HINT1_BOVIN
ID HINT1_BOVIN Reviewed; 126 AA.
AC P62958; P16436; Q3T060;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
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 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 [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 MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-126, AND ACETYLATION AT ALA-2.
RX PubMed=2307677; DOI=10.1016/s0021-9258(19)39603-6;
RA Pearson J.D., Dewald D.B., Mathews W.R., Mozier N.M., Zurcher-Neely H.A.,
RA Heinrikson R.L., Morris M.A., McCubbin W.D., McDonald J.R., Fraser E.D.,
RA Vogel H.J., Kay C.M., Walsh M.P.;
RT "Amino acid sequence and characterization of a protein inhibitor of protein
RT kinase C.";
RL J. Biol. Chem. 265:4583-4591(1990).
RN [4]
RP PUTATIVE ZINC-BINDING DOMAIN.
RX PubMed=1899836; DOI=10.1016/0014-5793(91)80238-x;
RA Mozier N.M., Walsh M.P., Pearson J.D.;
RT "Characterization of a novel zinc binding site of protein kinase C
RT inhibitor-1.";
RL FEBS Lett. 279:14-18(1991).
RN [5]
RP SIMILARITY TO OTHER MEMBERS OF THE HIT FAMILY.
RX PubMed=1472710; DOI=10.3109/10425179209034013;
RA Seraphin B.;
RT "The HIT protein family: a new family of proteins present in prokaryotes,
RT yeast and mammals.";
RL DNA Seq. 3:177-179(1992).
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 -!- TISSUE SPECIFICITY: Widely expressed.
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}.
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DR EMBL; U09405; AAA18396.1; -; mRNA.
DR EMBL; BC102553; AAI02554.1; -; mRNA.
DR PIR; A35350; A35350.
DR RefSeq; NP_787006.1; NM_175812.2.
DR AlphaFoldDB; P62958; -.
DR SMR; P62958; -.
DR STRING; 9913.ENSBTAP00000014552; -.
DR iPTMnet; P62958; -.
DR PaxDb; P62958; -.
DR PeptideAtlas; P62958; -.
DR PRIDE; P62958; -.
DR GeneID; 327693; -.
DR KEGG; bta:327693; -.
DR CTD; 3094; -.
DR eggNOG; KOG3275; Eukaryota.
DR HOGENOM; CLU_056776_8_1_1; -.
DR InParanoid; P62958; -.
DR OrthoDB; 1190598at2759; -.
DR TreeFam; TF314862; -.
DR Proteomes; UP000009136; Unplaced.
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: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:0000269|PubMed:2307677"
FT CHAIN 2..126
FT /note="Adenosine 5'-monophosphoramidase HINT1"
FT /id="PRO_0000109780"
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:0000269|PubMed:2307677"
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 62
FT /note="Q -> E (in Ref. 2; AAA18396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 126 AA; 13779 MW; 1E1CA1AC3F59152D CRC64;
MADEIAKAQV ARPGGDTIFG KIIRKEIPAK IIYEDDQCLA FHDISPQAPT HFLVIPKKYI
SQISAAEDDD ESLLGHLMIV GKKCAADLGL KKGYRMVVNE GSDGGQSVYH VHLHVLGGRQ
MNWPPG
