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FEM1B_CHICK
ID   FEM1B_CHICK             Reviewed;         627 AA.
AC   Q5ZM55;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Protein fem-1 homolog B {ECO:0000305};
DE            Short=FEM1b {ECO:0000250|UniProtKB:Q9UK73};
DE   AltName: Full=FEM1-beta;
GN   Name=FEM1B {ECO:0000250|UniProtKB:Q9UK73};
GN   ORFNames=RCJMB04_3b14 {ECO:0000303|PubMed:15642098};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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(FEM1B) complex specifically recognizes proteins ending with -Gly-
CC       Leu-Asp-Arg, leading to their ubiquitination and degradation.
CC       {ECO:0000250|UniProtKB:Q9UK73}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9UK73}.
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:Q9UK73}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UK73}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9UK73}.
CC   -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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DR   EMBL; AJ719529; CAG31188.1; -; mRNA.
DR   RefSeq; NP_001025724.1; NM_001030553.1.
DR   AlphaFoldDB; Q5ZM55; -.
DR   SMR; Q5ZM55; -.
DR   STRING; 9031.ENSGALP00000042401; -.
DR   GeneID; 415559; -.
DR   KEGG; gga:415559; -.
DR   CTD; 10116; -.
DR   VEuPathDB; HostDB:geneid_415559; -.
DR   eggNOG; KOG0508; Eukaryota.
DR   InParanoid; Q5ZM55; -.
DR   OrthoDB; 252380at2759; -.
DR   PhylomeDB; Q5ZM55; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5ZM55; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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:2000001; P:regulation of DNA damage checkpoint; ISS:UniProtKB.
DR   GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; ISS:UniProtKB.
DR   Gene3D; 1.25.40.20; -; 3.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
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; 6.
PE   2: Evidence at transcript level;
KW   ANK repeat; Apoptosis; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW   TPR repeat; Ubl conjugation pathway.
FT   CHAIN           1..627
FT                   /note="Protein fem-1 homolog B"
FT                   /id="PRO_0000324533"
FT   REPEAT          45..74
FT                   /note="ANK 1"
FT   REPEAT          87..116
FT                   /note="ANK 2"
FT   REPEAT          120..149
FT                   /note="ANK 3"
FT   REPEAT          153..182
FT                   /note="ANK 4"
FT   REPEAT          186..215
FT                   /note="ANK 5"
FT   REPEAT          218..248
FT                   /note="ANK 6"
FT   REPEAT          344..377
FT                   /note="TPR"
FT   REPEAT          483..527
FT                   /note="ANK 7"
FT   REPEAT          531..568
FT                   /note="ANK 8"
SQ   SEQUENCE   627 AA;  70394 MW;  8B31106D0DAE0708 CRC64;
     MEGLAGYVYK AASEGRVLTL AALLLNRSES DIKYLLGYVS QHGGQRSTPL IIAARNGHTK
     VVRLLLEHYR VQTQQTGTVR FDGFVIDGAT ALWCAAGAGH FEVVKLLVSH GANVNHTTVT
     NSTPLRAACF DGRLDIVKYL VENNANISIA NKYDNTCLMI AAYKGHTDVV RYLLEQHADP
     NAKAHCGATA LHFAAEAGHL EIVRELVKWK AAMMVNGHGM TPLKVAAESC KADVVELLLA
     HAGCNRRSRI EALELLGASF ANDRENYDIM KTYHYLYLAM LERYRDSENI IEKEVLPPIE
     AYGNRTECRT PQELESIRQD RDALHMEGLI VRERILGSDN IDVSHPIIYR GAVYADNMEF
     EQCIKLWLHA LHLRQKGNRN THKDLLRFAQ VFSQMIHLNE PVKAKDIESV LRCSVLEIEQ
     GMSRIKATQD DDIHTAVDNY ECNIFTFLYL VCISTKTQCS EEDQSRINKQ IYNLIHLDPR
     TRDGSTLLHH AVNSSTPVDD FHTNDVCSFP NALVTKLLLD CGADVNAVDN EGNSPLHLIV
     QYHRPISDFL TLHSIIISLV EAGAHTDMTN KQKKTPLDKS TTGVSEILLK TQMKLSLKCL
     AARAVRIYNI SYQNQIPRTL EEFVKFH
 
 
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