ID   COR1A_MACFA             Reviewed;         461 AA.
AC   Q4R4J2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Coronin-1A;
DE   AltName: Full=Coronin-like protein A;
DE            Short=Clipin-A;
GN   Name=CORO1A; ORFNames=QtrA-11316;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Temporal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be a crucial component of the cytoskeleton of highly
CC       motile cells, functioning both in the invagination of large pieces of
CC       plasma membrane, as well as in forming protrusions of the plasma
CC       membrane involved in cell locomotion. {ECO:0000250}.
CC   -!- SUBUNIT: Binds actin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC       Cytoplasmic vesicle, phagosome membrane {ECO:0000250}.
CC   -!- PTM: phosphorylation at Thr-412 by PKC strongly down-regulates the
CC       association with actin. {ECO:0000250}.
CC   -!- PTM: Polyubiquitinated by RNF128 with 'Lys-48'-linked chains, leading
CC       to proteasomal degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR   EMBL; AB169902; BAE01983.1; -; mRNA.
DR   AlphaFoldDB; Q4R4J2; -.
DR   SMR; Q4R4J2; -.
DR   STRING; 9541.XP_005591687.1; -.
DR   PRIDE; Q4R4J2; -.
DR   eggNOG; KOG0303; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0030595; P:leukocyte chemotaxis; IEA:InterPro.
DR   GO; GO:0001845; P:phagolysosome assembly; IEA:InterPro.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR029508; CORO1A.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
DR   InterPro; IPR015049; Trimer_CC.
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:SF18; PTHR10856:SF18; 1.
DR   Pfam; PF08953; DUF1899; 1.
DR   Pfam; PF08954; Trimer_CC; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM01166; DUF1899; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW   Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P31146"
FT   CHAIN           2..461
FT                   /note="Coronin-1A"
FT                   /id="PRO_0000270799"
FT   REPEAT          13..63
FT                   /note="WD 1"
FT   REPEAT          73..110
FT                   /note="WD 2"
FT   REPEAT          123..160
FT                   /note="WD 3"
FT   REPEAT          164..204
FT                   /note="WD 4"
FT   REPEAT          207..251
FT                   /note="WD 5"
FT   REPEAT          258..296
FT                   /note="WD 6"
FT   REPEAT          302..349
FT                   /note="WD 7"
FT   REGION          403..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          425..461
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P31146"
FT   MOD_RES         2
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P31146"
FT   MOD_RES         412
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P31146"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O89053"
FT   MOD_RES         449
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P31146"
SQ   SEQUENCE   461 AA;  50946 MW;  2F51033EB4885357 CRC64;
     MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFVALI CEASGGGAFL
     VLPLGKTGRV DKNAPTVCGH TAPVLDIAWC PHNDNVIASG SEDCTVMVWE IPDGGLVLPL
     REPVVTLEGH TKRVGIVAWH PTAQNVLLSA GCDNVIMVWD VGTGAAVLTL GPEVHPDTIY
     SVDWSRDGGL ICTSCRDKRV RIIEPRKCTV VAEKDRPHEG TRPVRAVFVS EGKILTTGFS
     RMSERQVALW GTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE
     APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERRCEPIAM TVPRKSDLFQ
     EDLYPPTAGP DPALTAEEWL GGRDAGPLLI SLKDGYVPPK SRELRVNRGL DTGRRRAAPE
     ASGTPSSDAV SRLEEEMRKL QATVQELQKR LDRLEETVQA K