DNAI3_MACFA
ID DNAI3_MACFA Reviewed; 891 AA.
AC Q95JP0; Q95LV8;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Dynein axonemal intermediate chain 3;
DE AltName: Full=WD repeat-containing protein 63;
GN Name=DNAI3; Synonyms=WDR63; ORFNames=QtsA-1482, QtsA-17302;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Hashimoto K., Osada N., Hida M., Kusuda J., Tanuma R., Hirai M., Terao K.,
RA Sugano S.;
RT "Isolation of novel full-length cDNA clones from macaque testis cDNA
RT libraries.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a negative regulator of cell migration, invasion, and
CC metastasis downstream of p53/TP53, through inhibition of Arp2/3
CC complex-mediated actin polymerization (By similarity). Via its
CC association with the multisubunit axonemal dynein complex, is
CC potentially involved in the regulation of cilia function. May play a
CC role in osteogenesis of dental tissue-derived mesenchymal stem cells
CC (By similarity). {ECO:0000250|UniProtKB:B2RY71,
CC ECO:0000250|UniProtKB:Q8IWG1}.
CC -!- SUBUNIT: Interacts with ACTR2; this interaction reduces binding of the
CC Arp2/3 complex to the VCA domain of nucleation promoting factors (By
CC similarity). Part of the multisubunit axonemal dynein complex formed at
CC least of two heavy chains and a number of intermediate and light
CC chains. Found in a associated with the catalytic heavy chain DNAH2, the
CC intermediate chain DNAI4, and the light chain DYNLT1 (By similarity).
CC {ECO:0000250|UniProtKB:B2RY71, ECO:0000250|UniProtKB:Q8IWG1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IWG1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q95JP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95JP0-2; Sequence=VSP_018081;
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DR EMBL; AB070141; BAB63086.1; -; mRNA.
DR EMBL; AB071082; BAB64476.1; -; mRNA.
DR AlphaFoldDB; Q95JP0; -.
DR STRING; 9541.XP_005542923.1; -.
DR eggNOG; KOG1587; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005858; C:axonemal dynein complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0071933; F:Arp2/3 complex binding; ISS:UniProtKB.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
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 SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Cytoplasm; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..891
FT /note="Dynein axonemal intermediate chain 3"
FT /id="PRO_0000233163"
FT REPEAT 395..435
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 477..533
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 670..709
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 713..753
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 817..861
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..392
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_018081"
FT CONFLICT 798
FT /note="H -> R (in Ref. 2; BAB64476)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="A -> T (in Ref. 2; BAB64476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 891 AA; 102832 MW; 9616F1C6A9160D9C CRC64;
MAPKQKKKSS RRKKSPKPIL AASEDMEPVN MESMGHPEIY PLVLTTKTQE IFNCRIDEDI
TDEQPYKLIN KEDIFEDLRN RAAVSDFHPV KKIVQEYPGN ELLLVYDKDF KYGLNFYLIG
TEEGEENYLN PPEVSEEQEE YKEYIPEDVY IYKPPVSKPW VSLGSEKEIE EESVTESTKQ
ITYMISRKRS EFGAPIKFSD QNASSVKDAY IECTAYPDKN FTLKQLEKDV GMQVIPQIKD
ISTQTKWTYP KNATTQYYPR EFSEEEKETL KQSKPLVDFL NNASISVEIA LQQNEITNTF
IDDWKHLAEE EGTFGDKTDT HLKEYQSFTD LHSPTEKMIT CVSWHPTIYG LIAVSVAVRL
SFEDRVHFSG KLLLQPSLIL FWSFSDPIHP QLMLESPDDI FCFKFCPSDP NIIAGGCING
QIVMWDITAH ADRIENIKGG GSRSKKATLK PMFLLEPESN KEAMYIRHCA VSSIENGHKR
VITDIHWLSD TFEINRMGSV FENRSGICCQ LVTCSADCTI CFWDIRPQKP LTPQTTEKKK
EESIEIPFDV PSTFLHLDLS WKPLTKLKLS KGETSLDHCP TKISLNEDHL LCKTQDKMLA
QSKTAKAEEM NPYHNLESGV ANLLKPIDDF CTKFFVGTEE GEVIYTDWKM ERDPETGRFM
PKKPVNLHTI HDGIVHTIQR SPFYDDIILT VGGWNVAIWK ESVMTGPLLQ SCCAPKRYTS
GHWSLTRPGV FYIGREDGYI DIWDLLEKTH EPAQSQNICI TMITCIKPWI FSPKQQFIAI
ADYYGTLHIL EIPWTLSHPS ANEMASINHY FEREVKHLEY VEQRKKIREQ EKKEMEQEMA
KKKVKIYQKS KEQMEAELKM DYESYLELEK TVLINLGLIK VTEKGSYLDV M
