ID F4K0X5_ARATH Unreviewed; 1075 AA.
AC F4K0X5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Regulator of chromosome condensation (RCC1) family with FYVE zinc finger domain-containing protein {ECO:0000313|EMBL:AED91798.1};
GN OrderedLocusNames=At5g12350 {ECO:0000313|Araport:AT5G12350,
GN ECO:0000313|EMBL:AED91798.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:AED91798.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AED91798.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130714; DOI=10.1038/35048507;
RG Kazusa DNA Research Institute;
RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG European Union Arabidopsis Genome Sequencing Consortium;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3] {ECO:0007829|PDB:6L0V, ECO:0007829|PDB:6L0W}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1006-1066.
RX PubMed=31900388; DOI=10.1038/s41467-019-13729-7;
RA Furutani M., Hirano Y., Nishimura T., Nakamura M., Taniguchi M., Suzuki K.,
RA Oshida R., Kondo C., Sun S., Kato K., Fukao Y., Hakoshima T., Morita M.T.;
RT "Polar recruitment of RLD by LAZY1-like protein during gravity signaling in
RT root branch angle control.";
RL Nat. Commun. 11:76-76(2020).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002688; AED91798.1; -; Genomic_DNA.
DR RefSeq; NP_568268.3; NM_121273.5.
DR PDB; 6L0V; X-ray; 1.35 A; A/C/E/G=1006-1066.
DR PDB; 6L0W; X-ray; 1.59 A; A/C=1006-1066.
DR PDBsum; 6L0V; -.
DR PDBsum; 6L0W; -.
DR AlphaFoldDB; F4K0X5; -.
DR SMR; F4K0X5; -.
DR STRING; 3702.F4K0X5; -.
DR iPTMnet; F4K0X5; -.
DR PaxDb; 3702-AT5G12350-1; -.
DR ProteomicsDB; 198189; -.
DR EnsemblPlants; AT5G12350.1; AT5G12350.1; AT5G12350.
DR GeneID; 831110; -.
DR Gramene; AT5G12350.1; AT5G12350.1; AT5G12350.
DR KEGG; ath:AT5G12350; -.
DR Araport; AT5G12350; -.
DR TAIR; AT5G12350; -.
DR eggNOG; ENOG502S0QB; Eukaryota.
DR HOGENOM; CLU_005343_0_0_1; -.
DR InParanoid; F4K0X5; -.
DR OMA; SHCHQRN; -.
DR OrthoDB; 551430at2759; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K0X5; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd13365; PH_PLC_plant-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013591; Brevis_radix_dom.
DR InterPro; IPR027988; BRX_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22870; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR PANTHER; PTHR22870:SF373; REGULATOR OF CHROMOSOME CONDENSATION (RCC1) FAMILY WITH FYVE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08381; BRX; 1.
DR Pfam; PF13713; BRX_N; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF16457; PH_12; 1.
DR Pfam; PF00415; RCC1; 6.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS51514; BRX; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 7.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6L0V, ECO:0007829|PDB:6L0W};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F4K0X5,
KW ECO:0007829|ProteomicsDB:F4K0X5};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT REPEAT 265..326
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 327..378
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 379..431
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 432..483
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 496..547
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 548..599
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 600..651
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 656..718
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1007..1062
FT /note="BRX"
FT /evidence="ECO:0000259|PROSITE:PS51514"
FT REGION 132..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 860..936
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 144..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1075 AA; 117521 MW; F25F32A1E595B911 CRC64;
MSRNGRMASD LSRAGPVERD IEQAIIALKK GAYLLKYGRR GKPKFCPFRL SNDETVLIWF
SGNEEKHLKL SHVSRIISGQ RTPIFQRYPR PEKEYQSFSL IYSERSLDVI CKDKDEAEVW
FTGLKALISH CHQRNRRTES RSDGTPSEAN SPRTYTRRSS PLHSPFSSND SLQKDGSNHL
RIHSPFESPP KNGLDKAFSD MALYAVPPKG FYPSDSATIS VHSGGSDSMH GHMRGMGMDA
FRVSMSSAVS SSSHGSGHDD GDALGDVFIW GEGIGEGVLG GGNRRVGSSF DIKMDSLLPK
ALESTIVLDV QNIACGGQHA VLVTKQGESF SWGEESEGRL GHGVDSNIQQ PKLIDALNTT
NIELVACGEF HSCAVTLSGD LYTWGKGDFG VLGHGNEVSH WVPKRVNFLL EGIHVSSIAC
GPYHTAVVTS AGQLFTFGDG TFGVLGHGDK KSVFIPREVD SLKGLRTVRA ACGVWHTAAV
VEVMVGSSSS SNCSSGKLFT WGDGDKGRLG HGNKEPKLVP TCVAALVEPN FCQVACGHSL
TVALTTSGHV YTMGSPVYGQ LGNSHADGKT PNRVEGKLHK SFVEEIACGA YHVAVLTSRT
EVYTWGKGSN GRLGHGDVDD RNSPTLVESL KDKQVKSIAC GTNFTAAVCI HRWASGMDQS
MCSGCRQPFS FKRKRHNCYN CGLVFCHSCT SKKSLKACMA PNPNKPYRVC DKCFNKLKKT
METDPSSHSS LSRRGSINQG SDPIDKDDKF DSRSDGQLAR FSLMESMRQV DSRHKKNKKY
EFNSSRVSPI PSGSSQRGAL NIAKSFNPVF GASKKFFSAS VPGSRIVSRA TSPISRRPSP
PRSTTPTPTL SGLATPKFVV DDTKRTNDNL SQEVVKLRSQ VESLTRKAQL QEVELERTTK
QLKEALAITN EETTRCKAAK EVIKSLTAQL KDMAERLPVG SARTVKSPPS LNSFGSSPGR
IDPFNILNQA NSQESEPNGI TTPMFSNGTM TPAFGNGEAT NEARNEKEWV EQDEPGVYIT
LTALAGGARD LKRVRFSRKR FSEIQAEQWW ADNRGRVYEQ YNVRMVDKAS EDLPR
//
