FEM1C_BOVIN
ID FEM1C_BOVIN Reviewed; 617 AA.
AC A7MB89;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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, such as SIL1 or OR51B2,
CC leading to their ubiquitination and degradation. The CRL2(FEM1C)
CC complex mediates ubiquitination and degradation of truncated
CC MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding.
CC {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, composed of
CC CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC FEM1C. {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; BC151399; AAI51400.1; -; mRNA.
DR RefSeq; NP_001094689.1; NM_001101219.1.
DR RefSeq; XP_005211271.1; XM_005211214.3.
DR RefSeq; XP_010807137.1; XM_010808835.2.
DR RefSeq; XP_010807138.1; XM_010808836.2.
DR AlphaFoldDB; A7MB89; -.
DR SMR; A7MB89; -.
DR STRING; 9913.ENSBTAP00000011464; -.
DR PaxDb; A7MB89; -.
DR PRIDE; A7MB89; -.
DR Ensembl; ENSBTAT00000011464; ENSBTAP00000011464; ENSBTAG00000008699.
DR GeneID; 541180; -.
DR KEGG; bta:541180; -.
DR CTD; 56929; -.
DR VEuPathDB; HostDB:ENSBTAG00000008699; -.
DR VGNC; VGNC:28946; FEM1C.
DR eggNOG; KOG0508; Eukaryota.
DR GeneTree; ENSGT00940000158626; -.
DR HOGENOM; CLU_020042_2_0_1; -.
DR InParanoid; A7MB89; -.
DR OMA; KQTQCPP; -.
DR OrthoDB; 252380at2759; -.
DR TreeFam; TF351376; -.
DR Reactome; R-BTA-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000008699; Expressed in spermatid and 104 other tissues.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
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:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; 2.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13857; Ank_5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 7.
PE 2: Evidence at transcript level;
KW Acetylation; 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_0000324535"
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"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96JP0"
SQ SEQUENCE 617 AA; 68700 MW; 3B18B39ACC48636C CRC64;
MDLKTAVFNA ARDGKLRLLT KLLASKSKEE VSSLISEKTN GATPLLMAAR YGHLDMVEFL
LEQCSASIEV GGSVNFDGET IEGAPPLWAA SAAGHLKVVQ SLLNHGASVN NTTLTNSTPL
RAACFDGHLE IVKYLVEHKA DLEVSNRHGH TCLMISCYKG HKEIAQYLLE KGADVNRKSV
KGNTALHDCA ESGSLDIMKM LLMYCAKMEK DGYGMTPLLS ASVTGHTNIV DFLTHHAQTS
KTERINALEL LGATFVDKKR DLLGALKYWK KAMNMRYSDR TNIISKPVPQ TLIMAYDYAK
EVNSAEELEG LIADPDEMRM QALLIRERIL GPSHPDTSYY IRYRGAVYAD SGNFKRCINL
WKYALDMQQN NLDPLSPMTA SSLLSFAELF SFMLQDRAKG LLGTTVTFDD LMGILCKSVL
EIERAIKQTQ CPADPLQLNK ALSIILHLIC LLEKVPCTLE QDHFKKQTIY RFLKLHPRGK
NNFSPLHLAV DKNTTCVGRY PVCKFPSLQV TAILIECGAD VNVRDSDDNS PLHIAALNNH
PDIMNLLIKS GAHFDATNLH KQTASDLLDE KEIAKNLIQP INHTTLQCLA ARVIVNHRIY
YKGHIPEKLE TFVSLHR
