ID   CORT_HELEA              Reviewed;         449 AA.
AC   P0DOB9;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Protein cortex {ECO:0000250|UniProtKB:Q960N3};
GN   Name=cort {ECO:0000250|UniProtKB:Q960N3};
OS   Heliconius erato (Crimson patched longwing butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Heliconiinae; Heliconiini; Heliconius.
OX   NCBI_TaxID=33431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND POLYMORPHISM.
RX   PubMed=27251285; DOI=10.1038/nature17961;
RA   Nadeau N.J., Pardo-Diaz C., Whibley A., Supple M.A., Saenko S.V.,
RA   Wallbank R.W., Wu G.C., Maroja L., Ferguson L., Hanly J.J., Hines H.,
RA   Salazar C., Merrill R.M., Dowling A.J., ffrench-Constant R.H., Llaurens V.,
RA   Joron M., McMillan W.O., Jiggins C.D.;
RT   "The gene cortex controls mimicry and crypsis in butterflies and moths.";
RL   Nature 534:106-110(2016).
CC   -!- FUNCTION: Controls wing pigmentation patterning by regulating scale
CC       cell development, thereby playing a key role in mimicry and crypsis
CC       (PubMed:27251285). Probably acts as an activator of the anaphase
CC       promoting complex/cyclosome (APC/C) that promotes the ubiquitin ligase
CC       activity and substrate specificity of the APC/C (By similarity).
CC       {ECO:0000250|UniProtKB:Q960N3, ECO:0000269|PubMed:27251285}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q960N3}.
CC   -!- POLYMORPHISM: Variations in cort gene cortex directly affect wing
CC       pigmentation patterning. Variations affecting cort expression have
CC       become a major target for natural selection acting on color and pattern
CC       variation in lepidoptera. {ECO:0000269|PubMed:27251285}.
CC   -!- SIMILARITY: Belongs to the WD repeat CORT family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DOB9; -.
DR   SMR; P0DOB9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0010997; F:anaphase-promoting complex binding; IEA:InterPro.
DR   GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:InterPro.
DR   GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IEA:InterPro.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR033010; Cdc20/Fizzy.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR19918; PTHR19918; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Repeat; WD repeat.
FT   CHAIN           1..449
FT                   /note="Protein cortex"
FT                   /id="PRO_0000437219"
FT   REPEAT          108..148
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          149..188
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          198..237
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          283..327
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          345..382
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          386..425
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   MOTIF           386..397
FT                   /note="D-box"
FT                   /evidence="ECO:0000250|UniProtKB:Q960N3"
SQ   SEQUENCE   449 AA;  51448 MW;  28520AF325EE3581 CRC64;
     MDRTTFGRKT FNTQRNRLDR FVAPRDSFSE TRRRRSWHAA CDVQPINNDI WFGKNLKKKK
     YTKYLDKALD LESPDKSNSI KRMVQPWPCI PRKKTYLSSA DSILDLPTYS YAIFPELLDW
     SNDNVLVAAL GRNYHKWSWR SQSLISQGYA EYQIQCCKFD PRGELLLLGT YMKTVEIHNN
     VKSKKIDSNT CNCLEKDNRN CSITAVDWSP TGNSFATGCS WGAVTSFTRA AKLISWRHFV
     REAILLILIA LSPNARYLAV TAVNTALVLL LTWPSLEMYS SIDSDWTIRT ISWHPWRSAL
     LGVGAVTDDL QARIALWDAP TCKVRDTSIG PKRYRLDAML FSHRTGELVL SMWNSDRAIL
     HPKACSQLVV MSDPDTMVDQ WGEGRSGLDR VRTMVFSPDG TKLATATSDE DLIIWNFLPE
     DKKMKKTKCR FFSALPEYLD EAMQGYSLR