ID A0A151WWT7_9HYME Unreviewed; 1178 AA.
AC A0A151WWT7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Coronin {ECO:0000256|RuleBase:RU280818};
GN ORFNames=ALC60_08553 {ECO:0000313|EMBL:KYQ52340.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ52340.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ52340.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ52340.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ52340.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC {ECO:0000256|RuleBase:RU280818}.
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DR EMBL; KQ982685; KYQ52340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151WWT7; -.
DR STRING; 64791.A0A151WWT7; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR024977; Apc4-like_WD40_dom.
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; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF08953; DUF1899; 2.
DR Pfam; PF00400; WD40; 4.
DR Pfam; PF16300; WD40_4; 2.
DR SMART; SM01166; DUF1899; 2.
DR SMART; SM01167; DUF1900; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF101908; Putative isomerase YbhE; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
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..117
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 167..208
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 691..755
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 764..798
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 814..856
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 862..903
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 475..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1178 AA; 131022 MW; 5113DEDEC71074DB CRC64;
MAWRFKASKY KNAAPIVPKP EACIRDISVG SYQTYGNNIT ASAAFMAFNV DHNGSSLAVL
PLEDCGRKSK TMPLLHAHAD TVTDMDFSPF HDGLLATGSQ DCLVKLWHIP ESGLEESLCN
PECTFSHRQR RVEAVCWHPS AEHLLTTASF TNLSLWDVLS QQELFSNSDH TEVIQSVSWK
EDGTVLATSC KDKQLRLIDP RASTCIVNSC SSHQSIKDSR TVWLNNDRIL TTGFDAARLR
QVYIRDLRHL NEPMKTLELD CSTGILMPLF DSDTNMLFLA GKGDTTIIYM EVTERDPYLV
EGIRHSGEQT KGVCLIPKRA LNVMQAEVNR LLQLTSNMVI PIMYQVPRKT YRDFHADIYP
DTTGPVAQNN ATSWFKGHNA PVPKISLDPA KRNKGQEPII VHKGNLAVLK DNQREIKVEQ
MNRSAKPLVI TAPKGFSKVQ SNVTTMNELQ RENDINIEKN DNNINTDKIE DLKKPSEAEE
EKLKIQNGGQ TVPPKPLPRA SRTNSISEEE PKPVARPRTS PNPGSVVTSV NPNAIGGYKP
RLGPKPFQAK SSSQEFSFDK VFSVPLAPNN DSNTNGYQNE INNTAEHNAE ADKSPTLTPN
ERAKDMENGK SDSSSIEEDA NSSDSGYKPK TPSTAERRKV FETKVKDESP ENEDVGNFER
GTNRNSIAER RRLYESRSVS VTDGNLAEKA MGRVSKFRHL KGTPGHKSTH IENIRNISRQ
ISGECDGFHA NPDRVAVPLS GPGGKIAVLE LKKTGRLPDG VMPALVHGAT VMDFQWDPFD
NQRLAVACDD GIIRLWEIPE SGLAEPTNEP KYIIEAHTDK IYLIKFHSLA LNVLASASYD
MTVKIWDLSL LSSTETNAKI TLIGHTDQIF SLAWSPCGQY LASTCKDGKL RIYKPRSSDV
PVKEGKGPVG TRGARVIWAL EGRYLVVMGF DKVSERQIYV FKVDNLNTPL NTVGLDVSPA
ILMPYYDEDS STLFLTGRGD STIYAFEVTE EAPHCCPLSH HRCSSLHQGL SFLPKNKCDV
ASVEFASALR LTNNTIEPLS FTVPRIKSEL FQDDLFPPTK VIWKPTLSAS EWFSGGNKQP
SRMCLKPPGM DNLTENQSQN AVTPPQIATK PSPTPFGITT QSYNRLGWNP DVKAKQEEIQ
KTMSHFVGDV IQCSLEQDHM EGVEEHEWVS RCFICCKS
//
