ID   COR1B_PONAB             Reviewed;         489 AA.
AC   Q5NVK4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Coronin-1B;
GN   Name=CORO1B;
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: Regulates leading edge dynamics and cell motility in
CC       fibroblasts. May be involved in cytokinesis and signal transduction (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms homooligomers, but does not form complexes with the
CC       other coronins. Interacts with Arp2/3 complex components, including
CC       ACTR2, ARPC1B and ARPC2. Binds actin (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9BR76}. Cytoplasm, cytoskeleton, stress fiber
CC       {ECO:0000250|UniProtKB:Q9BR76}. Note=Localized to the leading edge in
CC       fibroblasts, as well as weakly along actin stress fibers.
CC       {ECO:0000250|UniProtKB:Q9BR76}.
CC   -!- PTM: Phosphorylation on Ser-2 regulates the interaction with the Arp2/3
CC       complex and cell motility in fibroblasts. Phosphorylation does not seem
CC       to affect subcellular location (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI29659.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR926022; CAI29659.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001127097.1; NM_001133625.1.
DR   AlphaFoldDB; Q5NVK4; -.
DR   SMR; Q5NVK4; -.
DR   STRING; 9601.ENSPPYP00000003469; -.
DR   GeneID; 100174131; -.
DR   KEGG; pon:100174131; -.
DR   CTD; 57175; -.
DR   eggNOG; KOG0303; Eukaryota.
DR   InParanoid; Q5NVK4; -.
DR   OrthoDB; 552726at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR027340; Coro1b.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
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:SF24; PTHR10856:SF24; 1.
DR   Pfam; PF08953; DUF1899; 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; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..489
FT                   /note="Coronin-1B"
FT                   /id="PRO_0000229770"
FT   REPEAT          80..120
FT                   /note="WD 1"
FT   REPEAT          130..170
FT                   /note="WD 2"
FT   REPEAT          174..213
FT                   /note="WD 3"
FT   REPEAT          217..260
FT                   /note="WD 4"
FT   REPEAT          265..305
FT                   /note="WD 5"
FT   REGION          414..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          449..474
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BR76"
SQ   SEQUENCE   489 AA;  54229 MW;  652168F74D3AACF3 CRC64;
     MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV IVEASGGGAF
     LVLPLSKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS GSEDCTVMVW QIPENGLTSP
     LTEPVVVLEG HTKRVGIIAW HPTARNVLLS AGCDNVVLIW NVGTAEELYR LDSLHPDLIY
     NVSWNRNGSL FCSACKDKSV RIIDPRQGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS
     RMSERQLALW DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITEE
     PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM TVPRKSDLFQ
     DDLYPDTAGP EAALEAEEWV SGRDADPILI SLREAYVPSK QRDLKISRRN VLSDSRPAMA
     PGSSRLGAPA STTAAADATP SGSLARAGEA GKLEEVMQEL RALRALVKEQ GERICRLEEQ
     LGRMENGDA