{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8BZT9","secondaryAccessions":["Q14AQ3","Q3U600"],"uniProtkbId":"LACC1_MOUSE","entryAudit":{"firstPublicDate":"2003-06-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-03-01","entryVersion":121,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Purine nucleoside phosphorylase LACC1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}],"value":"2.4.2.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Adenosine deaminase LACC1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}],"value":"3.5.4.4"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27478939"}],"value":"Fatty acid metabolism-immunity nexus"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Guanosine phosphorylase LACC1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"35978195"}],"value":"Isocyanic acid synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35978195"}],"value":"4.3.3.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Laccase domain-containing protein 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"S-methyl-5'-thioadenosine phosphorylase LACC1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}],"value":"2.4.2.28"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"MGI","id":"MGI:2445077"}],"value":"Lacc1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27478939"}],"value":"Famin"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27478939"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31978345"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35978195"}],"value":"Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine, guanosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine, guanine and hypoxanthine (By similarity). Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (By similarity). Also has adenosine deaminase activity (By similarity). Acts as a regulator of innate immunity in macrophages by modulating the purine nucleotide metabolism, thereby regulating the metabolic function and bioenergetic state of macrophages (PubMed:27478939, PubMed:31978345). Enables a purine nucleotide cycle between adenosine and inosine monophosphate and adenylosuccinate that prevents cytoplasmic acidification and balances the cytoplasmic-mitochondrial redox interface (PubMed:31978345). The purine nucleotide cycle consumes aspartate and releases fumarate in a manner involving fatty acid oxidation and ATP-citrate lyase activity (PubMed:31978345). Participates in pattern recognition receptor-induced cytokines in macrophages: associates with the NOD2-signaling complex and promotes optimal NOD2-induced signaling, cytokine secretion and bacterial clearance (By similarity). Localizes to the endoplasmic reticulum upon PRR stimulation of macrophages and associates with endoplasmic reticulum-stress sensors, promoting the endoplasmic reticulum unfolded protein response (UPR) (By similarity). Does not show laccase activity (By similarity). Component of L-arginine metabolism in activated macrophages supporting anti-inflammatory and antibacterial macrophage effector functions. Cleaves L-citrulline, a product of L-arginine metabolized via NOS2, to yield isocyanate, a reactive carbonyl species-like cytotoxin, and L-ornithine, a precursor in polyamine biosynthesis. Through L-ornithine controls cellular polyamine pools likely triggering polyamine-mediated proinflammatory cytokine suppression and autophagy stimulation (PubMed:35978195). Directly interacts with components of autophagy machinery to regulate macrophage metabolism and bacterial phagocytosis. Acts downstream of the energy sensor AMP-activated protein kinase (AMPK) to promote autophagy associated to lipid droplets generation providing fatty acids for mitochondrial respiration (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + phosphate = alpha-D-ribose 1-phosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27642"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:27643"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27646"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:17596"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:27647"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13233"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:16750"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:13234"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-methyl-5'-thioadenosine + phosphate = 5-(methylsulfanyl)-alpha-D-ribose 1-phosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11852"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:17509"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58533"}],"ecNumber":"2.4.2.28","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:11853"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + H2O + H(+) = inosine + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24408"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:17596"},{"database":"ChEBI","id":"CHEBI:28938"}],"ecNumber":"3.5.4.4","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24409"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-citrulline + H(+) = isocyanate + L-ornithine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83407"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29202"},{"database":"ChEBI","id":"CHEBI:46911"},{"database":"ChEBI","id":"CHEBI:57743"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35978195"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:83408"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35978195"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35978195"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35978195"}],"value":"Binds 1 Zn(2+) ion per subunit."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":117.0,"unit":"uM","substrate":"L-citrulline","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35978195"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}],"value":"Interacts with FASN. Interacts with SDHA. Interacts with ATF6, EIF2AK3 and ERN1"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}],"value":"Upon stimulation of the pattern-recognition receptor (PRR) NOD2, localizes to the endoplasmic reticulum"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30510070"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30510070"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}],"value":"Endoplasmic reticulum","id":"SL-0095"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}],"value":"Peroxisome","id":"SL-0204"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30510070"}],"value":"Predominantly expressed in myeloid cells (PubMed:30510070). Highly expressed in primary macrophages and dendritic cells sorted from the peritoneum or spleen, respectively (at protein level) (PubMed:30510070)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}],"value":"Phosphorylated on tyrosine residues"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30510070"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35978195"}],"value":"No visible phenotype in normal conditions (PubMed:30510070). Mice show increased inflammatory response in mouse models of arthritis and inflammation (PubMed:30510070). Confers increased susceptibility to S. Typhimurium infection associated with decreased bacterial clearance and decreased mice survival. This phenotype is reversed by oral administration of L-ornithine"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the PgeF/LACC1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"Purine nucleoside phosphorylase LACC1","featureId":"PRO_0000163188"},{"type":"Binding site","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P84138"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P84138"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P84138"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Modified residue","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8IV20"}]},{"type":"Mutagenesis","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Reduced function.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27478939"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["I"]}},{"type":"Mutagenesis","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"Complete loss of function. Results in increased proinflammatory cytokine production and decreased antibacterial response upon S. Typhimurium infection.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27478939"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35978195"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["R"]}}],"keywords":[{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0391","category":"Biological process","name":"Immunity"},{"id":"KW-0395","category":"Biological process","name":"Inflammatory response"},{"id":"KW-0399","category":"Biological process","name":"Innate immunity"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"id":"KW-0576","category":"Cellular component","name":"Peroxisome"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"16141072","citationType":"journal article","authors":["Carninci P.","Kasukawa T.","Katayama S.","Gough J.","Frith M.C.","Maeda N.","Oyama R.","Ravasi T.","Lenhard B.","Wells C.","Kodzius R.","Shimokawa K.","Bajic V.B.","Brenner S.E.","Batalov S.","Forrest A.R.","Zavolan M.","Davis M.J.","Wilming L.G.","Aidinis V.","Allen J.E.","Ambesi-Impiombato A.","Apweiler R.","Aturaliya R.N.","Bailey T.L.","Bansal M.","Baxter L.","Beisel K.W.","Bersano T.","Bono H.","Chalk A.M.","Chiu K.P.","Choudhary V.","Christoffels A.","Clutterbuck D.R.","Crowe M.L.","Dalla E.","Dalrymple B.P.","de Bono B.","Della Gatta G.","di Bernardo D.","Down T.","Engstrom P.","Fagiolini M.","Faulkner G.","Fletcher C.F.","Fukushima T.","Furuno M.","Futaki S.","Gariboldi M.","Georgii-Hemming P.","Gingeras T.R.","Gojobori T.","Green R.E.","Gustincich S.","Harbers M.","Hayashi Y.","Hensch T.K.","Hirokawa N.","Hill D.","Huminiecki L.","Iacono M.","Ikeo K.","Iwama A.","Ishikawa T.","Jakt M.","Kanapin A.","Katoh M.","Kawasawa Y.","Kelso J.","Kitamura H.","Kitano H.","Kollias G.","Krishnan S.P.","Kruger A.","Kummerfeld S.K.","Kurochkin I.V.","Lareau L.F.","Lazarevic D.","Lipovich L.","Liu J.","Liuni S.","McWilliam S.","Madan Babu M.","Madera M.","Marchionni L.","Matsuda H.","Matsuzawa S.","Miki H.","Mignone F.","Miyake S.","Morris K.","Mottagui-Tabar S.","Mulder N.","Nakano N.","Nakauchi H.","Ng P.","Nilsson R.","Nishiguchi S.","Nishikawa S.","Nori F.","Ohara O.","Okazaki Y.","Orlando V.","Pang K.C.","Pavan W.J.","Pavesi G.","Pesole G.","Petrovsky N.","Piazza S.","Reed J.","Reid J.F.","Ring B.Z.","Ringwald M.","Rost B.","Ruan Y.","Salzberg S.L.","Sandelin A.","Schneider C.","Schoenbach C.","Sekiguchi K.","Semple C.A.","Seno S.","Sessa L.","Sheng Y.","Shibata Y.","Shimada H.","Shimada K.","Silva D.","Sinclair B.","Sperling S.","Stupka E.","Sugiura K.","Sultana R.","Takenaka Y.","Taki K.","Tammoja K.","Tan S.L.","Tang S.","Taylor M.S.","Tegner J.","Teichmann S.A.","Ueda H.R.","van Nimwegen E.","Verardo R.","Wei C.L.","Yagi K.","Yamanishi H.","Zabarovsky E.","Zhu S.","Zimmer A.","Hide W.","Bult C.","Grimmond S.M.","Teasdale R.D.","Liu E.T.","Brusic V.","Quackenbush J.","Wahlestedt C.","Mattick J.S.","Hume D.A.","Kai C.","Sasaki D.","Tomaru Y.","Fukuda S.","Kanamori-Katayama M.","Suzuki M.","Aoki J.","Arakawa T.","Iida J.","Imamura K.","Itoh M.","Kato T.","Kawaji H.","Kawagashira N.","Kawashima T.","Kojima M.","Kondo S.","Konno H.","Nakano K.","Ninomiya N.","Nishio T.","Okada M.","Plessy C.","Shibata K.","Shiraki T.","Suzuki S.","Tagami M.","Waki K.","Watahiki A.","Okamura-Oho Y.","Suzuki H.","Kawai J.","Hayashizaki Y."],"citationCrossReferences":[{"database":"PubMed","id":"16141072"},{"database":"DOI","id":"10.1126/science.1112014"}],"title":"The transcriptional landscape of the mammalian genome.","publicationDate":"2005","journal":"Science","firstPage":"1559","lastPage":"1563","volume":"309"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]"],"referenceComments":[{"value":"C57BL/6J","type":"STRAIN"},{"value":"Bone marrow","type":"TISSUE"},{"value":"Colon","type":"TISSUE"}]},{"referenceNumber":2,"citation":{"id":"15489334","citationType":"journal article","authoringGroup":["The MGC Project Team"],"citationCrossReferences":[{"database":"PubMed","id":"15489334"},{"database":"DOI","id":"10.1101/gr.2596504"}],"title":"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).","publicationDate":"2004","journal":"Genome Res.","firstPage":"2121","lastPage":"2127","volume":"14"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]"],"referenceComments":[{"value":"Brain","type":"TISSUE"}]},{"referenceNumber":3,"citation":{"id":"27478939","citationType":"journal article","authors":["Cader M.Z.","Boroviak K.","Zhang Q.","Assadi G.","Kempster S.L.","Sewell G.W.","Saveljeva S.","Ashcroft J.W.","Clare S.","Mukhopadhyay S.","Brown K.P.","Tschurtschenthaler M.","Raine T.","Doe B.","Chilvers E.R.","Griffin J.L.","Kaneider N.C.","Floto R.A.","D'Amato M.","Bradley A.","Wakelam M.J.","Dougan G.","Kaser A."],"citationCrossReferences":[{"database":"PubMed","id":"27478939"},{"database":"DOI","id":"10.1038/ni.3532"}],"title":"C13orf31 (FAMIN) is a central regulator of immunometabolic function.","publicationDate":"2016","journal":"Nat. Immunol.","firstPage":"1046","lastPage":"1056","volume":"17"},"referencePositions":["FUNCTION","MUTAGENESIS OF VAL-254 AND CYS-284"]},{"referenceNumber":4,"citation":{"id":"30510070","citationType":"journal article","authors":["Skon-Hegg C.","Zhang J.","Wu X.","Sagolla M.","Ota N.","Wuster A.","Tom J.","Doran E.","Ramamoorthi N.","Caplazi P.","Monroe J.","Lee W.P.","Behrens T.W."],"citationCrossReferences":[{"database":"PubMed","id":"30510070"},{"database":"DOI","id":"10.4049/jimmunol.1800636"}],"title":"LACC1 regulates TNF and IL-17 in mouse models of arthritis and inflammation.","publicationDate":"2019","journal":"J. Immunol.","firstPage":"183","lastPage":"193","volume":"202"},"referencePositions":["SUBCELLULAR LOCATION","TISSUE SPECIFICITY","DISRUPTION PHENOTYPE"]},{"referenceNumber":5,"citation":{"id":"31978345","citationType":"journal article","authors":["Cader M.Z.","de Almeida Rodrigues R.P.","West J.A.","Sewell G.W.","Md-Ibrahim M.N.","Reikine S.","Sirago G.","Unger L.W.","Inglesias-Romero A.B.","Ramshorn K.","Haag L.M.","Saveljeva S.","Ebel J.F.","Rosenstiel P.","Kaneider N.C.","Lee J.C.","Lawley T.D.","Bradley A.","Dougan G.","Modis Y.","Griffin J.L.","Kaser A."],"citationCrossReferences":[{"database":"PubMed","id":"31978345"},{"database":"DOI","id":"10.1016/j.cell.2019.12.017"}],"title":"FAMIN is a multifunctional purine enzyme enabling the purine nucleotide cycle.","publicationDate":"2020","journal":"Cell","firstPage":"278","lastPage":"295","volume":"180"},"referencePositions":["FUNCTION"]},{"referenceNumber":6,"citation":{"id":"35978195","citationType":"journal article","authors":["Wei Z.","Oh J.","Flavell R.A.","Crawford J.M."],"citationCrossReferences":[{"database":"PubMed","id":"35978195"},{"database":"DOI","id":"10.1038/s41586-022-05111-3"}],"title":"LACC1 bridges NOS2 and polyamine metabolism in inflammatory macrophages.","publicationDate":"2022","journal":"Nature","firstPage":"348","lastPage":"353","volume":"609"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","BIOPHYSICOCHEMICAL PROPERTIES","DISRUPTION PHENOTYPE","MUTAGENESIS OF CYS-284"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AK033565","properties":[{"key":"ProteinId","value":"BAC28363.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"AK152154","properties":[{"key":"ProteinId","value":"BAE30989.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"AK153349","properties":[{"key":"ProteinId","value":"BAE31925.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"BC116748","properties":[{"key":"ProteinId","value":"AAI16749.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"EMBL","id":"BC119140","properties":[{"key":"ProteinId","value":"AAI19141.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"CCDS","id":"CCDS27287.1","properties":[{"key":"Description","value":"-"}]},{"database":"RefSeq","id":"NP_766076.1","properties":[{"key":"NucleotideSequenceId","value":"NM_172488.2"}]},{"database":"AlphaFoldDB","id":"Q8BZT9","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q8BZT9","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"229184","properties":[{"key":"Interactions","value":"1"}]},{"database":"FunCoup","id":"Q8BZT9","properties":[{"key":"Number of interactors","value":"791"}]},{"database":"STRING","id":"10090.ENSMUSP00000059173","properties":[{"key":"Description","value":"-"}]},{"database":"GlyGen","id":"Q8BZT9","properties":[{"key":"glycosylation","value":"1 site, 1 O-linked glycan (1 site)"}]},{"database":"PhosphoSitePlus","id":"Q8BZT9","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"10090-ENSMUSP00000059173","properties":[{"key":"Description","value":"-"}]},{"database":"ProteomicsDB","id":"290006","properties":[{"key":"Description","value":"-"}]},{"database":"Pumba","id":"Q8BZT9","properties":[{"key":"Description","value":"-"}]},{"database":"DNASU","id":"210808","properties":[{"key":"Description","value":"-"}]},{"database":"Ensembl","id":"ENSMUST00000062789.15","properties":[{"key":"ProteinId","value":"ENSMUSP00000059173.9"},{"key":"GeneId","value":"ENSMUSG00000044350.15"}]},{"database":"GeneID","id":"210808","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"mmu:210808","properties":[{"key":"Description","value":"-"}]},{"database":"UCSC","id":"uc007urq.1","properties":[{"key":"OrganismName","value":"mouse"}]},{"database":"AGR","id":"MGI:2445077","properties":[{"key":"Description","value":"-"}]},{"database":"CTD","id":"144811","properties":[{"key":"Description","value":"-"}]},{"database":"MGI","id":"MGI:2445077","properties":[{"key":"GeneName","value":"Lacc1"}]},{"database":"VEuPathDB","id":"HostDB:ENSMUSG00000044350","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"ENOG502QUMA","properties":[{"key":"ToxonomicScope","value":"Eukaryota"}]},{"database":"GeneTree","id":"ENSGT00390000000693","properties":[{"key":"Description","value":"-"}]},{"database":"HOGENOM","id":"CLU_637703_0_0_1","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"Q8BZT9","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"HDNCELE","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"10055554at2759","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"Q8BZT9","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID-ORCS","id":"210808","properties":[{"key":"hits","value":"1 hit in 76 CRISPR screens"}]},{"database":"PRO","id":"PR:Q8BZT9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000589","properties":[{"key":"Component","value":"Chromosome 14"}]},{"database":"RNAct","id":"Q8BZT9","properties":[{"key":"moleculeType","value":"protein"}]},{"database":"Bgee","id":"ENSMUSG00000044350","properties":[{"key":"ExpressionPatterns","value":"Expressed in lens of camera-type eye and 127 other cell types or tissues"}]},{"database":"ExpressionAtlas","id":"Q8BZT9","properties":[{"key":"ExpressionPatterns","value":"baseline and differential"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"30510070"}]},{"database":"GO","id":"GO:0005783","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"30510070"}]},{"database":"GO","id":"GO:0005777","properties":[{"key":"GoTerm","value":"C:peroxisome"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0004000","properties":[{"key":"GoTerm","value":"F:adenosine deaminase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0005507","properties":[{"key":"GoTerm","value":"F:copper ion binding"},{"key":"GoEvidenceType","value":"IBA:GO_Central"}]},{"database":"GO","id":"GO:0047975","properties":[{"key":"GoTerm","value":"F:guanosine phosphorylase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0004731","properties":[{"key":"GoTerm","value":"F:purine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0017061","properties":[{"key":"GoTerm","value":"F:S-methyl-5-thioadenosine phosphorylase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0070431","properties":[{"key":"GoTerm","value":"P:nucleotide-binding oligomerization domain containing 2 signaling pathway"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0002221","properties":[{"key":"GoTerm","value":"P:pattern recognition receptor signaling pathway"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0002720","properties":[{"key":"GoTerm","value":"P:positive regulation of cytokine production involved in immune response"},{"key":"GoEvidenceType","value":"ISO:GO_Central"}]},{"database":"GO","id":"GO:0050727","properties":[{"key":"GoTerm","value":"P:regulation of inflammatory response"},{"key":"GoEvidenceType","value":"IMP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"30510070"}]},{"database":"GO","id":"GO:0051453","properties":[{"key":"GoTerm","value":"P:regulation of intracellular pH"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:1900542","properties":[{"key":"GoTerm","value":"P:regulation of purine nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IMP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"31978345"}]},{"database":"CDD","id":"cd16833","properties":[{"key":"EntryName","value":"YfiH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.140.10:FF:000002","properties":[{"key":"EntryName","value":"Laccase (multicopper oxidoreductase) domain-containing 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.140.10","properties":[{"key":"EntryName","value":"CNF1/YfiH-like putative cysteine hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003730","properties":[{"key":"EntryName","value":"Cu_polyphenol_OxRdtase"}]},{"database":"InterPro","id":"IPR038371","properties":[{"key":"EntryName","value":"Cu_polyphenol_OxRdtase_sf"}]},{"database":"InterPro","id":"IPR011324","properties":[{"key":"EntryName","value":"Cytotoxic_necrot_fac-like_cat"}]},{"database":"PANTHER","id":"PTHR30616:SF2","properties":[{"key":"EntryName","value":"PURINE NUCLEOSIDE PHOSPHORYLASE LACC1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30616","properties":[{"key":"EntryName","value":"UNCHARACTERIZED PROTEIN YFIH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02578","properties":[{"key":"EntryName","value":"Cu-oxidase_4"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64438","properties":[{"key":"EntryName","value":"CNF1/YfiH-like putative cysteine hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAEAVLIDLSGLQLNAQKNCHETLLETLDGIHYHHAPKAKFLCIICCRNASKEKDGEYGLCELEAGNGFSRLAGKFETVSHPCLAASLYTIKQKIDEENLSCIKVIVPEHRKLLMKAYVGQLFTEVYEFEFEDLQGAWRDSLLKPSTGINVTTTQELEDIQHEIETYLRSLPALKGDLTIVTSPLIPDNFLHGFTTRTGGISSVPTLSSLNLFSSSKRRDPKVVVQENVRRLANAAGFNAEKFYRIKTDHASEVWVMGKKEPESYDGIVTNQRGVTITALGADCIPIVFADPVKKACGVAHSGWKGTLLGVAMATVNAMIAEYGCDVEDIIVVLGPSVGSCCFTLPKESAVSFHSLHPSCVRHFDSPRPYVDIRKATRILLERGGILPQNIQDQKEDLDLCTSCHPEKFFSHVRDGLNFGTQIGFISLRE","length":430,"molWeight":47514,"crc64":"4F73BC343D9F3414","md5":"A4CA695877D18EEFB525D0B47C9C0845"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"COFACTOR":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"TISSUE SPECIFICITY":1,"PTM":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":3,"Modified residue":1,"Mutagenesis":2},"uniParcId":"UPI0000029FD5"}}