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Database: UniProt
Entry: O74881
LinkDB: O74881
Original site: O74881 
ID   BTB1_SCHPO              Reviewed;        1347 AA.
AC   O74881;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=BTB/POZ domain-containing protein 1;
GN   Name=btb1; ORFNames=SPCC330.11;
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.
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).
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       O74881; Q09760: cul3; NbExp=3; IntAct=EBI-3647943, EBI-3647930;
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DR   EMBL; CU329672; CAA20916.1; -; Genomic_DNA.
DR   PIR; T41321; T41321.
DR   RefSeq; NP_587711.1; NM_001022706.1.
DR   AlphaFoldDB; O74881; -.
DR   SMR; O74881; -.
DR   BioGRID; 275298; 29.
DR   IntAct; O74881; 2.
DR   STRING; 284812.O74881; -.
DR   iPTMnet; O74881; -.
DR   MaxQB; O74881; -.
DR   PaxDb; 4896-SPCC330-11-1; -.
DR   EnsemblFungi; SPCC330.11.1; SPCC330.11.1:pep; SPCC330.11.
DR   GeneID; 2538714; -.
DR   KEGG; spo:SPCC330.11; -.
DR   PomBase; SPCC330.11; btb1.
DR   VEuPathDB; FungiDB:SPCC330.11; -.
DR   eggNOG; KOG0783; Eukaryota.
DR   HOGENOM; CLU_004619_0_0_1; -.
DR   InParanoid; O74881; -.
DR   OMA; RIPVHEF; -.
DR   PhylomeDB; O74881; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O74881; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IPI:PomBase.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISM:PomBase.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd18286; BTB2_POZ_BTBD8; 1.
DR   CDD; cd18186; BTB_POZ_ZBTB_KLHL-like; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR22872:SF2; BTB_POZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR22872; BTK-BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00651; BTB; 2.
DR   Pfam; PF00415; RCC1; 2.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00225; BTB; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF54695; POZ domain; 2.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50097; BTB; 2.
DR   PROSITE; PS50012; RCC1_3; 4.
PE   1: Evidence at protein level;
KW   ANK repeat; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..1347
FT                   /note="BTB/POZ domain-containing protein 1"
FT                   /id="PRO_0000278357"
FT   REPEAT          51..81
FT                   /note="ANK 1"
FT   REPEAT          86..115
FT                   /note="ANK 2"
FT   REPEAT          148..198
FT                   /note="RCC1 1"
FT   REPEAT          215..264
FT                   /note="RCC1 2"
FT   REPEAT          265..322
FT                   /note="RCC1 3"
FT   REPEAT          324..372
FT                   /note="RCC1 4"
FT   DOMAIN          619..698
FT                   /note="BTB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          758..829
FT                   /note="BTB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REGION          1006..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1104..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1193..1237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1286..1347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1122..1138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1196..1237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1307..1322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1347 AA;  152586 MW;  A5A3C9FF2E682C3C CRC64;
     MSHLLFAYYL CNDIRSFQNL LKQDDSKVKE PRKGFSEKSG QKLRINQKDR YGRTVLHIAV
     SENKNSFVRS LLQHKGIDVF VQDEESGYTA LHRAIYVGNL EAASLLLSKD PSFRSLRIKD
     KEGLSPFQFL SRVLSSTIHP VLDLPIIGNE LYGFGTNVNN TLGIANGKEP SSPERVFLLK
     NQTESPTSGQ LFSRDKILDV QASKFHSVVL TDEPSQNVYV CGIGAGGRIG FNTDVQYNFI
     PIPGIIHKVI QISVSHTHSL ALTKFGSIYS WGKNGSGELG LSNDELKKDD PIQITPRRIS
     AFKDYQIIGM AAGKSYSVAW TDTDIYSWGL NNGQLGISDH ISVVSTPRRV AGLLSPVIHA
     VCTTRATICL LQNNSIIAFC NYNQVKLPFN VDFGSSLKVT KHPLSLTRFN VRKLLASENK
     LAVLTELGEV YEFDMKLLLD RDSTSSKNST RTSFKFTPLW IFESSDLAAL DIAWTADNSL
     ILCTRNGTCW KRELRSKKRE KSSSSPYSRG PYKYNRIENL QMVVGVRASA SGSFFAIRND
     YLPPPIYKPS NMLIDLLRSL LPYDHLLHVR QPRLIPPEDE DGVPIFDEDR AASSNEMQLL
     FEGSIPILTS YENYKQSFSD VTIYCGTSMF HSHKFILCAR SSFLRKLLLQ KKKSSVSNII
     YIEEITQSHS TIRVEDIPPL AVAILLHYLY TDTLLSPWHL DSRFSPLKEN LSKLANLLEL
     PHLAEVLPFS VSRQPLLSLT NDILQLYNNF YVLCEETMDT VIKLKDGELK AHGLFLSLRS
     EYFSSYFQFV SMESNSFDIP ITVNLSHLTV EHMSIVLRHV YSDLKVELFD DLKESDFHNW
     LETMFEILSI ADELLFLELK SIAQQSLLRF LNLKTLPTLM DLSLSYHAEE LYSRCIDYAC
     HNIEFFLEAN RISEWDGFHL KKVAQRLTEL LSDQRVHLPS SKIANRLLIR DPVLMEKRNY
     ELKVLREYLF SQESSQLWDD SPYRSIFEDR RCSTSAVILE SGIVPSSNQS DSLNKEDAEE
     KSPKPNVVNV TSITKTAGAS VEIQNNIESA SSGGDKTQLN GPGADQPVTA TITFDKTSPW
     RNRENLSHNN NTTRASLREL LEQEKADAST TTVLSDSRFM KAPTKKSQRE KKKELSKQVP
     ISKTNVGHID IELGKSNHSN PWSVATHQRG SFSSSTGVKK SFNGILREAA REEGSSQVIY
     QESKKRISNG SPTSWNLLTK PSPRSASLPK NSQPLSISEI MTEQKEEIES QKRRSSFRKT
     IEEIQQEEEF QKWWEEESLR VQKELGILKT ERDTSTNRKQ GQASKQPQRR HRKEKDSKVS
     ESTAEFKSLP IDIPRTTHKK GKARAVK
//
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