FEM1B_XENLA
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