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Database: UniProt
Entry: BTB3_SCHPO
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Original site: 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   27-MAR-2024, entry version 154.
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; 284812.Q10225; -.
DR   MaxQB; Q10225; -.
DR   PaxDb; 4896-SPAC13D6-04c-1; -.
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; EGARCIY; -.
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   CDD; cd18497; BACK_ABTB1_BPOZ; 1.
DR   CDD; cd18296; BTB2_POZ_ABTB1_BPOZ1; 1.
DR   CDD; cd18186; BTB_POZ_ZBTB_KLHL-like; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
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; ANKYRIN REPEAT AND BTB/POZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46231:SF1; ANKYRIN REPEAT AND BTB_POZ DOMAIN-CONTAINING PROTEIN 1; 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; Ankyrin repeat; 1.
DR   SUPFAM; SSF54695; POZ domain; 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
//
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