FEM1C_XENLA
ID FEM1C_XENLA Reviewed; 617 AA.
AC Q2T9K6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein fem-1 homolog C {ECO:0000305};
DE Short=FEM1c {ECO:0000250|UniProtKB:Q96JP0};
DE AltName: Full=FEM1-gamma;
GN Name=fem1c {ECO:0000250|UniProtKB:Q96JP0};
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 (DEC-2005) 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(FEM1C) complex specifically recognizes proteins with an arginine
CC at the C-terminus: recognizes and binds proteins ending with -Lys/Arg-
CC Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, leading to their
CC ubiquitination and degradation. {ECO:0000250|UniProtKB:Q96JP0}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q96JP0}.
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:Q96JP0}.
CC -!- DOMAIN: The first seven ANK repeats at the N-terminus (1-242) are
CC essnetial for recognition of Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg
CC C-degrons. {ECO:0000250|UniProtKB:Q96JP0}.
CC -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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DR EMBL; BC111474; AAI11475.1; -; mRNA.
DR RefSeq; NP_001090163.1; NM_001096694.1.
DR RefSeq; XP_018106323.1; XM_018250834.1.
DR AlphaFoldDB; Q2T9K6; -.
DR SMR; Q2T9K6; -.
DR PRIDE; Q2T9K6; -.
DR DNASU; 735243; -.
DR GeneID; 735243; -.
DR KEGG; xla:735243; -.
DR CTD; 735243; -.
DR Xenbase; XB-GENE-998532; fem1c.L.
DR OMA; KQTQCPP; -.
DR OrthoDB; 252380at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 735243; Expressed in ovary and 19 other tissues.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
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:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13857; Ank_5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SUPFAM; SSF48403; SSF48403; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 7.
PE 2: Evidence at transcript level;
KW ANK repeat; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..617
FT /note="Protein fem-1 homolog C"
FT /id="PRO_0000324539"
FT REPEAT 2..31
FT /note="ANK 1"
FT REPEAT 40..70
FT /note="ANK 2"
FT REPEAT 82..111
FT /note="ANK 3"
FT REPEAT 115..144
FT /note="ANK 4"
FT REPEAT 148..177
FT /note="ANK 5"
FT REPEAT 181..210
FT /note="ANK 6"
FT REPEAT 213..242
FT /note="ANK 7"
FT REPEAT 245..279
FT /note="TPR 1"
FT REPEAT 338..371
FT /note="TPR 2"
FT REPEAT 481..523
FT /note="ANK 8"
FT REPEAT 527..556
FT /note="ANK 9"
SQ SEQUENCE 617 AA; 68806 MW; 69B7FCF6226D38A6 CRC64;
MDLKTAVFNA ARDGKLRLLS KLLENKAKDD VVLLMSEKTN GATPLLMAAR YGHLDMVDYL
LDQCSASVEI GGSVNFDGET IEGAPPLWAA SAAGHLKVVR SLLVHGASVN NTTLTNSTPL
RAACFDGHLE IVKYLVEHKA DLEVANRHGH TCLMISCYKG HKEIAQFLLE KGADVNRKSV
KGNTALHDCA ESGSLEIMQM LLKYGARMEK DGYGMTPLLS ASVTGHTNIV DFLTQNPQTS
KNERINALEL LGATFVDKKR DLLGALKYWK RAMDMRHSDR TNIVSKPEPQ TLIMAYDYAR
EVNTAEELDN LIADPDEMRM QALLIRERIL GPSHPDTSYY IRYRGAVYAD SGNFKRCINL
WKYALDMQQN NLDPLSPMTA SSLLSFAELF SFMLQDRAKG LLGTTVTFDD LMGILCKSVM
EIDRAVKQTA PPPDQVQLNK ALSIILHLIC LLEKVPCSPD QDHFKKQNIY RFLKLHPKGK
NNFSPLHLAV DKNTTCVGRY PVCKFPSFQV TAILLECGAD VNVRDAEQNS PLHVAALNNH
PDIMNLLVKS GAHFDSTNSH NQTACDLLDE KEMAKNLIQP INHTTLQCLA ARVIVKHNIQ
YKQEIPEKLE SFVLLHR