DWWA_DICDI
ID DWWA_DICDI Reviewed; 568 AA.
AC Q54T86; Q86SB0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=WW domain-containing protein A;
GN Name=dwwA {ECO:0000312|EMBL:EAL66473.1}; ORFNames=DDB_G0281827;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC56858.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CALMODULIN,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX2 {ECO:0000269|PubMed:14595117};
RX PubMed=14595117; DOI=10.1091/mbc.e03-05-0329;
RA Nagasaki A., Uyeda T.Q.P.;
RT "DWWA, a novel protein containing two WW domains and an IQ motif, is
RT required for scission of the residual cytoplasmic bridge during cytokinesis
RT in Dictyostelium.";
RL Mol. Biol. Cell 15:435-446(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:EAL66473.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000269|PubMed:15875012};
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).
CC -!- FUNCTION: Involved in regulation of actin cytoskeleton organization and
CC cytokinesis. {ECO:0000269|PubMed:14595117}.
CC -!- SUBUNIT: Interacts with calmodulin in the absence of Ca(2+).
CC {ECO:0000269|PubMed:14595117}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14595117}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:14595117}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:14595117}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14595117}. Note=In living cells localizes to the
CC cell cortex and nucleus. In formaldehyde fixed cells localizes to the
CC nucleolus. {ECO:0000269|PubMed:14595117}.
CC -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth. Expression
CC decreases rapidly during early development and is not detected after 12
CC hours of development. {ECO:0000269|PubMed:14595117}.
CC -!- DISRUPTION PHENOTYPE: Cells fail to complete the final step of
CC cytokinesis and form multinucleated cells when grown on a solid
CC surface. Null mutants show excessive accumulation of F-actin around the
CC periphery of the ventral surface. When grown in suspension, mutants
CC lacking dwwA complete cytokinesis normally. Mutants lacking the N-
CC terminal C2 domain fail to localize to the cell cortex.
CC {ECO:0000269|PubMed:14595117}.
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DR EMBL; AB089315; BAC56858.1; -; mRNA.
DR EMBL; AAFI02000043; EAL66473.1; -; Genomic_DNA.
DR RefSeq; XP_640503.1; XM_635411.1.
DR AlphaFoldDB; Q54T86; -.
DR IntAct; Q54T86; 1.
DR STRING; 44689.DDB0216188; -.
DR PaxDb; Q54T86; -.
DR EnsemblProtists; EAL66473; EAL66473; DDB_G0281827.
DR GeneID; 8623318; -.
DR KEGG; ddi:DDB_G0281827; -.
DR dictyBase; DDB_G0281827; dwwA.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_480156_0_0_1; -.
DR InParanoid; Q54T86; -.
DR OMA; IENTICP; -.
DR PRO; PR:Q54T86; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..568
FT /note="WW domain-containing protein A"
FT /id="PRO_0000293628"
FT DOMAIN 6..129
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 325..359
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 519..552
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 376..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 209
FT /note="L -> S (in Ref. 1; BAC56858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 64751 MW; F297EBB82BD15C78 CRC64;
MSNKNPLNNS NGSNSSTIVN SDKFLVKIHS LSVSHTSKSS NIYLVGDFDQ FKQFKTETKK
SSSTHGSCIY NEFAMEFQYE TKYIHKLDHK HFKICVYKKK SIGSDKYIGS FGVDLYTLAT
GPISHDVVFQ KDNTGVGRLQ FRLEMNHITD IQISFKSILL SNLMKQSNYQ IDYSLNKINP
LKSSIIENTI CPSWYNQSSI LMNISLKDLV DGSIFFNLKD TKSSKVIGEL KLPVKSIFSF
VEGDIKIVKT LLYNEKQNKI CDACIEIQFN NIPQLAQLRG GIQTEQGIRG AESFFSGVPL
PKIIGEISNA STSDGYSKEA QLQHVKLPDG WESRIDPVSG KVFYLNHNNK TTSWISPLEH
APVKKRTPTV VISNTTILDN NNNNNNNNNN NNNNNNNNNN NINNTNNIQQ KQQAQQQPVQ
PPPQPVQQQV QQPQQKEKEK EKEINAEDYK ISRPKKTPAT PEEAAVIIQR TFRNHKKQSY
NKTIRNSKTI IPPNNVQQQQ PQQTEKPSIY QVFGQQIDQG LPNGWEVRQD QFGRVFYVDH
INRATTWTRP TVKHPKQHQQ ATLVQQRK
