CORT_BISBE
ID CORT_BISBE Reviewed; 441 AA.
AC P0DOC0;
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 Biston betularia (Pepper-and-salt geometer moth) (Phalaena betularia).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC Geometridae; Ennominae; Biston.
OX NCBI_TaxID=82595;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A1; A2; A3; A4; A5; B1; B3 AND B4),
RP FUNCTION, DEVELOPMENTAL STAGE, AND POLYMORPHISM.
RC STRAIN=f. carbonaria, and f. typica;
RX PubMed=27251284; DOI=10.1038/nature17951;
RA Van't Hof A.E., Campagne P., Rigden D.J., Yung C.J., Lingley J.,
RA Quail M.A., Hall N., Darby A.C., Saccheri I.J.;
RT "The industrial melanism mutation in British peppered moths is a
RT transposable element.";
RL Nature 534:102-105(2016).
CC -!- FUNCTION: Controls wing pigmentation patterning, possibly by regulating
CC scale cell development (PubMed:27251284). Probably acts as an activator
CC of the anaphase promoting complex/cyclosome (APC/C) that promotes the
CC ubiquitin ligase activity and substrate specificity of the APC/C (By
CC similarity). {ECO:0000250|UniProtKB:Q960N3,
CC ECO:0000269|PubMed:27251284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q960N3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=A1 {ECO:0000303|PubMed:27251284};
CC IsoId=P0DOC0-1; Sequence=Displayed;
CC Name=A2 {ECO:0000303|PubMed:27251284}; Synonyms=A6
CC {ECO:0000303|PubMed:27251284}, B2 {ECO:0000303|PubMed:27251284}, B5
CC {ECO:0000303|PubMed:27251284}, B6 {ECO:0000303|PubMed:27251284};
CC IsoId=P0DOC0-2; Sequence=VSP_058498;
CC Name=A3 {ECO:0000303|PubMed:27251284};
CC IsoId=P0DOC0-3; Sequence=VSP_058502;
CC Name=A4 {ECO:0000303|PubMed:27251284};
CC IsoId=P0DOC0-4; Sequence=VSP_058500;
CC Name=A5 {ECO:0000303|PubMed:27251284};
CC IsoId=P0DOC0-5; Sequence=VSP_058501;
CC Name=B1 {ECO:0000303|PubMed:27251284};
CC IsoId=P0DOC0-7; Sequence=VSP_058499;
CC Name=B3 {ECO:0000303|PubMed:27251284};
CC IsoId=P0DOC0-9; Sequence=VSP_058499, VSP_058502;
CC Name=B4 {ECO:0000303|PubMed:27251284};
CC IsoId=P0DOC0-10; Sequence=VSP_058497;
CC -!- DEVELOPMENTAL STAGE: Highly expressed between the sixth larval instar
CC (La6) and day 4 prepupa (Cr4), coinciding with a phase of rapid wing
CC disk morphogenesis. Expression drops to a low level by day 6 prepupa
CC (Cr6). {ECO:0000269|PubMed:27251284}.
CC -!- POLYMORPHISM: Variations in cort gene cortex directly affect wing
CC pigmentation patterning and are the cause of the darkening of the wing
CC in the f. carbonaria strain. This phenomenon, known as industrial
CC melanism, is a classroom example of evolution: during industrial
CC revolution, the common pale B.betularia strain (f. typica) was replaced
CC by a previously unknown black strain (f. carbonaria), driven by the
CC interaction between bird predation and coal pollution. The variation is
CC caused by insertion of a transposable element into the first intron of
CC cort gene, which occured around 1819, in the early years of the
CC industrial revolution. {ECO:0000269|PubMed:27251284}.
CC -!- SIMILARITY: Belongs to the WD repeat CORT family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=You want it darker - Issue
CC 183 of September 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/183/";
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DR EMBL; KT235895; ANG83466.1; -; mRNA.
DR EMBL; KT235896; ANG83467.1; -; mRNA.
DR EMBL; KT235897; ANG83468.1; -; mRNA.
DR EMBL; KT235898; ANG83469.1; -; mRNA.
DR EMBL; KT235899; ANG83470.1; -; mRNA.
DR EMBL; KT235900; ANG83471.1; -; mRNA.
DR EMBL; KT235901; ANG83472.1; -; mRNA.
DR EMBL; KT235902; ANG83473.1; -; mRNA.
DR EMBL; KT235903; ANG83474.1; -; mRNA.
DR EMBL; KT235904; ANG83475.1; -; mRNA.
DR EMBL; KT235905; ANG83476.1; -; mRNA.
DR EMBL; KT235906; ANG83477.1; -; mRNA.
DR AlphaFoldDB; P0DOC0; -.
DR SMR; P0DOC0; -.
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 Pfam; PF00400; WD40; 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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Repeat; WD repeat.
FT CHAIN 1..441
FT /note="Protein cortex"
FT /id="PRO_0000437220"
FT REPEAT 110..148
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 149..187
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 193..233
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 235..276
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 277..320
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 345..379
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 380..420
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT MOTIF 379..390
FT /note="D-box"
FT /evidence="ECO:0000250|UniProtKB:Q960N3"
FT VAR_SEQ 1..171
FT /note="Missing (in isoform B4)"
FT /evidence="ECO:0000305|PubMed:27251284"
FT /id="VSP_058497"
FT VAR_SEQ 1..150
FT /note="Missing (in isoform A2)"
FT /evidence="ECO:0000305|PubMed:27251284"
FT /id="VSP_058498"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform B1 and isoform B3)"
FT /evidence="ECO:0000305|PubMed:27251284"
FT /id="VSP_058499"
FT VAR_SEQ 11..167
FT /note="Missing (in isoform A4)"
FT /evidence="ECO:0000305|PubMed:27251284"
FT /id="VSP_058500"
FT VAR_SEQ 11..49
FT /note="Missing (in isoform A5)"
FT /evidence="ECO:0000305|PubMed:27251284"
FT /id="VSP_058501"
FT VAR_SEQ 50..167
FT /note="Missing (in isoform A3 and isoform B3)"
FT /evidence="ECO:0000305|PubMed:27251284"
FT /id="VSP_058502"
SQ SEQUENCE 441 AA; 50902 MW; CBB41D1010BE6C7A CRC64;
MGVGSSLRMQ LTAQKPRVDR FVVPRYSLPE IHRRMTWSDR CEKYNGEIWS SKYLQQKRYI
NFLDEAFGLA PLKAQQRNSD TFDDWCWPCA PRKKSYLSTA DNVLDLPSYS ITSFPDVLDW
SHDDILVAAL GKKYHKWSWR TQSPVDQGQT MFDIRCCKFD PKGKRLLLGT DMRVEVHNEL
SKCQFVQYCK CNIQICTITA IDWSPTGNSF VTGCSRGRIC AMNEKDFPIK SLVLIEGAML
VVKISPNARY VAVAGVHKHR VWILSWPDLI RFRFMKTNEI VKDLNWHPWQ TALLGVATLS
SDRHASMIIW EPHATDKLRQ QDVGRGRYSI DAMRFNNKTG ELLLSLWSLD VNVPYPKSSE
LVVMSNFDTV VDHWGESHTG LNRIRTMVFS PDGTKLATAT ADEDLIIWNF LPNDYKKILA
RKKFTAFPQF LDICSYGYTI R
