BTB1_SCHPO
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 03-AUG-2022, entry version 132.
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; 4896.SPCC330.11.1; -.
DR iPTMnet; O74881; -.
DR MaxQB; O74881; -.
DR PaxDb; O74881; -.
DR PRIDE; O74881; -.
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; DLMFQMD; -.
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 Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.130.10.30; -; 1.
DR Gene3D; 3.30.710.10; -; 2.
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 Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00651; BTB; 2.
DR Pfam; PF00415; RCC1; 2.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00225; BTB; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF54695; SSF54695; 2.
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
