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FEM1A_DANRE
ID   FEM1A_DANRE             Reviewed;         617 AA.
AC   Q6P9Z4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Protein fem-1 homolog A {ECO:0000305};
DE            Short=FEM1a {ECO:0000305};
DE   AltName: Full=FEM1-alpha {ECO:0000305};
GN   Name=fem1a {ECO:0000250|UniProtKB:Q9BSK4};
GN   ORFNames=zgc:63483 {ECO:0000303|Ref.1};
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 [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-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(FEM1A) 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:Q9BSK4}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9BSK4}.
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:Q9BSK4}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BSK4}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q9BSK4}.
CC   -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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DR   EMBL; BC060522; AAH60522.1; -; mRNA.
DR   RefSeq; NP_956131.1; NM_199837.1.
DR   AlphaFoldDB; Q6P9Z4; -.
DR   SMR; Q6P9Z4; -.
DR   STRING; 7955.ENSDARP00000110111; -.
DR   PaxDb; Q6P9Z4; -.
DR   GeneID; 327613; -.
DR   KEGG; dre:327613; -.
DR   CTD; 55527; -.
DR   ZFIN; ZDB-GENE-030131-5824; fem1a.
DR   eggNOG; KOG0508; Eukaryota.
DR   InParanoid; Q6P9Z4; -.
DR   OrthoDB; 252380at2759; -.
DR   PhylomeDB; Q6P9Z4; -.
DR   Reactome; R-DRE-8951664; Neddylation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q6P9Z4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; 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:0050728; P:negative regulation of inflammatory response; IBA:GO_Central.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; ISS:UniProtKB.
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; 8.
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; Cytoplasm; Mitochondrion; Reference proteome; Repeat;
KW   TPR repeat; Ubl conjugation pathway.
FT   CHAIN           1..617
FT                   /note="Protein fem-1 homolog A"
FT                   /id="PRO_0000324529"
FT   REPEAT          2..32
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          339..372
FT                   /note="TPR 2"
FT   REPEAT          482..524
FT                   /note="ANK 8"
FT   REPEAT          528..557
FT                   /note="ANK 9"
SQ   SEQUENCE   617 AA;  68011 MW;  40C5523DE8BA84BA CRC64;
     MDISAAVFNA ARDGKLKLMQ KLLINKSPEE RAALAEERTE GGTPLLIAAR YGHLPVVHFL
     LERCGANVAL GGSVNFDGET IEGAPPLWAA SAAGHLPVVK ALLEHGAPVN NTTLTNSTPL
     RAACFDGHLE IVRYLVEHQA DLEVANRHGH TCLMISCYKG HREIAQFLLE KGADVNRKSV
     KGNTALHDCA ESGSLEIMKM LLKCDARMER DGYGMTPLLA ASVTGHTNIV EFLVHQPRAS
     REQRIHALEL LGATFVDKKR DLLGAMRYWR RAMELRWAGG QAGALEKPTA GPLVPAYDCS
     REVSTAEELE ALITDPDDMR MQALLVRERI LGPAHPDTSY YIRYRGAVYA DSGNFERCIR
     LWKYALDMQQ SNLEPLSPMT ASSFLSFAEL FSFVLQDRAK GTLAARVSFQ DLMGVLSKSV
     REVERAVAQR ERPPEPPQFS KALSIILHLL FLLQKLRCGP EQEHLKRQTV YRLLKLNPRA
     RGGHTPLHMA VDRDTTSVGR YPVGRFPSLA VASLLLECGA DVDSRDYDNN TPLHIAAANG
     CPDIMAALIR AGAHFDATNA AQQTAYQLLE AQSSGRHALH PLNHTTLQCL AARAVTAHRL
     PYKGLISEQM EAFIELH
 
 
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