HINT1_RAT
ID HINT1_RAT Reviewed; 126 AA.
AC P62959; B5DEM9; P16436;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 5.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Adenosine 5'-monophosphoramidase HINT1 {ECO:0000250|UniProtKB:P49773};
DE EC=3.9.1.- {ECO:0000250|UniProtKB:P49773};
DE AltName: Full=17 kDa inhibitor of protein kinase C;
DE AltName: Full=Desumoylating isopeptidase HINT1 {ECO:0000250|UniProtKB:P49773};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:P49773};
DE AltName: Full=Histidine triad nucleotide-binding protein 1;
DE AltName: Full=Protein kinase C inhibitor 1;
DE AltName: Full=Protein kinase C-interacting protein 1;
DE Short=PKCI-1;
GN Name=Hint1; Synonyms=Hint, Pkci1;
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].
RC TISSUE=Hypothalamus;
RA Waller S.J., Murphy D.;
RT "Cloning of a putative inhibitor of protein kinase C from several
RT species.";
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 31-37.
RC STRAIN=Wistar; TISSUE=Liver;
RA Negoro M., Wakabayashi I.;
RT "Purification of PKCI from rat liver.";
RL Submitted (JUN-2003) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 37-57; 58-82 AND 96-119, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Chen W.-Q., Diao W., Afjehi-Sadat L.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (DEC-2008) to UniProtKB.
CC -!- FUNCTION: Exhibits adenosine 5'-monophosphoramidase activity,
CC hydrolyzing purine nucleotide phosphoramidates with a single phosphate
CC group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP
CC and NH2 (By similarity). Hydrolyzes adenosine 5'monophosphomorpholidate
CC (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-
CC morpholidate) (By similarity). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-
CC alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as
CC well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-
CC alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester (By
CC similarity). Can also convert adenosine 5'-O-phosphorothioate and
CC guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O-
CC phosphates with concomitant release of hydrogen sulfide (By
CC similarity). In addition, functions as scaffolding protein that
CC modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex
CC and by the complex formed with MITF and CTNNB1 (By similarity).
CC Modulates p53/TP53 levels and p53/TP53-mediated apoptosis. Modulates
CC proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex (By similarity). Also
CC exhibits SUMO-specific isopeptidase activity, deconjugating SUMO1 from
CC RANGAP1 and RGS17 (By similarity). {ECO:0000250|UniProtKB:P49773,
CC ECO:0000250|UniProtKB:P70349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+);
CC Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57890, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:P49773};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with CDK7 (By
CC similarity). Interacts with RUVBL1 and RUVBL2 and is associated with
CC the LEF1/TCF1-CTNNB1 complex and with a KAT5 histone acetyltransferase
CC complex (By similarity). Identified in a complex with MITF and CTNNB1
CC (By similarity). Interacts with CDC34 and RBX1, and is part of a SCF
CC (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (By
CC similarity). Interacts with SUMO1, SUMO2 and RGS17 (By similarity).
CC Interacts with the Ten-1 ICD form of TENM1 (By similarity). Interacts
CC with CALM1; interaction increases in the presence of calcium ions (By
CC similarity). {ECO:0000250|UniProtKB:P49773,
CC ECO:0000250|UniProtKB:P70349}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49773}. Nucleus
CC {ECO:0000250|UniProtKB:P49773}.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a protein kinase C inhibitor and
CC to bind zinc in solution. Both seem to be incorrect. {ECO:0000305}.
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; U09407; AAA18398.1; -; mRNA.
DR EMBL; CH473948; EDM04446.1; -; Genomic_DNA.
DR EMBL; BC168732; AAI68732.1; -; mRNA.
DR PIR; A59489; A59489.
DR RefSeq; NP_001103077.1; NM_001109607.1.
DR AlphaFoldDB; P62959; -.
DR BMRB; P62959; -.
DR SMR; P62959; -.
DR BioGRID; 605472; 1.
DR CORUM; P62959; -.
DR IntAct; P62959; 1.
DR MINT; P62959; -.
DR STRING; 10116.ENSRNOP00000000772; -.
DR BindingDB; P62959; -.
DR iPTMnet; P62959; -.
DR PhosphoSitePlus; P62959; -.
DR SwissPalm; P62959; -.
DR jPOST; P62959; -.
DR PaxDb; P62959; -.
DR PRIDE; P62959; -.
DR GeneID; 690660; -.
DR KEGG; rno:690660; -.
DR CTD; 3094; -.
DR RGD; 1593411; Hint1.
DR eggNOG; KOG3275; Eukaryota.
DR HOGENOM; CLU_056776_8_1_1; -.
DR InParanoid; P62959; -.
DR OMA; YHLHAHL; -.
DR OrthoDB; 1190598at2759; -.
DR PhylomeDB; P62959; -.
DR TreeFam; TF314862; -.
DR PRO; PR:P62959; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000000622; Expressed in duodenum and 19 other tissues.
DR Genevisible; P62959; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; ISS:UniProtKB.
DR GO; GO:0016929; F:deSUMOylase activity; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:RGD.
DR GO; GO:0016926; P:protein desumoylation; ISS:UniProtKB.
DR GO; GO:0009154; P:purine ribonucleotide catabolic process; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR23089; PTHR23089; 1.
DR Pfam; PF01230; HIT; 1.
DR PRINTS; PR00332; HISTRIAD.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Transcription; Transcription regulation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62958"
FT CHAIN 2..126
FT /note="Adenosine 5'-monophosphoramidase HINT1"
FT /id="PRO_0000109784"
FT DOMAIN 18..126
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 110..114
FT /note="Histidine triad motif"
FT ACT_SITE 112
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 43..44
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 99
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 105..107
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 112..114
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P62958"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70349"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70349"
FT CONFLICT 12
FT /note="Q -> R (in Ref. 1; AAA18398)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="F -> Y (in Ref. 1; AAA18398)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="R -> Q (in Ref. 1; AAA18398)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="H -> Y (in Ref. 1; AAA18398)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="V -> A (in Ref. 1; AAA18398)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="D -> E (in Ref. 1; AAA18398)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="R -> K (in Ref. 1; AAA18398)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="A -> S (in Ref. 1; AAA18398)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="I -> V (in Ref. 1; AAA18398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 126 AA; 13777 MW; 30DA241476389805 CRC64;
MADEIAKAQV AQPGGDTIFG KIIRKEIPAK IIFEDDRCLA FHDISPQAPT HFLVIPKKHI
SQISVADDDD ESLLGHLMIV GKKCAADLGL KRGYRMVVNE GADGGQSVYH IHLHVLGGRQ
MNWPPG
