ID   BAT41_CAEEL             Reviewed;         418 AA.
AC   P41886;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=BTB and MATH domain-containing protein 41;
GN   Name=bath-41; ORFNames=F37A4.9;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH CUL3.
RX   PubMed=13679922; DOI=10.1038/nature01985;
RA   Xu L., Wei Y., Reboul J., Vaglio P., Shin T.H., Vidal M., Elledge S.J.,
RA   Harper J.W.;
RT   "BTB proteins are substrate-specific adaptors in an SCF-like modular
RT   ubiquitin ligase containing CUL-3.";
RL   Nature 425:316-321(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       {ECO:0000269|PubMed:13679922}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with cul-3. {ECO:0000269|PubMed:13679922}.
CC   -!- INTERACTION:
CC       P41886; Q17391: cul-3; NbExp=2; IntAct=EBI-314147, EBI-593075;
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO081312; CCD70710.1; -; Genomic_DNA.
DR   PIR; S44646; S44646.
DR   RefSeq; NP_498473.1; NM_066072.4.
DR   AlphaFoldDB; P41886; -.
DR   SMR; P41886; -.
DR   BioGRID; 41162; 7.
DR   DIP; DIP-26170N; -.
DR   IntAct; P41886; 5.
DR   STRING; 6239.F37A4.9; -.
DR   EPD; P41886; -.
DR   PaxDb; P41886; -.
DR   PeptideAtlas; P41886; -.
DR   EnsemblMetazoa; F37A4.9.1; F37A4.9.1; WBGene00018137.
DR   GeneID; 175946; -.
DR   KEGG; cel:CELE_F37A4.9; -.
DR   UCSC; F37A4.9; c. elegans.
DR   CTD; 175946; -.
DR   WormBase; F37A4.9; CE00790; WBGene00018137; bath-41.
DR   eggNOG; KOG1987; Eukaryota.
DR   HOGENOM; CLU_657627_0_0_1; -.
DR   InParanoid; P41886; -.
DR   OMA; KDEECRG; -.
DR   OrthoDB; 864323at2759; -.
DR   PhylomeDB; P41886; -.
DR   Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR   SignaLink; P41886; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P41886; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00018137; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030162; P:regulation of proteolysis; IBA:GO_Central.
DR   Gene3D; 2.60.210.10; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR008974; TRAF-like.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00061; MATH; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS50144; MATH; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..418
FT                   /note="BTB and MATH domain-containing protein 41"
FT                   /id="PRO_0000065329"
FT   DOMAIN          45..173
FT                   /note="MATH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT   DOMAIN          232..293
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  47019 MW;  365CEDED4034FD8C CRC64;
     MEINNGAQPE NAAVSIPSRS PSGKSEKRKS PSIVSGCRTV MNERSFTNYW SVERFTVQLE
     LHNPAEFMLA PKFGDGDYEF VMKLFPNGKD EETAGYLSLF LLINKCPNPR LRFRVSFTVE
     TADGPRSCHL NKNLVTINRS GIVTASKFFS LDILRSAMNV YIPNDILTIG CELTIFGECT
     TQISSLFKPY QRTHSASSTS RSLSSPNTKC LKIDESSAHD AFTEFLSTGE FSDFIIVASC
     GREFPTHMCI LAARSEYFKV LLRNHSTKEF MSKRLQFDDI SARTLDVLLR HMYASAAGRV
     VKLEEDQLTE DLISAMDRLM INSLRDEVAR LIGSKVTVDN VLTRISMAAE LRLDDTYDVL
     LDFFSNHKHE CMKLTAWDEL ESAKPPLAIK ILRDAFSNTD SPSTTSMDSR IIDRITLT