BTB3_SCHPO
ID BTB3_SCHPO Reviewed; 523 AA.
AC Q10225;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=BTB/POZ domain-containing protein 3;
GN Name=btb3; ORFNames=SPAC13D6.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP INTERACTION WITH CUL3, AND UBIQUITINATION.
RX PubMed=14527422; DOI=10.1016/s1097-2765(03)00341-1;
RA Geyer R., Wee S., Anderson S., Yates J. III, Wolf D.A.;
RT "BTB/POZ domain proteins are putative substrate adaptors for cullin 3
RT ubiquitin ligases.";
RL Mol. Cell 12:783-790(2003).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Probable substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with cul3. {ECO:0000269|PubMed:14527422}.
CC -!- INTERACTION:
CC Q10225; Q09760: cul3; NbExp=4; IntAct=EBI-3648208, EBI-3647930;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Ubiquitinated and targeted for cul3-dependent degradation.
CC {ECO:0000269|PubMed:14527422}.
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DR EMBL; CU329670; CAA93544.1; -; Genomic_DNA.
DR PIR; T37624; T37624.
DR RefSeq; NP_593682.1; NM_001019114.2.
DR AlphaFoldDB; Q10225; -.
DR SMR; Q10225; -.
DR BioGRID; 279317; 4.
DR IntAct; Q10225; 2.
DR STRING; 4896.SPAC13D6.04c.1; -.
DR MaxQB; Q10225; -.
DR PaxDb; Q10225; -.
DR PRIDE; Q10225; -.
DR EnsemblFungi; SPAC13D6.04c.1; SPAC13D6.04c.1:pep; SPAC13D6.04c.
DR GeneID; 2542872; -.
DR KEGG; spo:SPAC13D6.04c; -.
DR PomBase; SPAC13D6.04c; btb3.
DR VEuPathDB; FungiDB:SPAC13D6.04c; -.
DR eggNOG; KOG0511; Eukaryota.
DR HOGENOM; CLU_022885_2_0_1; -.
DR InParanoid; Q10225; -.
DR OMA; LQYDYSK; -.
DR PhylomeDB; Q10225; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q10225; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; ISS:PomBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IPI:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.710.10; -; 2.
DR InterPro; IPR044515; ABTB1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR46231; PTHR46231; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00651; BTB; 2.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00225; BTB; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF54695; SSF54695; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50097; BTB; 2.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Reference proteome; Repeat; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..523
FT /note="BTB/POZ domain-containing protein 3"
FT /id="PRO_0000067248"
FT REPEAT 85..114
FT /note="ANK"
FT DOMAIN 167..223
FT /note="BTB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 306..373
FT /note="BTB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
SQ SEQUENCE 523 AA; 60445 MW; B565690ECCBF6A5E CRC64;
MASQDQNTGT THVELQGGEN SKKLFSKYDL WSKAMDEKKL SSSLFTVNDT QEFLELCEAC
RRGDLEVVKS LVENYNTPIN QVDQFDYSPL VLASLCGHEP VVKFLLENGA LCERDTFQGE
RCLYGALNDN IRRMLLSYDI TKAIDESQPY ASHITSLLSN SALHFTTDIV FAGQYGRVFA
HKFYLAARSS YFKSKFSKLG PSEHEIEVKH FAKEFESILR YLYLDTNAVF TKQYNNALLS
IGKKFQLNDF IALYEKDREQ LHSRDWKKIQ LAKTQNDLGE FLDYIISNYK VPIESLNQPS
DQYSFHDAYL QSYTHRYPVH RAIMCRCEYF LDMLAGPFLE SNQELPVLSL PFSSSVVEIV
LKFLYTDKTD IAPELALDVV YVADMLSLDK DRSLKSLASI VITKQEEPID SIYDILRTAW
DTSTPRLEQY ASEYMANHLE HLIDDPEFCE LVKESADRIL QRQETDTIEL IDDIRYFLSK
RFGIYHEDLC IDGVVDTLTP YESEYNQKME MIDDLLDKLE LQA
