ID   FEM1B_XENLA             Reviewed;         629 AA.
AC   Q6GPE5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein fem-1 homolog B {ECO:0000305};
DE            Short=FEM1b {ECO:0000250|UniProtKB:Q9UK73};
DE   AltName: Full=FEM1-beta;
GN   Name=fem1b {ECO:0000250|UniProtKB:Q9UK73};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC       ubiquitin-protein ligase complex of the DesCEND (destruction via C-end
CC       degrons) pathway, which recognizes a C-degron located at the extreme C
CC       terminus of target proteins, leading to their ubiquitination and
CC       degradation. The C-degron recognized by the DesCEND pathway is usually
CC       a motif of less than ten residues and can be present in full-length
CC       proteins, truncated proteins or proteolytically cleaved forms. The
CC       CRL2(FEM1B) complex specifically recognizes proteins ending with -Gly-
CC       Leu-Asp-Arg, leading to their ubiquitination and degradation.
CC       {ECO:0000250|UniProtKB:Q9UK73}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9UK73}.
CC   -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC       named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex.
CC       {ECO:0000250|UniProtKB:Q9UK73}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UK73}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9UK73}.
CC   -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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DR   EMBL; BC073194; AAH73194.1; -; mRNA.
DR   RefSeq; NP_001085685.1; NM_001092216.1.
DR   AlphaFoldDB; Q6GPE5; -.
DR   SMR; Q6GPE5; -.
DR   GeneID; 444111; -.
DR   KEGG; xla:444111; -.
DR   CTD; 444111; -.
DR   Xenbase; XB-GENE-999859; fem1b.L.
DR   OrthoDB; 252380at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 444111; Expressed in blastula and 19 other tissues.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:2000001; P:regulation of DNA damage checkpoint; ISS:UniProtKB.
DR   GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; ISS:UniProtKB.
DR   Gene3D; 1.25.40.20; -; 3.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 8.
DR   SUPFAM; SSF48403; SSF48403; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
PE   2: Evidence at transcript level;
KW   ANK repeat; Apoptosis; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW   TPR repeat; Ubl conjugation pathway.
FT   CHAIN           1..629
FT                   /note="Protein fem-1 homolog B"
FT                   /id="PRO_0000324534"
FT   REPEAT          47..77
FT                   /note="ANK 1"
FT   REPEAT          89..118
FT                   /note="ANK 2"
FT   REPEAT          122..151
FT                   /note="ANK 3"
FT   REPEAT          155..184
FT                   /note="ANK 4"
FT   REPEAT          188..217
FT                   /note="ANK 5"
FT   REPEAT          220..250
FT                   /note="ANK 6"
FT   REPEAT          346..379
FT                   /note="TPR"
FT   REPEAT          485..529
FT                   /note="ANK 7"
FT   REPEAT          533..570
FT                   /note="ANK 8"
SQ   SEQUENCE   629 AA;  70274 MW;  6065D4E0A852EC47 CRC64;
     MALDGLAGYV YKAAAEGRVL TLAALLLHRT EPEIRTLLST VTQHGGQRST PLIIAARNGH
     SKVVRLLLEH YKVDVQQTGT VRFDGYIIDG ATALWCAAGA GHYEVVKLLV SHEANVNHTT
     VTNSTPLRAA CFDGRLDIVR FLVENNANIS IANKYDNTCL MIAAYKGHSD VVHYLLRQHA
     DPNARAHCGA TALHFAAEAG HLDIVRELVK WKAAMVVNGH GMTPLKVAAE SCKADVVELL
     LAHSDCDAKS RIEALELLGA SFANDRENYN ITKTYQYLYL AMLERFRDPS NILHKEVLPP
     IEAYGMRTEC RNPQELGAIL HNTDDLHLEG LIVRERILGS DNIDVSHPII YRGAVYADNM
     QFEQCIKLWL HALQLRQKGN RNTHKDLLRF AQVFSQMIHL NEPVKSRDVE RVLECSVLEI
     ERGIARIQNP QEPDAHSTLE NHECNLYTFL YLVCISTKTC CSEEEQPCIN KQIYRLVHLD
     PRTREGGSLL HLAVDSGTPV DDFHTNDVCS FPSAPVAKLL IDCGANVNAV DQMGNSPLHV
     IVQYNRPISD FLTLHAIIIS LVEAGAHTDM TNKEKKTPLD RSTTGVSEIL LKTQMKLSLK
     CLAARAVRLH NIKYQNQIPR TLEEFVEFH