AIP1_DICDI
ID AIP1_DICDI Reviewed; 597 AA.
AC P54686; Q54XM3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Actin-interacting protein 1;
DE Short=DAip1;
DE AltName: Full=WD repeat-containing protein 2 homolog;
GN Name=aip1; Synonyms=wdpA; ORFNames=DDB_G0278733;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RA Mueller-Taubenberger A., Gerisch G.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10427097; DOI=10.1083/jcb.146.2.453;
RA Konzok A., Weber I., Simmeth E., Hacker U., Maniak M.,
RA Muller-Taubenberger A.;
RT "DAip1, a Dictyostelium homologue of the yeast actin-interacting protein 1,
RT is involved in endocytosis, cytokinesis, and motility.";
RL J. Cell Biol. 146:453-464(1999).
RN [4]
RP FUNCTION, INTERACTION WITH COFILIN AND F-ACTIN, AND MUTAGENESIS OF GLU-125;
RP GLU-167; PHE-181 AND PHE-193.
RX PubMed=20668166; DOI=10.1091/mbc.e09-12-1058;
RA Choi C.H., Patel H., Barber D.L.;
RT "Expression of actin-interacting protein 1 suppresses impaired chemotaxis
RT of Dictyostelium cells lacking the Na+-H+ exchanger NHE1.";
RL Mol. Biol. Cell 21:3162-3170(2010).
CC -!- FUNCTION: Implicated in both actin filament depolymerization and
CC polymerization. May enhance chemotaxis by promoting cofilin-dependent
CC actin assembly at cell leading edges. {ECO:0000269|PubMed:10427097,
CC ECO:0000269|PubMed:20668166}.
CC -!- SUBUNIT: Interacts with cofilin and F-actin.
CC {ECO:0000269|PubMed:20668166}.
CC -!- SUBCELLULAR LOCATION: Cell projection, phagocytic cup
CC {ECO:0000269|PubMed:10427097}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:10427097}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:10427097}. Note=Localizes to dynamic regions of the
CC cell cortex that are enriched in filamentous actin and rapidly
CC redistributes to newly formed cortical protrusions.
CC -!- DISRUPTION PHENOTYPE: Impairment of growth, macropinocytosis,
CC phagocytosis and movement. Prolonged cytokinesis with exaggerated
CC cortical protrusions and production of multinucleate cells.
CC {ECO:0000269|PubMed:10427097}.
CC -!- MISCELLANEOUS: Suppresses the impaired F-actin assembly and defective
CC chemotaxis characteristic of cells lacking the sodium/hydrogen
CC exchanger nhe1.
CC -!- SIMILARITY: Belongs to the WD repeat AIP1 family. {ECO:0000305}.
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DR EMBL; U36936; AAB05588.1; -; mRNA.
DR EMBL; AAFI02000024; EAL67968.1; -; Genomic_DNA.
DR RefSeq; XP_642008.1; XM_636916.1.
DR AlphaFoldDB; P54686; -.
DR SMR; P54686; -.
DR STRING; 44689.DDB0214916; -.
DR PaxDb; P54686; -.
DR PRIDE; P54686; -.
DR EnsemblProtists; EAL67968; EAL67968; DDB_G0278733.
DR GeneID; 8621739; -.
DR KEGG; ddi:DDB_G0278733; -.
DR dictyBase; DDB_G0278733; aip1.
DR eggNOG; KOG0318; Eukaryota.
DR HOGENOM; CLU_015246_2_0_1; -.
DR InParanoid; P54686; -.
DR OMA; TNPAKHT; -.
DR PhylomeDB; P54686; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR PRO; PR:P54686; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0042641; C:actomyosin; IDA:dictyBase.
DR GO; GO:0060187; C:cell pole; IDA:dictyBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:dictyBase.
DR GO; GO:0061836; C:intranuclear rod; IDA:dictyBase.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0030042; P:actin filament depolymerization; IMP:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IGI:dictyBase.
DR GO; GO:0030041; P:actin filament polymerization; IGI:dictyBase.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IGI:dictyBase.
DR GO; GO:0030010; P:establishment of cell polarity; IGI:dictyBase.
DR GO; GO:1905861; P:intranuclear rod assembly; IMP:dictyBase.
DR GO; GO:1903673; P:mitotic cleavage furrow formation; IGI:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
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; 6.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Chemotaxis; Cytoplasm; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..597
FT /note="Actin-interacting protein 1"
FT /id="PRO_0000051333"
FT REPEAT 56..95
FT /note="WD 1"
FT REPEAT 100..143
FT /note="WD 2"
FT REPEAT 144..186
FT /note="WD 3"
FT REPEAT 189..228
FT /note="WD 4"
FT REPEAT 234..273
FT /note="WD 5"
FT REPEAT 320..359
FT /note="WD 6"
FT REPEAT 363..397
FT /note="WD 7"
FT REPEAT 438..475
FT /note="WD 8"
FT REPEAT 480..517
FT /note="WD 9"
FT REPEAT 521..561
FT /note="WD 10"
FT REPEAT 566..596
FT /note="WD 11"
FT MUTAGEN 125
FT /note="E->A: No effect on binding to cofilin or F-actin but
FT does not restore impaired chemotaxis or F-actin assembly in
FT cells lacking nhe1; when associated with A-167; A-181 and
FT A-193."
FT /evidence="ECO:0000269|PubMed:20668166"
FT MUTAGEN 167
FT /note="E->A: No effect on binding to cofilin or F-actin but
FT does not restore impaired chemotaxis or F-actin assembly in
FT cells lacking nhe1; when associated with A-125; A-181 and
FT A-193."
FT /evidence="ECO:0000269|PubMed:20668166"
FT MUTAGEN 181
FT /note="F->A: No effect on binding to cofilin or F-actin but
FT does not restore impaired chemotaxis or F-actin assembly in
FT cells lacking nhe1; when associated with A-125; A-167 and
FT A-193."
FT /evidence="ECO:0000269|PubMed:20668166"
FT MUTAGEN 193
FT /note="F->A: No effect on binding to cofilin or F-actin but
FT does not restore impaired chemotaxis or F-actin assembly in
FT cells lacking nhe1; when associated with A-125; A-167 and
FT A-181."
FT /evidence="ECO:0000269|PubMed:20668166"
FT CONFLICT 594
FT /note="N -> Y (in Ref. 1; AAB05588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 597 AA; 63976 MW; 5A192480263636B3 CRC64;
MSVTLKNIIA PTPATTRGKS VAINGDPKGE NIVYASGSSI IIRNVKNPMV ADIYYEHPCQ
TTVAKYAPSG NYIASGDVQG NLRIWDTLQK EHILKATYKV LNGAILDIAW TSDNQRLVVV
GDGKERFGAA ILWDSGSSCG EITGHSKMIL SCDIKSTRPF RAATGSEDFA VNWFEGPPFK
FQKNIAAGDF TRFVNCVRFS PDGNKLVTVG ADKKAFVYDG KTGEKLIELN PAQQHTGGIY
GCSWSADNNR VLTASADKSC KIWDTTTGQC INSFTFGSDV NDQQLGCLWF GDSLLSVNLA
GEISTLNLDD VAKPSRVIKG HNKLVGTIAF DKNAGSLYSA SYDASLLQWD LSTGLATNFT
GPAHKNQITS IKINGDQLIT CAMDDSVKIS SISKKTYGES IGVDSPAQAV AFSGDVVVAV
SMKTIYVIKG GKIVSQTAAT WEPTSVAIND TEVSVGGKDN KIHVFTLSGN NLTASHTLDN
HRGAITDLSY SPCGKYLASG CSNREVIVWS GKEAKSKGWV NHTARINAVA WSNDSKFVAS
ASLDSQIYIW NVENPTASPV QVKNSHLGGV NDVIYGSNNE IFSAGNEGAI KIWNVSN
