TMUB1_BOVIN
ID TMUB1_BOVIN Reviewed; 246 AA.
AC Q3ZBI9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Transmembrane and ubiquitin-like domain-containing protein 1;
DE Contains:
DE RecName: Full=iHOPS;
GN Name=TMUB1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in sterol-regulated ubiquitination and degradation
CC of HMG-CoA reductase HMGCR. Involved in positive regulation of AMPA-
CC selective glutamate receptor GRIA2 recycling to the cell surface. Acts
CC as negative regulator of hepatocyte growth during regeneration.
CC {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000250|UniProtKB:Q9BVT8,
CC ECO:0000250|UniProtKB:Q9JMG3}.
CC -!- FUNCTION: [iHOPS]: May contribute to the regulation of translation
CC during cell-cycle progression. May contribute to the regulation of cell
CC proliferation. May be involved in centrosome assembly. Modulates
CC stabilization and nucleolar localization of tumor suppressor CDKN2A and
CC enhances association between CDKN2A and NPM1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JMG3}.
CC -!- SUBUNIT: Interacts with EEF1A1, GRIA2, GRIP1, CAMLG, TUBG1. Interacts
CC with NPM1 and CDKN2A; TMUB1 can enhance interaction between NPM1 and
CC CDKN2A and is proposed to bridge the proteins; proposed to be mediated
CC by iHOPS. Interacts with ERLIN2 and AMFR; TMUB1 promotes the
CC interaction of ERLIN2 with AMFR (By similarity).
CC {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000250|UniProtKB:Q9BVT8,
CC ECO:0000250|UniProtKB:Q9JMG3}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9JMG3}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q9JMG3}. Postsynaptic cell
CC membrane {ECO:0000250|UniProtKB:Q9JMG3}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q53AQ4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9JMG3}. Nucleus {ECO:0000250|UniProtKB:Q9JMG3}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9JMG3}.
CC -!- SUBCELLULAR LOCATION: [iHOPS]: Cytoplasm {ECO:0000250|UniProtKB:Q53AQ4,
CC ECO:0000250|UniProtKB:Q9JMG3}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9JMG3}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q9JMG3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9JMG3}. Note=iHOPS is proposed to be the
CC shuttling form across different cellular compartments. XPO1-dependent
CC exported from the nucleus in dividing cells. Predominantly nuclear
CC during growth arrest. {ECO:0000250|UniProtKB:Q9JMG3}.
CC -!- PTM: [iHOPS]: Processed by regulated intramembrane proteolysis (RIP) in
CC the N-terminus to release iHOPS from membranes.
CC {ECO:0000250|UniProtKB:Q9JMG3}.
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DR EMBL; BC103270; AAI03271.1; -; mRNA.
DR RefSeq; NP_001029847.1; NM_001034675.1.
DR AlphaFoldDB; Q3ZBI9; -.
DR SMR; Q3ZBI9; -.
DR STRING; 9913.ENSBTAP00000014915; -.
DR PaxDb; Q3ZBI9; -.
DR PRIDE; Q3ZBI9; -.
DR GeneID; 539388; -.
DR KEGG; bta:539388; -.
DR CTD; 83590; -.
DR eggNOG; ENOG502QU8U; Eukaryota.
DR HOGENOM; CLU_053940_1_0_1; -.
DR InParanoid; Q3ZBI9; -.
DR OrthoDB; 1164744at2759; -.
DR TreeFam; TF329265; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR040352; TMUB1/2.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR14557; PTHR14557; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Endosome; Membrane; Nucleus;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..246
FT /note="Transmembrane and ubiquitin-like domain-containing
FT protein 1"
FT /id="PRO_0000246184"
FT CHAIN ?..246
FT /note="iHOPS"
FT /evidence="ECO:0000250|UniProtKB:Q9JMG3"
FT /id="PRO_0000435487"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 103..176
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 2..30
FT /note="Required to release iHOPS from membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9JMG3"
FT REGION 35..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
SQ SEQUENCE 246 AA; 26206 MW; 3560ED8F4EBA9EF7 CRC64;
MALIEGVGDE VTILFSALAC LLVLALAWVS THTAEGADPL PQPSGTPTPT QPSEAMAVTD
SIRGEAPGAE TPGLRHRGQA APPEPSVGLA ATPPPPDSPQ EPLVLRLKFL NDSEQVARAW
PHDTIGSLKR TQFPGREQHV RLIYQGQLLG DDTQTLGSLH LPPNCVLHCH VSTRVGPPLP
PCPPGSEPGP SGLEVGSLLL PLLLLLLLLL WYCQIQYRPF FPLTATLGLA GFTLLLSLLA
FAMYRP
