ID A7RFP3_NEMVE Unreviewed; 932 AA.
AC A7RFP3;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Coronin {ECO:0000256|RuleBase:RU280818};
GN ORFNames=NEMVEDRAFT_v1g157985 {ECO:0000313|EMBL:EDO49756.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO49756.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO49756.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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; DS469508; EDO49756.1; -; Genomic_DNA.
DR RefSeq; XP_001641819.1; XM_001641769.1.
DR AlphaFoldDB; A7RFP3; -.
DR STRING; 45351.A7RFP3; -.
DR EnsemblMetazoa; EDO49756; EDO49756; NEMVEDRAFT_v1g157985.
DR eggNOG; KOG1445; Eukaryota.
DR HOGENOM; CLU_006604_0_0_1; -.
DR InParanoid; A7RFP3; -.
DR OMA; TIMYMEV; -.
DR PhylomeDB; A7RFP3; -.
DR Proteomes; UP000001593; 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; 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; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
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 3..65
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 73..115
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 124..165
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 166..207
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 470..535
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 594..636
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 637..669
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 424..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 103884 MW; 1D1214D36D9EBE03 CRC64;
MNRFKTSKFH NAAAKSPKRE NCYNDINVGS LKMSCGNHLK ASTSFIAFNV DKGGCLGIIP
LSDIGRRATT PLLHVHSDFV TDMDFSPFDD GLLATCSYDC SIKIWQIPES GVAQNHSLTP
LSAFPLHSSR VENVLFHPTA EEVLASSCSS TVSVWDVSQN KVKFSLDSHK DAVQSLSWKE
DGSLLVTSCK DKTIRIFDPR KSSCTVETLG FAGIKDSRVI WRSDKGHIIG TGFSSSRERQ
VAIWDIHNMK EPLQRIGLDT NTGTLMPFHD ADSDMLLIAG KGDTSVLYFE IKDSGSEYLK
QASVHMTEDQ HKGMGMVPKL ALDVMSCEVV RLLQLTKNSV VPISYLVPRK NLKDFNADLY
PDTLGPEPAI TAERWFQGNK ALVRKYYINS GYLRVWFICH SKRHFNVCLH RHLQPNIETP
KPTIWSASSS SSNIQKDATT NSTNQHPASS QSSNQEPVSD TNVETWKSFS GVRSSKFRHI
IGVPMHKSTN IENIRNLSMS TFGECDGLQL NKEFVAYPLS GPGGQIAVLP HNKPCRLPDS
GMPVVQCGST VMDFVFDPLD VNRMAVACET GVISIWNLPS GGLTEILDEP VEELKGHYDK
PNIVRYHPNA ENLLTSAAYD LTVKLWDINA AKSVITLEGH NEQVFSLAWS ADGKQLATFS
RDKKLRIYDP RAQVTPVLEG PGPEGSRGGR VIWGGPDGNM LLVCGSDKMS HRTVSVYDSG
NLSEPLSVSE INIAPSILIP FYDEDANVIM LSGKGDTVLY AYEVSNEHPY LFDLTHYRVT
DPFQAIAFFD KRVCDVKKVE FARAIKLTKT NLEKIMFQVP RIKKEYFQDD LFPETRAKWE
AAVACEEWLA GQDGEQSRIS LRPPNMKPLS EAPKAPPASK KYDSTKELDD FKSDERRKEE
LVTAMVEKLG TYDEDPLPQD LMEGVDDDEW DD
//
