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ZER1_PONAB
ID   ZER1_PONAB              Reviewed;         766 AA.
AC   Q5RAG3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Protein zer-1 homolog;
DE   AltName: Full=Zyg-11 homolog B-like protein;
GN   Name=ZER1; Synonyms=ZYG11BL;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves as substrate adapter subunit in the E3 ubiquitin
CC       ligase complex ZYG11B-CUL2-Elongin BC. Acts redudantly with ZYG11B to
CC       target substrates bearing N-terminal glycine degrons for proteasomal
CC       degradation. Involved in the clearance of proteolytic fragments
CC       generated by caspase cleavage during apoptosis since N-terminal glycine
CC       degrons are strongly enriched at caspase cleavage sites. Also important
CC       in the quality control of protein N-myristoylation in which N-terminal
CC       glycine degrons are conditionally exposed after a failure of N-
CC       myristoylation. {ECO:0000250|UniProtKB:Q7Z7L7}.
CC   -!- SUBUNIT: Interacts with the ELOC-ELOB/Elongin BC complex. Part of an E3
CC       ubiquitin ligase complex including ZER1, CUL2 and Elongin BC (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zyg-11 family. {ECO:0000305}.
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DR   EMBL; CR859054; CAH91247.1; -; mRNA.
DR   RefSeq; NP_001125736.1; NM_001132264.1.
DR   AlphaFoldDB; Q5RAG3; -.
DR   SMR; Q5RAG3; -.
DR   STRING; 9601.ENSPPYP00000022035; -.
DR   PRIDE; Q5RAG3; -.
DR   GeneID; 100172661; -.
DR   KEGG; pon:100172661; -.
DR   CTD; 10444; -.
DR   eggNOG; KOG3665; Eukaryota.
DR   InParanoid; Q5RAG3; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR040368; Zer-1.
DR   PANTHER; PTHR12904:SF23; PTHR12904:SF23; 1.
DR   SMART; SM00185; ARM; 4.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Leucine-rich repeat; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z7L7"
FT   CHAIN           2..766
FT                   /note="Protein zer-1 homolog"
FT                   /id="PRO_0000066600"
FT   REPEAT          226..245
FT                   /note="LRR 1"
FT   REPEAT          246..268
FT                   /note="LRR 2"
FT   REPEAT          278..302
FT                   /note="LRR 3"
FT   REPEAT          427..467
FT                   /note="ARM 1"
FT   REPEAT          511..556
FT                   /note="ARM 2"
FT   REPEAT          558..600
FT                   /note="ARM 3"
FT   REPEAT          602..643
FT                   /note="ARM 4"
FT   REPEAT          714..756
FT                   /note="ARM 5"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z7L7"
SQ   SEQUENCE   766 AA;  88152 MW;  05902603A0E12867 CRC64;
     MASDTPESLM ALCTDFCLRN LDGTLGYLLD KETLRLHPDI FLPSEICDRL VNEYVELVNA
     ACNFEPHESF FSLFSDPRST RLTRIHLRED LVQDQDLEAI RKQDLVELYL TNCEKLSAKS
     LQTLRSFSHT LVSLSLFGCT NIFYEEENPG GCEDEYLVNP TCQVLVKDFT FEGFSRLRFL
     NLGRMIDWVP VESLLRPLNS LAALDLSGIQ TSDAAFLTQW KDSLVSLVLY NMDLSDDHIR
     VIVQLHKLRH LDISRDRLSS YYKFKLTREV LSLFVQKLGN LMSLDISGHM ILENCSISKM
     EEEAGQTSIE PSKSSIIPFR ALKRPLQFLG LFENSLCRLT HIPAYKVSGD KNEEQVLNAI
     EAYTEHRPEI TSRAINLLFD IARIERCNQL LRALKLVITA LKCHKYDRNI QVTGSAALFY
     LTNSEYRSEQ SVKLRRQVIQ VVLNGMESYQ EVTVQRNCCL TLCNFGIPEE LEFQYRRVNE
     LLLSILNPTR QDESIQRIAV HLCNALVCQV DNDHKEAVGK MGFVVTMLKL IQKKLLDKIC
     DQVMEFSWSA LWNITDETPD NCEMFLNFNG MKLFLDCLKE FPEKQELHRN MLGLLGNVAE
     VKELRPQLMT SQFISVFSNL LESKADGIEV SYNACGVLSH IMFDGPEAWG VCEPQREEVE
     ERMWAAIQSW DINSRRNINY RSFEPILRLL PQGISPVSQH WATWALYNLV SVYPDKYCPL
     LIKEGGMPLL RDIIKMATAR QETKEMARKV IEHCSNFKEE NMDTSR
 
 
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