ID   YPEL5_MACFA             Reviewed;         121 AA.
AC   Q4R4Q6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Protein yippee-like 5;
GN   Name=YPEL5; ORFNames=QnpA-18437;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the CTLH E3 ubiquitin-protein ligase complex
CC       that selectively accepts ubiquitin from UBE2H and mediates
CC       ubiquitination and subsequent proteasomal degradation of the
CC       transcription factor HBP1 (By similarity). Required for normal cell
CC       proliferation (By similarity). {ECO:0000250|UniProtKB:P62699,
CC       ECO:0000250|UniProtKB:Q65Z55}.
CC   -!- SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9
CC       and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog
CC       RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA,
CC       RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9
CC       and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and
CC       YPEL5 have ancillary roles. Interacts with RANBP9 and RANBP10.
CC       {ECO:0000250|UniProtKB:P62699}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q65Z55}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q65Z55}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:Q65Z55}. Midbody {ECO:0000250|UniProtKB:Q65Z55}.
CC       Note=Deteted in nucleus and at the centrosome during interphase. During
CC       mitosis, detected on the mitotic spindle, at spindle poles and at the
CC       midbody. {ECO:0000250|UniProtKB:Q65Z55}.
CC   -!- SIMILARITY: Belongs to the yippee family. {ECO:0000305}.
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DR   EMBL; AB169838; BAE01919.1; -; mRNA.
DR   AlphaFoldDB; Q4R4Q6; -.
DR   STRING; 9541.XP_005576276.1; -.
DR   eggNOG; KOG3399; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR   InterPro; IPR034751; Yippee.
DR   InterPro; IPR004910; Yippee/Mis18/Cereblon.
DR   InterPro; IPR039058; Yippee_fam.
DR   PANTHER; PTHR13848; PTHR13848; 1.
DR   Pfam; PF03226; Yippee-Mis18; 1.
DR   PROSITE; PS51792; YIPPEE; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   CHAIN           1..121
FT                   /note="Protein yippee-like 5"
FT                   /id="PRO_0000273969"
FT   DOMAIN          13..110
FT                   /note="Yippee"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01128"
FT   MOD_RES         118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62700"
SQ   SEQUENCE   121 AA;  13812 MW;  FDDE9D519078F870 CRC64;
     MGRIFLDHIG GTRLFSCANC DAILTNRSEL ISTRFTGATG RAFLFNKVVN LQYSEVQDRV
     MLTGRHMVRD VSCKNCNSKL GWIYEFATED SQRYKEGRVI LERALVRESE GFEEHVPSDN
     S