ID G1SCT5_RABIT Unreviewed; 1050 AA.
AC G1SCT5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Coronin {ECO:0000256|RuleBase:RU280818};
GN Name=CORO7 {ECO:0000313|Ensembl:ENSOCUP00000000173.4};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000000173.4, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000000173.4, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000000173.4}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000000173.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; G1SCT5; -.
DR STRING; 9986.ENSOCUP00000000173; -.
DR PaxDb; 9986-ENSOCUP00000000173; -.
DR Ensembl; ENSOCUT00000000195.4; ENSOCUP00000000173.4; ENSOCUG00000000193.4.
DR eggNOG; KOG1445; Eukaryota.
DR GeneTree; ENSGT00940000156606; -.
DR HOGENOM; CLU_006604_0_0_1; -.
DR InParanoid; G1SCT5; -.
DR TreeFam; TF314280; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000000193; Expressed in blood and 18 other cell types or tissues.
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; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030041; P:actin filament polymerization; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0006895; P:Golgi to endosome transport; IEA:Ensembl.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IEA:Ensembl.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR10856; CORONIN; 1.
DR PANTHER; PTHR10856:SF20; CORONIN-7; 1.
DR Pfam; PF08953; DUF1899; 2.
DR Pfam; PF00400; WD40; 5.
DR Pfam; PF16300; WD40_4; 2.
DR SMART; SM01166; DUF1899; 2.
DR SMART; SM01167; DUF1900; 2.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU280818};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 3..64
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 73..107
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 458..523
FT /note="DUF1899"
FT /evidence="ECO:0000259|SMART:SM01166"
FT REPEAT 582..624
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 625..666
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 198..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..935
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 113017 MW; 16A6862292430472 CRC64;
MNRFKVSKFR NVEVRLSRRE AWISNIQAGT APSSGNRIKS SCSLIAFNSD RPGVLGIVPL
EGQGGDKRQV AHLGCHSDLV TDLDFSPFDD FLLATGSADK TVKLWRLPAP GQAPPSGPGV
VLGPEEHPVE ALQFHPTADG VLVSAAGTAV KVWDAAARQP LTELVAHGDL VQSAVWSRDG
ALVGTACKDK QLRIFDPRAK HQASQSTQAH ENSRDGQLAW TATQEHLVST GFNQMREREV
KLWDTRLFSS ALASLTLDTS PRSLMPLLDP DSGLLVLAGK GESQLYCYET APRQPALSPV
NQCILENVLQ GAALVPRRAL AVMSCEVLRV LQLSDTAIVP VGYHVPRKTV EFHEDLFPDT
AGCVPASDSH AWWTGSNQQV QKVSLDPARR PHPSFTSCLV PALEPHLGTA QPAETPVDDA
DPSEGFSSPP SSLTSPSTLS STTSGIGTSL SQRSLQSLLG PSSKFRHAQG TVLHRDSHIT
NLKGLNLTTP GESDGFCANQ LRVAVPLLSS GGQVAVLELR KPGRLPDTAL PTLQNGAAVT
DLAWDPFDPH RLAVAAEDAR IRLWRVPPEG LEEVLTTPEA VLTGHTEKIY SLRFHPRAAD
VLASSSYDLT VRIWDLQAGA ERLRLRGHQD QIFGMAWSPD GQQLATVCKD GRVRVYEPRN
GPEPLQEGPG PEGGRGARVV WVCDGRCLLV SGFDSRSERQ LLLYAAGALA GGPSAVLGLD
VAPSTLLPSY DPDTGLVLLT GKGDTRVFLY ELLPEAPFFL ECNSFTSPDP HKGFVLLPKT
ECDVREVEFA RCLRLRQTSL EPVAFRLPRV RKEFFQDDVF PATAVTWEPV LSAQAWLGGA
DGQPRMLSLQ PPGMTPVSQA PREAPARRGP SSAQYLEEKS DQQKKEELLS AMVAKLGNRG
GPLPQDSFER RGRGRVGEWP VRPAPPPPRR VRRLPATAPL PPSHCLVCAP RTSRPTISSG
LTCCCRAPEP HPTSHSQTGR RLPGLACRSP EAPGPWASCT PVDCLVPLLS LGLAASLQLP
ASMWSQGCRV GGPQHGPGQA LGSSSPPPSY
//
