ID A0A2J7R8V2_9NEOP Unreviewed; 897 AA.
AC A0A2J7R8V2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Coronin {ECO:0000256|RuleBase:RU280818};
GN ORFNames=B7P43_G00408 {ECO:0000313|EMBL:PNF37261.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF37261.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF37261.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF37261.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) 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.
CC {ECO:0000256|ARBA:ARBA00024838}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC {ECO:0000256|RuleBase:RU280818}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNF37261.1}.
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DR EMBL; NEVH01006721; PNF37261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7R8V2; -.
DR InParanoid; A0A2J7R8V2; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
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; IPR024977; Apc4-like_WD40_dom.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF08953; DUF1899; 1.
DR Pfam; PF00400; WD40; 1.
DR Pfam; PF16300; WD40_4; 1.
DR SMART; SM01166; DUF1899; 1.
DR SMART; SM01167; DUF1900; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000235965};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280818};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 4..38
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 54..95
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 96..128
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 786..851
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REGION 347..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 98942 MW; C821B7B215B85DE2 CRC64;
MPLLHAHTDT VTDMDFSPFH DGLLATGSQD CLVKLWHIPD KGLEESLYNA ECTFSHKQRR
VETVCFHPTA DCLLTTTSYT TLTLWDISSE KEMLSNAEHS DVIQSLSWKK DGTLLATSCK
DKQVRILDPR LPANSFTHMA NSHQSIKDSR VVWLGDTGKI LTTGFDSGRQ REVFIRDLRN
FEDCEKALVL DSSTGILIPL YDPDTGMLFL AGKGDTTISY LEVTDREPYL LEGIRHNGEQ
TKGACLVPKR SLAVMQGEVN RLLQLTSSSV IPIMYQVPRK SYRDFHADLF PDTTGCEAQL
SAVQWLQGHN APVPRISLDP AKRSAGESPI QVHRGSLSEM RKHLQHNPYT STSVSQQKTS
NKIQTAVKLK EEGHMVRDHK IGKDDERSSS ENGLHHNSDS TKSHQQNGSS ENHQIIPPKP
LPRALRGGSL SETEDVVVAP PKPKPRTTTS TISTSQPTSV IPPVTSVNPA TAITGGYKPR
LGPKPFTPPK LNFSSSGSGD GDIKGTTEFS FDKVFSVPVA PGHEAMNGAL NRHGNSFHTV
DNENSGTNQN LSYIENDLQS KGGEYRDEEL KEVCEDIPLS ACKDNVGPYQ DETKSRIGLQ
SENVSEGDVQ PNSGSFEELS PTSPTLHGKP KTPSTAERRK FYEKRISSIA GEQEGTQLAV
DTLKFDDTDD KLEDFERASV QRSSIAERRR VYENRSASIQ EASAAEKRSP TLSPTPLRRK
DSYKSSKACV PDVVKEDKED TESKRSPVAV QRQQSQEQPA AGKSPPTQDK KPEPATTPTP
KRTSTVFGRV SKFRHLKGTS LHKSTHIENI RNVSRQISGE CDGFHANRER VAVPLSGPGG
KIAVFELSKT GKLPDGVIPT LVHGTNIMDF AWDPFNCKRL AVGEEHRLKI PLISNIS
//
