MIDNA_XENLA
ID MIDNA_XENLA Reviewed; 453 AA.
AC Q7ZWN4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Midnolin-A;
DE AltName: Full=Midbrain nucleolar protein A;
GN Name=midn-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Facilitates ubiquitin-independent proteasomal degradation of
CC polycomb protein CBX4. Plays a role in inhibiting the activity of
CC glucokinase GCK and both glucose-induced and basal insulin secretion.
CC {ECO:0000250|UniProtKB:D4AE48, ECO:0000250|UniProtKB:Q3TPJ7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3TPJ7}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q3TPJ7}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q3TPJ7}. Note=Detected in the nucleus and
CC nucleolus with no expression in the cytoplasm. However, a later study
CC finds expression in the nucleus and cytoplasm with no expression in the
CC nucleolus. {ECO:0000250|UniProtKB:Q3TPJ7}.
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DR EMBL; BC046865; AAH46865.1; -; mRNA.
DR RefSeq; NP_001079678.1; NM_001086209.1.
DR AlphaFoldDB; Q7ZWN4; -.
DR SMR; Q7ZWN4; -.
DR DNASU; 379365; -.
DR GeneID; 379365; -.
DR KEGG; xla:379365; -.
DR CTD; 379365; -.
DR Xenbase; XB-GENE-1005239; midn.L.
DR OMA; EANCSTN; -.
DR OrthoDB; 1159802at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 379365; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR InterPro; IPR039336; Midnolin.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23010; PTHR23010; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..453
FT /note="Midnolin-A"
FT /id="PRO_0000287539"
FT DOMAIN 20..94
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 184..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 49543 MW; 899816BABC82FD24 CRC64;
MEQQPSVPRS CTNVARETPM NLNIQSTTGT RYELSVPPDE TVDGLKRRIS QRLKVPKDRL
TLLHRETRLS SGKLQDLGIS DGSRLTLLPS VEAGLMSQMS RPEQSVMQAL ESLTETQVND
FLSGRSPLTL ALRVGDHMMF VQLQLAAQQS GSSHLQHRHV ITRGAETSAS PQYRTLHTST
SAVSHLASCT PGPTPPTTLS PTSSTHCNGP HSSPLTTSVF RSHGEGVAVS PCAEQAPCST
RGTEGTSSSP SSRSRKPGAI IESFVNHAPG VFSGTFSGTL HPQCQDSAGR PRRDIGTILQ
ILNDLLSATR HYQGMPPSLT TLRCHTQCAS QARNAKATSP QSTSPQQTTH PVGHCQTQTR
TYKPSGDRLR QTENRATRCK VERLQLLMHQ KRLRRKARRD SRAPYHWMPT RKSSRTSSNS
STSSGEGSLE IDFEDSLWKP DVKAELNSEF VVA