ID   CORO7_BOVIN             Reviewed;         915 AA.
AC   Q0V8F1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Coronin-7;
DE            Short=Crn7;
GN   Name=CORO7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with clathrin adapter AP1 complex. This interaction
CC       takes place at Golgi membranes and not AP1-positive endosomal
CC       membranes. Interacts (when ubiquitinated at Lys-463) with EPS15 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}. Golgi
CC       apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle
CC       {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Predominantly
CC       cytosolic. Detected on vesicle-like cytoplasmic structures and on the
CC       cis-Golgi. Not associated with actin filaments (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: The membrane-associated form is phosphorylated on tyrosine
CC       residues. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated via 'Lys-33'-linked ubiquitin chains by the
CC       BCR(KLHL20) E3 ubiquitin ligase complex: 'Lys-33'-linked ubiquitination
CC       promotes interaction with EPS15 and facilitates actin polymerization at
CC       the trans-Golgi network, thereby facilitating post-Golgi trafficking.
CC       Deubiquitinated by ZRANB1/TRABID (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR   EMBL; BT026268; ABG67107.1; -; mRNA.
DR   RefSeq; NP_001069371.1; NM_001075903.1.
DR   AlphaFoldDB; Q0V8F1; -.
DR   SMR; Q0V8F1; -.
DR   STRING; 9913.ENSBTAP00000012121; -.
DR   PaxDb; Q0V8F1; -.
DR   PeptideAtlas; Q0V8F1; -.
DR   PRIDE; Q0V8F1; -.
DR   GeneID; 527934; -.
DR   KEGG; bta:527934; -.
DR   CTD; 79585; -.
DR   eggNOG; KOG1445; Eukaryota.
DR   InParanoid; Q0V8F1; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR   GO; GO:0006895; P:Golgi to endosome transport; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR027331; CORO7.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   PANTHER; PTHR10856; PTHR10856; 1.
DR   PANTHER; PTHR10856:SF20; PTHR10856:SF20; 1.
DR   Pfam; PF08953; DUF1899; 2.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM01166; DUF1899; 2.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW   Isopeptide bond; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Repeat; Transport; Ubl conjugation; WD repeat.
FT   CHAIN           1..915
FT                   /note="Coronin-7"
FT                   /id="PRO_0000291588"
FT   REPEAT          75..115
FT                   /note="WD 1"
FT   REPEAT          124..163
FT                   /note="WD 2"
FT   REPEAT          166..205
FT                   /note="WD 3"
FT   REPEAT          209..253
FT                   /note="WD 4"
FT   REPEAT          533..573
FT                   /note="WD 5"
FT   REPEAT          583..623
FT                   /note="WD 6"
FT   REPEAT          626..665
FT                   /note="WD 7"
FT   REPEAT          719..759
FT                   /note="WD 8"
FT   REGION          396..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2V7"
FT   MOD_RES         456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35828"
FT   MOD_RES         905
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2V7"
FT   CROSSLNK        463
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P57737"
SQ   SEQUENCE   915 AA;  99252 MW;  379F42385306212A CRC64;
     MNRFKVSKFR HTEARQPRRE AWIGDIRAGT APSCGNHIKA SCSLIAFNSD HPGVLGIVPL
     ESQGEDKRQV THLGCHSDLV TDLDFSPFDD FLLATASADR TVKLWRLPLS GQALPSGPGL
     LLGPEDAQVE VLQFHPTADG VLLSAAGRAV KVWDATKQQP LTELATHGDL VQGAAWSRDG
     ALLGTTCKDK QLRIFDPRAK PEAAQSTPAH ENSRDGRLVW TGTQEYLVST GFNQMREREV
     KLWDTRLFSA ALTSLTLDTS PRSLVPLLDP DSGLLVLAGK GENQLYCYEA APQQPALSPV
     TQCLLESVLR GAALVPRRAL AVMGCEVLRV LQLSDTAIVP ISYHVPRKTV EFHEDLFPDT
     AGCVPASDPH AWWAGSDQQV QRVSLHPARR AHPSFTSCLA PPAELTPATA QPAGTPEGFS
     STPSSLTSPS TPSSLGPSLT STSGIGTSPS QRSLQSLLGP SSKFRHAQGS VLHRDSHITN
     LKGLNLTTPG ESDGFCANQL RVAVPLLSSG GQVAVLELRK PGRLPDTALP TLQNGVAVTD
     LAWDPFDPHR LAVAGEDARI RLWRVPPDGL QEVLTMPEAV LTGHTEKIYS LRFHPLAADV
     LASSSYDLTV RIWDLKVGAE QLRLQGHRDQ IFGLAWSPDG QQLATVCKDG RLRIYEPRGS
     PEPLQEGPGP EGARGARVVW VCDGHYLLVS GFDSRSERQL LLYSAKALAG GPSAVLGLDV
     APSTLLPSYD PDTGLVLLTG KGDTRVFLYE LLPGAPFFLE CNSFTSPDPH KGFILLPKTE
     CDVREVEFAR CLRLRQTSLE PVAFRLPRVR KEFFQDDVFP DTTVSWEPAL SAEAWLGGAN
     GTPRLLSLQP PGMTPVSQAP REAPARRAPS SVYLEEKSDQ QKKEELLSAM VAKLGNREDP
     LPQDSFEGVD EDEWD