FEM1C_DANRE
ID FEM1C_DANRE Reviewed; 618 AA.
AC Q7T3P8; Q6PGZ5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 106.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14527725; DOI=10.1016/s0378-1119(03)00712-1;
RA Ventura-Holman T., Lu D., Si X., Izevbigie E.B., Maher J.F.;
RT "The Fem1c genes: conserved members of the Fem1 gene family in
RT vertebrates.";
RL Gene 314:133-139(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) 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 (1-243) 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; AY249190; AAO64431.1; -; mRNA.
DR EMBL; BC056774; AAH56774.1; -; mRNA.
DR RefSeq; NP_937788.2; NM_198145.2.
DR AlphaFoldDB; Q7T3P8; -.
DR SMR; Q7T3P8; -.
DR STRING; 7955.ENSDARP00000007949; -.
DR PaxDb; Q7T3P8; -.
DR GeneID; 378965; -.
DR KEGG; dre:378965; -.
DR CTD; 56929; -.
DR ZFIN; ZDB-GENE-031008-3; fem1c.
DR eggNOG; KOG0508; Eukaryota.
DR InParanoid; Q7T3P8; -.
DR OrthoDB; 252380at2759; -.
DR PhylomeDB; Q7T3P8; -.
DR Reactome; R-DRE-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7T3P8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
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; 3.
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 ANK repeat; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..618
FT /note="Protein fem-1 homolog C"
FT /id="PRO_0000324538"
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..243
FT /note="ANK 7"
FT REPEAT 245..279
FT /note="TPR 1"
FT REPEAT 337..370
FT /note="TPR 2"
FT REPEAT 482..524
FT /note="ANK 8"
FT REPEAT 528..557
FT /note="ANK 9"
FT CONFLICT 418
FT /note="V -> M (in Ref. 1; AAO64431)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="H -> R (in Ref. 1; AAO64431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 68479 MW; 9366489EBFE25665 CRC64;
MDLKTAVFNA ARDGKLKLLQ KLLENKSDRE VLKLMAEKTN GATPLLMASR YGHLELVEFL
MECCCAPVEL GGSVNFDGEV IEGAPPLWAA SAAGHLKVVQ SLLGHGASVN NTTLTNSTPL
RAACFDGHLD IVRYLVEHQA DLEVANRHGH TCLMISCYKG HREIAQFLLE KGADVNRRSV
KGNTALHDCA ESGSLEIMKM LLKFGASMEK DGYGMTPLLS ASVTGHTNIV DFLTAHPQTG
LAERISALEL LGATFVDKKR DLLGALQYWK RAMELRHSEA DCMRREEPLE PEPAYDCSRE
VSTAEELDGL IADPDDMRMQ ALLIRERILG PAHPDTSYYI RYRGAVYADS GNFERCIRLW
KYALDMQQSN LEPLSPMTAS SLLSFAELFS FMLQDRAKGL LGAGVSFQQL MEILCRSVLE
IERAVKQPRP SPDPDPAQLS KLLSIILHLI CLLEKLPCSP EQDQHKKETI YRFLKLQACG
RNGFSPLHLA VDHNTTCVGR YPVCKFPSLQ VASVLLECGA DVNSRDLDDN SPLHVAASNN
HPDIMKLLIS GGTHFDSTNA LQQTACDLLD HTQLAKSLIQ PINHTTLQCL AARAIIRHRL
VYRGSIPERL EAFVLLHR
