TMUB1_RAT
ID TMUB1_RAT Reviewed; 245 AA.
AC Q53AQ4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Transmembrane and ubiquitin-like domain-containing protein 1;
DE AltName: Full=Hepatocyte odd protein shuttling protein;
DE Contains:
DE RecName: Full=iHOPS {ECO:0000303|PubMed:24240191};
GN Name=Tmub1; Synonyms=Hops;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=16014383; DOI=10.1242/jcs.02452;
RA Della Fazia M.A., Castelli M., Bartoli D., Pieroni S., Pettirossi V.,
RA Piobbico D., Viola-Magni M., Servillo G.;
RT "HOPS: a novel cAMP-dependent shuttling protein involved in protein
RT synthesis regulation.";
RL J. Cell Sci. 118:3185-3194(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TUBG1.
RX PubMed=18418082; DOI=10.4161/cc.7.10.5882;
RA Pieroni S., Della Fazia M.A., Castelli M., Piobbico D., Bartoli D.,
RA Brunacci C., Bellet M.M., Viola-Magni M., Servillo G.;
RT "HOPS is an essential constituent of centrosome assembly.";
RL Cell Cycle 7:1462-1466(2008).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18665261; DOI=10.1371/journal.pone.0002809;
RA Yang H., Takagi H., Konishi Y., Ageta H., Ikegami K., Yao I., Sato S.,
RA Hatanaka K., Inokuchi K., Seog D.H., Setou M.;
RT "Transmembrane and ubiquitin-like domain-containing protein 1 (Tmub1/HOPS)
RT facilitates surface expression of GluR2-containing AMPA receptors.";
RL PLoS ONE 3:E2809-E2809(2008).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAMLG.
RX PubMed=22426572; DOI=10.3892/ijmm.2012.939;
RA Liu M., Liu H., Wang X., Chen P., Chen H.;
RT "IL-6 induction of hepatocyte proliferation through the Tmub1-regulated
RT gene pathway.";
RL Int. J. Mol. Med. 29:1106-1112(2012).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NPM1 AND CDKN2A.
RX PubMed=22890319; DOI=10.1038/onc.2012.353;
RA Castelli M., Pieroni S., Brunacci C., Piobbico D., Bartoli D., Bellet M.M.,
RA Colombo E., Pelicci P.G., Della Fazia M.A., Servillo G.;
RT "Hepatocyte odd protein shuttling (HOPS) is a bridging protein in the
RT nucleophosmin-p19 Arf network.";
RL Oncogene 32:3350-3358(2013).
RN [7]
RP SUBCELLULAR LOCATION (IHOPS), AND PROTEOLYTIC CLEAVAGE (IHOPS).
RX PubMed=24240191; DOI=10.4161/cc.27054;
RA Castelli M., Piobbico D., Bartoli D., Pieroni S., Brunacci C., Bellet M.M.,
RA Chiacchiaretta M., Della Fazia M.A., Servillo G.;
RT "Different functions of HOPS isoforms in the cell: HOPS shuttling isoform
RT is determined by RIP cleavage system.";
RL Cell Cycle 13:293-302(2014).
CC -!- FUNCTION: Involved in sterol-regulated ubiquitination and degradation
CC of HMG-CoA reductase HMGCR (By similarity). Involved in positive
CC regulation of AMPA-selective glutamate receptor GRIA2 recycling to the
CC cell surface (PubMed:18665261). Acts as negative regulator of
CC hepatocyte growth during regeneration (PubMed:22426572).
CC {ECO:0000250|UniProtKB:Q9BVT8, ECO:0000250|UniProtKB:Q9JMG3,
CC ECO:0000269|PubMed:18665261, ECO:0000269|PubMed:22426572}.
CC -!- FUNCTION: [iHOPS]: May contribute to the regulation of translation
CC during cell-cycle progression. May contribute to the regulation of cell
CC proliferation (By similarity). May be involved in centrosome assembly.
CC Modulates stabilization and nucleolar localization of tumor suppressor
CC CDKN2A and enhances association between CDKN2A and NPM1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9JMG3}.
CC -!- SUBUNIT: Interacts with EEF1A1, GRIA2, GRIP1 (By similarity). Interacts
CC with CAMLG, TUBG1. Interacts with NPM1 and CDKN2A; TMUB1 can enhance
CC interaction between NPM1 and CDKN2A and is proposed to bridge the
CC proteins; proposed to be mediated by iHOPS (PubMed:18418082,
CC PubMed:22426572, PubMed:22890319). Interacts with ERLIN2 and AMFR;
CC TMUB1 promotes the interaction of ERLIN2 with AMFR (By similarity).
CC {ECO:0000250|UniProtKB:Q9BVT8, ECO:0000250|UniProtKB:Q9JMG3,
CC ECO:0000269|PubMed:18418082, ECO:0000269|PubMed:22426572,
CC ECO:0000269|PubMed:22890319}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:24240191,
CC ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Postsynaptic
CC cell membrane {ECO:0000250|UniProtKB:Q9JMG3}. Recycling endosome
CC {ECO:0000269|PubMed:18665261}. Cytoplasm {ECO:0000269|PubMed:16014383,
CC ECO:0000269|PubMed:22426572}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:18418082}. Nucleus
CC {ECO:0000269|PubMed:16014383}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:22890319}. Note=Localized to neuronal soma and
CC dendrites (PubMed:18665261). {ECO:0000269|PubMed:18665261}.
CC -!- SUBCELLULAR LOCATION: [iHOPS]: Cytoplasm {ECO:0000250|UniProtKB:Q9JMG3,
CC ECO:0000269|PubMed:24240191}. 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 (By similarity).
CC XPO1-dependent exported from the nucleus in dividing cells.
CC Predominantly nuclear during growth arrest (PubMed:16014383).
CC {ECO:0000250|UniProtKB:Q9JMG3, ECO:0000269|PubMed:16014383}.
CC -!- INDUCTION: Up-regulated in regenerating liver.
CC {ECO:0000269|PubMed:16014383}.
CC -!- PTM: [iHOPS]: Processed by regulated intramembrane proteolysis (RIP) in
CC the N-terminus to release iHOPS from membranes.
CC {ECO:0000269|PubMed:24240191}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY603378; AAU00154.1; -; mRNA.
DR EMBL; CH474020; EDL99355.1; -; Genomic_DNA.
DR RefSeq; NP_001073622.1; NM_001080153.2.
DR RefSeq; NP_942076.2; NM_198781.3.
DR RefSeq; XP_006236007.1; XM_006235945.3.
DR AlphaFoldDB; Q53AQ4; -.
DR SMR; Q53AQ4; -.
DR BioGRID; 263349; 2.
DR IntAct; Q53AQ4; 2.
DR STRING; 10116.ENSRNOP00000058703; -.
DR iPTMnet; Q53AQ4; -.
DR PhosphoSitePlus; Q53AQ4; -.
DR PaxDb; Q53AQ4; -.
DR PRIDE; Q53AQ4; -.
DR GeneID; 362301; -.
DR KEGG; rno:362301; -.
DR CTD; 83590; -.
DR RGD; 735120; Tmub1.
DR VEuPathDB; HostDB:ENSRNOG00000013383; -.
DR eggNOG; ENOG502QU8U; Eukaryota.
DR InParanoid; Q53AQ4; -.
DR OMA; AWISTHT; -.
DR OrthoDB; 1164744at2759; -.
DR PhylomeDB; Q53AQ4; -.
DR TreeFam; TF329265; -.
DR PRO; PR:Q53AQ4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Proteomes; UP000234681; Chromosome 4.
DR Bgee; ENSRNOG00000013383; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q53AQ4; RN.
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; ISO:RGD.
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 SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Endosome; Membrane; Nucleus;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..245
FT /note="Transmembrane and ubiquitin-like domain-containing
FT protein 1"
FT /id="PRO_0000370251"
FT CHAIN ?..245
FT /note="iHOPS"
FT /id="PRO_0000435490"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 102..175
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 34..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
SQ SEQUENCE 245 AA; 26349 MW; A83B3C4AB6C992A0 CRC64;
MALIEGVGDE VTVLFSVLAC LLVLALAWVS THTTESTDPL PQSSGTTTPA QPSEAMTAID
SIREEAPGAE SPSLRHRGPS AQPEPEAGVT ASTPPDSPQE PLLLRLKFLN DSEQVARAWP
QDTIGSLKRT QFPGREQQVR LIYQGQLLGD DTQTLGSLHL PPNCVLHCHV STRVGPPHPP
CPPGSEPGPS GLEIGSLLLP LLLLLLLLLW YCQIQYRPFF PLTATLGLAG FTLLLSLLAF
AMYRP
