ID A0A8C1LFV5_CYPCA Unreviewed; 897 AA.
AC A0A8C1LFV5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Coronin {ECO:0000256|RuleBase:RU280818};
GN Name=LOC109103489 {ECO:0000313|Ensembl:ENSCCRP00010060292.1};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|Ensembl:ENSCCRP00010060292.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010060292.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010060292.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A8C1LFV5; -.
DR Ensembl; ENSCCRT00010066120.1; ENSCCRP00010060292.1; ENSCCRG00010023933.1.
DR Proteomes; UP000694427; Unplaced.
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:001013; 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; 1.
DR Pfam; PF00400; WD40; 4.
DR Pfam; PF16300; WD40_4; 2.
DR SMART; SM01166; DUF1899; 1.
DR SMART; SM01167; DUF1900; 2.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000694427};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280818};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 49..83
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 140..181
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 437..502
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 561..603
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 604..636
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 357..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..431
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 98014 MW; 8614F07C560A766D CRC64;
MPDQIKQQEK QSVLGFVCNR VCCVSGGGGM VGLTSVNAAS DGKWTVTQIS CHADLVTDLD
FSPFDDYLLA TCSADETVKL WRVCDPAQDQ CSDAEVTLSP ADGRLELVLF HPAASELLAV
ASVRGLQVWD VTRDTALTVL EQHEDQLQGL SWKEDGSLLA SSCKDKKLRL FDPRAQTSAV
QCVQGHQANR DSRILWVKDD NLLTTGFNQM RQQEVRLWDS RKLSSSLSSL SLATSNATLM
PLFDPDSGLL TVSGNGESVI DCFEVNSSEP FLSQVSHCLT DLSTRGTALV PKLALDVSCC
EVLRLLQLTD NFIVPISYQV PRKAGQDFHA DLYPDTVGHT PAMTAEDWWK GENKQVERVS
LHPSKRPKPA ATSAQETKPK DLPRGKSKEE ASTSSSPLST PSSSAAPSRS PSSTSGLSSG
FLPSPSPSQS SRAIQNMLGP SSKFRHIQGA VLHRDTHITN LRGLHLTTPG ECDGFCANGQ
RVAVPLAIAG GQIAVFELSQ PGKLPDTALP TIQNSVNVAD FCWDPFDTHK LVVAGDDAKI
RVWQIPKGGL TETLTEPECV LRGHTEKIYS IKFHPHASGL LASSSYDLTV RLWNLGTGEE
VKRLSGHQDQ IFGIAWSPDG KLLATVCKDG KVRLYDPRKS TLPIQEGPGP EGHRGARVVW
VCDGKYLLVS GFDSRSERQL YLFSAESLAS GSVASVPADV SPSTLIPFYD SDTSVLILTG
KGDTRVYTYE ILPEAPYFME CSSFHSSEPH KGLCFLPKTE CDVRDVEVAR AIRLGKSTIE
PVAFRVPRVK KEFFQDDVFP ETAVWWEASL TAAAWLSGSN GQHRKISLQP KDMMPVSEAP
KEVPVRKYLP SSVYLEEKTD EQKKEELLSA MVAKLGNRED PLPQASCEGV DEDEWDD
//
