ID FIP2_ARATH Reviewed; 298 AA.
AC Q9SE95;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=FH protein interacting protein FIP2;
DE AltName: Full=BTB/POZ domain-containing protein At5g55000;
GN Name=FIP2; OrderedLocusNames=At5g55000; ORFNames=MBG8.27;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH FH1.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10929945; DOI=10.1093/pcp/41.5.617;
RA Banno H., Chua N.-H.;
RT "Characterization of the Arabidopsis formin-like protein AFH1 and its
RT interacting protein.";
RL Plant Cell Physiol. 41:617-626(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DOMAIN BTB.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with FH1. {ECO:0000269|PubMed:10929945}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SE95-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues but preferentially in
CC roots and flowers. {ECO:0000269|PubMed:10929945}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
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DR EMBL; AF174429; AAF14550.1; -; mRNA.
DR EMBL; AB017059; BAB10574.1; -; Genomic_DNA.
DR EMBL; AB005232; BAB10574.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED96567.1; -; Genomic_DNA.
DR EMBL; BT030093; ABN04831.1; -; mRNA.
DR RefSeq; NP_200311.1; NM_124882.4. [Q9SE95-1]
DR AlphaFoldDB; Q9SE95; -.
DR SMR; Q9SE95; -.
DR BioGRID; 20835; 1.
DR STRING; 3702.Q9SE95; -.
DR iPTMnet; Q9SE95; -.
DR PaxDb; 3702-AT5G55000-2; -.
DR ProteomicsDB; 228923; -. [Q9SE95-1]
DR EnsemblPlants; AT5G55000.2; AT5G55000.2; AT5G55000. [Q9SE95-1]
DR GeneID; 835591; -.
DR Gramene; AT5G55000.2; AT5G55000.2; AT5G55000. [Q9SE95-1]
DR KEGG; ath:AT5G55000; -.
DR Araport; AT5G55000; -.
DR TAIR; AT5G55000; FIP2.
DR eggNOG; KOG1665; Eukaryota.
DR HOGENOM; CLU_043894_1_1_1; -.
DR InParanoid; Q9SE95; -.
DR OMA; YACIKNA; -.
DR OrthoDB; 54069at2759; -.
DR PhylomeDB; Q9SE95; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SE95; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SE95; baseline and differential.
DR Genevisible; Q9SE95; AT.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd18376; BTB_POZ_FIP2-like; 1.
DR Gene3D; 2.160.20.80; E3 ubiquitin-protein ligase SopA; 2.
DR InterPro; IPR001646; 5peptide_repeat.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR PANTHER; PTHR14136:SF17; BTB_POZ DOMAIN-CONTAINING PROTEIN KCTD9; 1.
DR PANTHER; PTHR14136; UNCHARACTERIZED; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00805; Pentapeptide; 3.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF141571; Pentapeptide repeat-like; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..298
FT /note="FH protein interacting protein FIP2"
FT /id="PRO_0000405333"
FT DOMAIN 9..80
FT /note="BTB"
FT DOMAIN 129..165
FT /note="Pentapeptide repeat 1"
FT DOMAIN 166..203
FT /note="Pentapeptide repeat 2"
FT DOMAIN 216..255
FT /note="Pentapeptide repeat 3"
FT DOMAIN 256..295
FT /note="Pentapeptide repeat 4"
SQ SEQUENCE 298 AA; 32828 MW; 07B493A8656A84F6 CRC64;
METSSNLSSM VRLNIGGKKF CTTIDTLTIR EPDSMLAAMF SGRHAMCQES KKGYVFIDRD
GKHFRHILNW LRDGVIPSLS DPDCSELLRE ADYYQLLGLK DGIKDSRKEV GEVEAELTRI
DIIKCIQTER VRFRGVNLSG IDLSKLDLSL VDFSYACLRN VFFSRTNLQC AKFRNADAEG
SIFHNAILRE CEFTSANLRG ALLAGTNLQS ANLQDACLVG CSFCGADLRT AHLQNADLTN
ANLEGANLEG ANLKGAKLSN ANFKGANLQR AYLRHVNLRE AHMEGANLGG ANMTGAIR
//
