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Database: UniProt
Entry: F6YNT4_CIOIN
LinkDB: F6YNT4_CIOIN
Original site: F6YNT4_CIOIN 
ID   F6YNT4_CIOIN            Unreviewed;       925 AA.
AC   F6YNT4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Coronin {ECO:0000256|RuleBase:RU280818};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000009121.3, ECO:0000313|Proteomes:UP000008144};
RN   [1] {ECO:0000313|Proteomes:UP000008144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12481130; DOI=10.1126/science.1080049;
RA   Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA   Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA   Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA   Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA   Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA   Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA   Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA   Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA   Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA   Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA   Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA   Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA   Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA   Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA   Satoh N., Rokhsar D.S.;
RT   "The draft genome of Ciona intestinalis: insights into chordate and
RT   vertebrate origins.";
RL   Science 298:2157-2167(2002).
RN   [2] {ECO:0000313|Ensembl:ENSCINP00000009121.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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   -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC       {ECO:0000256|ARBA:ARBA00009482, ECO:0000256|RuleBase:RU280818}.
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DR   EMBL; EAAA01001482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; EAAA01001483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F6YNT4; -.
DR   STRING; 7719.ENSCINP00000009121; -.
DR   Ensembl; ENSCINT00000009121.3; ENSCINP00000009121.3; ENSCING00000004409.3.
DR   GeneTree; ENSGT00940000156606; -.
DR   HOGENOM; CLU_006604_0_0_1; -.
DR   InParanoid; F6YNT4; -.
DR   OMA; TIMYMEV; -.
DR   TreeFam; TF314280; -.
DR   Proteomes; UP000008144; Chromosome 2.
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; IPR020472; G-protein_beta_WD-40_rep.
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; 3.
DR   Pfam; PF16300; WD40_4; 2.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM01166; DUF1899; 2.
DR   SMART; SM01167; DUF1900; 2.
DR   SMART; SM00320; WD40; 5.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008144};
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..66
FT                   /note="DUF1899"
FT                   /evidence="ECO:0000259|SMART:SM01166"
FT   REPEAT          74..116
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          467..532
FT                   /note="DUF1899"
FT                   /evidence="ECO:0000259|SMART:SM01166"
FT   REPEAT          591..633
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          634..675
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          378..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   925 AA;  101278 MW;  380E3C0F02413BF4 CRC64;
     MHRFKSSKYK NGVAKVPKKE LCITDVSVEA PVSYGNHVSC GAKFFVCNLG GAGGGKLGVF
     GVDDCGRKGQ HPMLAAHAGI ITDIEFSPFY HDTFLSASDD STVKIWKIPD SGVMNSGSYS
     PASVFKGFKK RPEVLQHHPV AESLCALATG GEIKLLNMKQ EDVALNCEVC SDTLQSIAWS
     YDGKTIAATS KNKKLFIADP RVGQQVVETA AHGNHKDSRV ICLGDSEKFA TTGFTTSRSR
     ELKAWDPRNL TSCLQTIEFG TSTGVLMPFY DADAKLIFLA GKGDSSLSIL EVVDGTELIS
     QASQTMLPDQ SKGMGILPKL AVDVMSCEVD RLMQLCARQI VPVKIEVPRK SHRDFISELY
     PDTDSDEIVL TAENWLSGTN GQRTKTSLDP STRKSLRVSQ NAPTVAAPAA PAEPTEPVEP
     VEPAESAAQA APAAEVVKNT TPTDTKKVAS SSPPPPSESK LPAPEKKVEV HSKFRHWTGT
     VLHPTTHITN IPKLNTSLSG SCDGFHINTE RVAFPLSTPG GHVAIWELSK IGRLPSSDPP
     SLQNTAAVTD MRWDPFNSHR IAVGLENGKI KVWEIPEGGL KEVVSEESFS LSGHYNKVIC
     VRFHPLASGI LASASSDSTI KIWDLESQEN CITLTGHEDE ILNISWSSDG KYIASMCKDN
     KIRIYDPRSS TEPIKVATGS EGSSRGGRIV WACSDQLLIS SGFKSGAREI AVYDVTDMDR
     GQVESQDLGG SPSTLIPHYD EDSSTLFVTG KGDTTMHSFE VSPTEPHLHQ LNTFTSDKMH
     QGFLFLPKTT CDPRKVEFAR AWRLSKTTLV PISFKVPRIK MEYFQDDLFP ETRDLRKPTM
     TSQQWLDGKN VQASKISVCP KDMKPLSEAP KEAPKARKYE SYDPSTYKTD EEKKEELLAA
     MSNRLDLDKE LEQDTMEGVD EDEWD
//
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