ID   CORT_HELME              Reviewed;         447 AA.
AC   P0DOB8;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-SEP-2016, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Protein cortex {ECO:0000250|UniProtKB:Q960N3};
GN   Name=cort {ECO:0000250|UniProtKB:Q960N3};
OS   Heliconius melpomene (Postman butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Heliconiinae; Heliconiini; Heliconius.
OX   NCBI_TaxID=34740;
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; P0DOB8; -.
DR   SMR; P0DOB8; -.
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..447
FT                   /note="Protein cortex"
FT                   /id="PRO_0000437218"
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          281..325
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          344..380
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          384..423
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   MOTIF           384..395
FT                   /note="D-box"
FT                   /evidence="ECO:0000250|UniProtKB:Q960N3"
SQ   SEQUENCE   447 AA;  51096 MW;  E8F468DAC1B04593 CRC64;
     MDRRTFDRKT NNPQRYRLDR FVATRDSFSE TRRRRSWHAA FDVHPVNNDR WSEGNLKKKN
     YIKYLDKAFD LESPDKNKSI KRMNRLWPCI PRKKTYLSSA DSILDLPTYS YAIYPELLDW
     SNDNMLVAAL GSSYHKWSWR SQSLIGHGFA EYEIQCCKFD PRGELLALGT YMKTLEIHNN
     SKSKKIMSNT CKCLEIDNMN CSITAVDWSP TGNSFAAGCS GGAVTSFTRA AKLISWRHLV
     REAILLIRVS PNARYLAVTA MNTALVLLLS WPSLEMYSSI DSDWSIRAIC WHPWRSALLG
     VGAVTDDLQA RIALWNAPTR EVRDTSIGPK GYRLDSMLFS HRTGELVLSM WHSDRATLHP
     KTCSQLVVLS DPDTMVDQWG EGRSGLDRVR TMIFSPDGTK LATATTDEDL IIWNFLPEDN
     KMKKTKCRSF SALPECLDNA MLGYSLR