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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
 
 
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