HINT3_MOUSE
ID HINT3_MOUSE Reviewed; 165 AA.
AC Q9CPS6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Adenosine 5'-monophosphoramidase HINT3 {ECO:0000250|UniProtKB:Q9NQE9};
DE EC=3.9.1.- {ECO:0000250|UniProtKB:Q9NQE9};
DE AltName: Full=HINT-4;
DE AltName: Full=Histidine triad nucleotide-binding protein 3;
DE Short=HINT-3;
GN Name=Hint3; Synonyms=Hint4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Huang C.-H., Chen H., Peng J., Chen Y.;
RT "Conservation of the fourth member of the histidine triad protein family
RT (Hint-4) in rat and mouse.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH CALM1.
RX PubMed=31088288; DOI=10.1089/ars.2019.7724;
RA Cortes-Montero E., Rodriguez-Munoz M., Sanchez-Blazquez P., Garzon J.;
RT "The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and
RT Calmodulin-Regulated Cysteine SUMO Protease.";
RL Antioxid. Redox Signal. 31:503-520(2019).
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 lysyl-AMP (AMP-N-epsilon-(N-alpha-
CC acetyl lysine methyl ester)) generated by lysine tRNA ligase (By
CC similarity). {ECO:0000250|UniProtKB:Q9NQE9}.
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:Q9NQE9};
CC -!- SUBUNIT: Forms dimers to octamers and even larger oligomer (By
CC similarity). Interacts with CALM1 (PubMed:31088288).
CC {ECO:0000250|UniProtKB:Q9NQE9, ECO:0000269|PubMed:31088288}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQE9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NQE9}.
CC -!- SIMILARITY: Belongs to the HINT family. {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; AY040768; AAK94778.1; -; mRNA.
DR EMBL; AK002482; BAB22134.1; -; mRNA.
DR EMBL; AK007758; BAB25237.1; -; mRNA.
DR EMBL; AK027974; BAC25684.1; -; mRNA.
DR EMBL; BC025065; AAH25065.1; -; mRNA.
DR CCDS; CCDS23764.1; -.
DR RefSeq; NP_080074.1; NM_025798.3.
DR AlphaFoldDB; Q9CPS6; -.
DR SMR; Q9CPS6; -.
DR STRING; 10090.ENSMUSP00000125552; -.
DR iPTMnet; Q9CPS6; -.
DR PhosphoSitePlus; Q9CPS6; -.
DR EPD; Q9CPS6; -.
DR MaxQB; Q9CPS6; -.
DR PaxDb; Q9CPS6; -.
DR PeptideAtlas; Q9CPS6; -.
DR PRIDE; Q9CPS6; -.
DR ProteomicsDB; 273112; -.
DR Antibodypedia; 32730; 80 antibodies from 17 providers.
DR DNASU; 66847; -.
DR Ensembl; ENSMUST00000161074; ENSMUSP00000125552; ENSMUSG00000019791.
DR GeneID; 66847; -.
DR KEGG; mmu:66847; -.
DR UCSC; uc007etg.1; mouse.
DR CTD; 135114; -.
DR MGI; MGI:1914097; Hint3.
DR VEuPathDB; HostDB:ENSMUSG00000019791; -.
DR eggNOG; KOG4359; Eukaryota.
DR GeneTree; ENSGT00510000047616; -.
DR HOGENOM; CLU_056776_4_2_1; -.
DR InParanoid; Q9CPS6; -.
DR OMA; CRIAGRQ; -.
DR OrthoDB; 1496385at2759; -.
DR PhylomeDB; Q9CPS6; -.
DR TreeFam; TF353069; -.
DR BioGRID-ORCS; 66847; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Hint3; mouse.
DR PRO; PR:Q9CPS6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CPS6; protein.
DR Bgee; ENSMUSG00000019791; Expressed in interventricular septum and 243 other tissues.
DR ExpressionAtlas; Q9CPS6; baseline and differential.
DR Genevisible; Q9CPS6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT CHAIN 2..165
FT /note="Adenosine 5'-monophosphoramidase HINT3"
FT /id="PRO_0000324328"
FT DOMAIN 32..143
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 126..130
FT /note="Histidine triad motif"
FT ACT_SITE 128
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT BINDING 59..60
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P49773"
FT BINDING 128..130
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:Q9NQE9"
SQ SEQUENCE 165 AA; 18788 MW; FC17E00E2848E0C5 CRC64;
MAEKQAGLVG EPDPEGSSPG TSESWNYDSN CVFCRVAAGQ EPKTELFHCE NEDLVCFKDI
KPAALYHYLV VPKKHIGSCK DLNKDHIEMV ESMVAAGKTM LERNNFTDFT DVRMGFHVPP
FCSISHLHLH VIAPVKEFGF LSKLVYRQDS YWFVTVDYLL EKLRK
