..519
FT /evidence="ECO:0007829|PDB:1NR0"
FT TURN 520..524
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 539..544
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 548..555
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:1NR0"
FT TURN 576..581
FT /evidence="ECO:0007829|PDB:1PEV"
FT STRAND 584..591
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:1NR0"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:1NR0"
SQ SEQUENCE 611 AA; 65323 MW; 821452C661B5D27A CRC64;
MSEFSQTALF PSLPRTARGT AVVLGNTPAG DKIQYCNGTS VYTVPVGSLT DTEIYTEHSH
QTTVAKTSPS GYYCASGDVH GNVRIWDTTQ TTHILKTTIP VFSGPVKDIS WDSESKRIAA
VGEGRERFGH VFLFDTGTSN GNLTGQARAM NSVDFKPSRP FRIISGSDDN TVAIFEGPPF
KFKSTFGEHT KFVHSVRYNP DGSLFASTGG DGTIVLYNGV DGTKTGVFED DSLKNVAHSG
SVFGLTWSPD GTKIASASAD KTIKIWNVAT LKVEKTIPVG TRIEDQQLGI IWTKQALVSI
SANGFINFVN PELGSIDQVR YGHNKAITAL SSSADGKTLF SADAEGHINS WDISTGISNR
VFPDVHATMI TGIKTTSKGD LFTVSWDDHL KVVPAGGSGV DSSKAVANKL SSQPLGLAVS
ADGDIAVAAC YKHIAIYSHG KLTEVPISYN SSCVALSNDK QFVAVGGQDS KVHVYKLSGA
SVSEVKTIVH PAEITSVAFS NNGAFLVATD QSRKVIPYSV ANNFELAHTN SWTFHTAKVA
CVSWSPDNVR LATGSLDNSV IVWNMNKPSD HPIIIKGAHA MSSVNSVIWL NETTIVSAGQ
DSNIKFWNVP F
