ID   CORO7_PONAB             Reviewed;         925 AA.
AC   Q5RBW3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Coronin-7;
DE            Short=Crn7;
GN   Name=CORO7;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 (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-472) 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; CR858520; CAH90747.1; -; mRNA.
DR   RefSeq; NP_001127329.1; NM_001133857.1.
DR   AlphaFoldDB; Q5RBW3; -.
DR   SMR; Q5RBW3; -.
DR   STRING; 9601.ENSPPYP00000007981; -.
DR   GeneID; 100174390; -.
DR   KEGG; pon:100174390; -.
DR   CTD; 79585; -.
DR   eggNOG; KOG1445; Eukaryota.
DR   InParanoid; Q5RBW3; -.
DR   Proteomes; UP000001595; 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: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; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR10856; PTHR10856; 1.
DR   PANTHER; PTHR10856:SF20; PTHR10856:SF20; 1.
DR   Pfam; PF08953; DUF1899; 2.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM01166; DUF1899; 2.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
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..925
FT                   /note="Coronin-7"
FT                   /id="PRO_0000284444"
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          542..582
FT                   /note="WD 5"
FT   REPEAT          592..632
FT                   /note="WD 6"
FT   REPEAT          635..674
FT                   /note="WD 7"
FT   REPEAT          728..768
FT                   /note="WD 8"
FT   REGION          196..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         462
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2V7"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35828"
FT   MOD_RES         915
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2V7"
FT   CROSSLNK        472
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P57737"
FT   CROSSLNK        680
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P57737"
SQ   SEQUENCE   925 AA;  100542 MW;  AD40A3E0D2A80393 CRC64;
     MNRFRVSKFR HTEARPPRRE AWLSDIRAGT APSCRNHIKS SCSLITFNSD RPGVLGIVPL
     QGQGEDKRRV AHLGCHSDLV TDLDFSPFDD FLLATGSADR TVKLWRLPGP GQALPSAPGV
     VLGPEDLPVE VLQFHPTSDG ILVSAAGTTV KVWDAAKQQP LTELEAHGDL VQSAVWSRDG
     ALVGTACKDK QLRIFDPRTK PQASQSTQAH ENSRDSRLAW TGTWEHFVST GFNQMREHEV
     KLWDTRFFSS ALASLTLDTS LGCLMPLLDP DSGLLVLAGK GKRQLYCYEV VPQQPALSPV
     TQCVLESVLR GAALVPRQAL AVMSCEVLRV LQLSDTAIVP IGYHVPRKAV EFHEDLFPDT
     AGCVPATDPH SWWAGDNQQA QKVSLNPACR PHPSFTSCLV PPTEPLPDTA QPAVTETPVG
     DADASEGFSS PPSSLTSPST PSSLGPTLSS TSGIGTGPSL RSLQSLLGPS SKFRHAQGTV
     LHRDSHITNL KGLNLTTPGE SDGFCANKLR VAVPLLSSGG QVAVLELRKP GRLPDTALPT
     LQNGAAVTDL AWDPFDPHRL AVAGEDARIR LWRVPAEGLE EVLTVPETVL TGHMEKICSL
     RFHPLAADVL ASSSYDLTVR IWDLQAGVDR LKLQGHQDQI FSLAWSPDGQ QLATVCKDGR
     VRVYRPRSGP EPLQEGPGPK GGRGARIVWV CDGRCLLVSG FDSQSERQLL LYEAEALAGG
     PLAVLGLDVA PSTLVPSYEP RHWPGAPDWQ GDARVFLYEL LPESPFFMEC NSFTSPDPHK
     GFVLLPKTEC DVREVELMRC LRCASPPWSL WPSGCPESGK SSFQDDVFPD TAVSWEPVLS
     AEAWLQGANG QPWLLSLQPP DMSPVSQAPR EAPARRAPSS AQYLEEKSDQ QKKEELLNAM
     VAKLGNREDP LPQDSFEGVD EDEWD