ID A0A6P7FG70_DIAVI Unreviewed; 1243 AA.
AC A0A6P7FG70;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Coronin {ECO:0000256|RuleBase:RU280818};
GN Name=LOC114329962 {ECO:0000313|RefSeq:XP_028135049.1,
GN ECO:0000313|RefSeq:XP_028135050.1};
OS Diabrotica virgifera virgifera (western corn rootworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Galerucinae; Diabroticina; Diabroticites;
OC Diabrotica.
OX NCBI_TaxID=50390 {ECO:0000313|RefSeq:XP_028135049.1};
RN [1] {ECO:0000313|RefSeq:XP_028135049.1, ECO:0000313|RefSeq:XP_028135050.1}
RP IDENTIFICATION.
RC TISSUE=Whole insect {ECO:0000313|RefSeq:XP_028135049.1,
RC ECO:0000313|RefSeq:XP_028135050.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
CC -!- FUNCTION: F-actin regulator involved in anterograde Golgi to endosome
CC transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by
CC the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and
CC localizes to the trans-Golgi network, where it promotes actin
CC polymerization, thereby facilitating post-Golgi trafficking. May play a
CC role in the maintenance of the Golgi apparatus morphology.
CC {ECO:0000256|ARBA:ARBA00024838}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC {ECO:0000256|ARBA:ARBA00009482, ECO:0000256|RuleBase:RU280818}.
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DR RefSeq; XP_028135049.1; XM_028279248.1.
DR RefSeq; XP_028135050.1; XM_028279249.1.
DR AlphaFoldDB; A0A6P7FG70; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProtKB-ARBA.
DR FunFam; 2.130.10.10:FF:000076; Coronin; 1.
DR FunFam; 2.130.10.10:FF:000362; Coronin; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR10856; CORONIN; 1.
DR PANTHER; PTHR10856:SF20; CORONIN-7; 1.
DR Pfam; PF08953; DUF1899; 2.
DR Pfam; PF00400; WD40; 5.
DR Pfam; PF16300; WD40_4; 2.
DR SMART; SM01166; DUF1899; 2.
DR SMART; SM01167; DUF1900; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280818};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 4..66
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 75..109
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 769..834
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 893..929
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 936..977
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 483..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 444..481
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 537..550
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1243 AA; 138195 MW; 0FEBABCE00F04B0B CRC64;
MAWRFKASKY KNAAPIVPKP ENYVRDISVG SYQTYGNNIA ASAKFMAFNW DHAGSSLAVL
PLDDYGRKGK LMPLLHAHSD TVTDISFSPF HDGLLATGSQ DCLVKIWHIP KEGLQESLSN
PESTFSHKQR RVEIVGFHPT ADFLLHSTSF TTLTLWDLMT EQEIFSNSDP SEVIQSVSWK
RDGTLLATSA KDKQVRILDP RAENCCVQSA NSHPGIKDSK VVWLGDQNKI LTTGFDAQRL
RQVIIRDLRN IVEPEKTLEL DCSTGILIPL YDADTGMLFL AGKGDTTILY MEVTDKDPHL
IEGIRHSGEQ TKGVCLVPKR ALNIMQGEVN RILQLTSSSV VPVTYQVPRK TYRDFHADIY
PDTPGYKTDL VSSDWFQGTN IPLQKMSLDP AKREHGEEPI VIHRGTLQEM REEYNNKKIT
AKPEPKAKPA PAQKIEHHPV KGIIKDFEKD NKQIEASNKQ IEASNKLIEA SNKLIEEEKN
NINMKSTEDD GDKIPSIIPP KPLPRTSRTS SMCDSQPAED ANSAPKPVAR PRTNSCVPVV
TSVSPVAPVS GGYKPRLGPK PFTPPNLADT ENTFSKVFSV PAVPGQTTTS LSQEKDKSPT
VEEVPEKTEA VNGKSEENHT KSDVGNGKSA SSGEEEASSD SGYVPRTPST AERRKLFETK
PNSKENNTEE LDSVDFERGS LQRASIAERR KMYESRSISV QEQGLEKKEN SPVMMRRKDS
FKNRKNAEDV LKDDNNRKSM PIAKQQSLDP VGVRKSEVSM PTPKRTSTVF GRVSKFRHLK
GTPLHKSFHI ENIRNLSRQI PGECDGFQAN PERVAVPLSG PGGKIAIFEL SKTGKLPDGV
IPALVHGNSV MDFTWDPFDT KRLAVACDDG VVKLWRIPDN GLTEQTNEAE AEFCAHSDKI
YFIKFHPTAK DVLASGSYDM TIKLWDLSTL TEKIVLKGHT DQIFSFAWSP CGSFCATVSK
DSKIRIYKPR SNDSPIREGK GPEGNRGARI TWALDGHFIV ATGFDKVSER QITAYKANDL
SNPLNTVGLD VSPAILIPFY DDDSSTLFVT GKGDSTIYAF EITEEHPFIC PLSHHRCPTL
HQGLSFLSKN VCDVSNVEFA KALRLTNNSI EPLSFTVPRI KTDLFQDDLF PPTRVTWNPT
MSSSEWFSGK EKPPQKISLQ PEGMELLSES QGQPNSATER TINKSASSPF IGINHGRVGW
DVDASDVKNK QDEIKRSVSN KLQVNKTLEQ DAMEGVDEKE WLE
//
