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Adenosine deaminase 2 (EC 3.5.4.4) (Cat eye syndrome critical region protein 1)

 ADA2_HUMAN              Reviewed;         511 AA.
Q9NZK5; A8K9H4; Q6ICF1; Q86UB6; Q8NCJ2; Q96K41;
16-APR-2002, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 2.
25-OCT-2017, entry version 139.
RecName: Full=Adenosine deaminase 2 {ECO:0000312|HGNC:HGNC:1839};
EC=3.5.4.4 {ECO:0000269|PubMed:15926889, ECO:0000269|PubMed:20453107};
AltName: Full=Cat eye syndrome critical region protein 1;
Flags: Precursor;
Name=ADA2 {ECO:0000312|HGNC:HGNC:1839}; Synonyms=ADGF, CECR1, IDGFL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-335.
PubMed=10756095; DOI=10.1006/geno.1999.6099;
Riazi M.A., Brinkman-Mills P., Nguyen T., Pan H., Phan S., Ying F.,
Roe B.A., Tochigi J., Shimizu Y., Minoshima S., Shimizu N.,
Buchwald M., McDermid H.E.;
"The human homolog of insect-derived growth factor, CECR1, is a
candidate gene for features of cat eye syndrome.";
Genomics 64:277-285(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ARG-335.
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
IDENTIFICATION BY MASS SPECTROMETRY, HEPARIN-BINDING, AND SUBCELLULAR
LOCATION.
PubMed=15926889; DOI=10.1042/BJ20050683;
Zavialov A.V., Engstroem A.;
"Human ADA2 belongs to a new family of growth factors with adenosine
deaminase activity.";
Biochem. J. 391:51-57(2005).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174 AND ASN-378.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, HEPARIN-BINDING,
AND SUBUNIT.
PubMed=20453107; DOI=10.1189/jlb.1109764;
Zavialov A.V., Gracia E., Glaichenhaus N., Franco R., Zavialov A.V.,
Lauvau G.;
"Human adenosine deaminase 2 induces differentiation of monocytes into
macrophages and stimulates proliferation of T helper cells and
macrophages.";
J. Leukoc. Biol. 88:279-290(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-511 IN COMPLEX WITH ZINC
IONS AND TRANSITION STATE ANALOG COFORMYCIN, FUNCTION, COFACTOR,
SUBCELLULAR LOCATION, SUBUNIT, DISULFIDE BOND, DOMAINS,
GLYCOSAMINOCLYCAN BINDING, MUTAGENESIS OF CYS-137 AND TRP-362, AND
GLYCOSYLATION AT ASN-127; ASN-185 AND ASN-378.
PubMed=20147294; DOI=10.1074/jbc.M109.083527;
Zavialov A.V., Yu X., Spillmann D., Lauvau G., Zavialov A.V.;
"Structural basis for the growth factor activity of human adenosine
deaminase ADA2.";
J. Biol. Chem. 285:12367-12377(2010).
[12]
INVOLVEMENT IN PAN, AND VARIANTS PAN ARG-47; ASP-109; GLN-112; GLN-169
AND CYS-453.
PubMed=24552284; DOI=10.1056/NEJMoa1307361;
Zhou Q., Yang D., Ombrello A.K., Zavialov A.V., Toro C.,
Zavialov A.V., Stone D.L., Chae J.J., Rosenzweig S.D., Bishop K.,
Barron K.S., Kuehn H.S., Hoffmann P., Negro A., Tsai W.L., Cowen E.W.,
Pei W., Milner J.D., Silvin C., Heller T., Chin D.T., Patronas N.J.,
Barber J.S., Lee C.C., Wood G.M., Ling A., Kelly S.J., Kleiner D.E.,
Mullikin J.C., Ganson N.J., Kong H.H., Hambleton S., Candotti F.,
Quezado M.M., Calvo K.R., Alao H., Barham B.K., Jones A.,
Meschia J.F., Worrall B.B., Kasner S.E., Rich S.S.,
Goldbach-Mansky R., Abinun M., Chalom E., Gotte A.C., Punaro M.,
Pascual V., Verbsky J.W., Torgerson T.R., Singer N.G., Gershon T.R.,
Ozen S., Karadag O., Fleisher T.A., Remmers E.F., Burgess S.M.,
Moir S.L., Gadina M., Sood R., Hershfield M.S., Boehm M.,
Kastner D.L., Aksentijevich I.;
"Early-onset stroke and vasculopathy associated with mutations in
ADA2.";
N. Engl. J. Med. 370:911-920(2014).
[13]
VARIANTS PAN VAL-47; ARG-47; GLN-169; LEU-251 AND SER-264.
PubMed=24552285; DOI=10.1056/NEJMoa1307362;
Navon Elkan P., Pierce S.B., Segel R., Walsh T., Barash J., Padeh S.,
Zlotogorski A., Berkun Y., Press J.J., Mukamel M., Voth I.,
Hashkes P.J., Harel L., Hoffer V., Ling E., Yalcinkaya F.,
Kasapcopur O., Lee M.K., Klevit R.E., Renbaum P., Weinberg-Shukron A.,
Sener E.F., Schormair B., Zeligson S., Marek-Yagel D., Strom T.M.,
Shohat M., Singer A., Rubinow A., Pras E., Winkelmann J., Tekin M.,
Anikster Y., King M.C., Levy-Lahad E.;
"Mutant adenosine deaminase 2 in a polyarteritis nodosa
vasculopathy.";
N. Engl. J. Med. 370:921-931(2014).
[14]
INVOLVEMENT IN SNDDS, AND VARIANTS SNDDS ALA-119 AND SER-142.
PubMed=25075847; DOI=10.1056/NEJMc1405506#SA3;
Bras J., Guerreiro R., Santo G.C.;
"Mutant ADA2 in vasculopathies.";
N. Engl. J. Med. 371:478-480(2014).
-!- FUNCTION: Adenosine deaminase that may contribute to the
degradation of extracellular adenosine, a signaling molecule that
controls a variety of cellular responses. Requires elevated
adenosine levels for optimal enzyme activity. Binds to cell
surfaces via proteoglycans and may play a role in the regulation
of cell proliferation and differentiation, independently of its
enzyme activity. {ECO:0000269|PubMed:20147294,
ECO:0000269|PubMed:20453107}.
-!- CATALYTIC ACTIVITY: Adenosine + H(2)O = inosine + NH(3).
{ECO:0000269|PubMed:15926889, ECO:0000269|PubMed:20453107}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:20147294};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:20147294};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.25 mM for adenosine {ECO:0000269|PubMed:15926889};
pH dependence:
Optimum pH is 6.6. {ECO:0000269|PubMed:15926889};
-!- SUBUNIT: Homodimer. Interacts with adenosine receptors. Binds
heparin. {ECO:0000269|PubMed:20147294,
ECO:0000269|PubMed:20453107}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15926889,
ECO:0000269|PubMed:20147294, ECO:0000269|PubMed:20453107}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NZK5-1; Sequence=Displayed;
Name=2;
IsoId=Q9NZK5-2; Sequence=VSP_041509, VSP_041510;
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
Widely expressed, with most abundant expression in human adult
heart, lung, lymphoblasts, and placenta as well as fetal lung,
liver, and kidney. In embryo, expressed in the outflow tract and
atrium of the developing heart, the VII/VIII cranial nerve
ganglion, and the notochord. {ECO:0000269|PubMed:15926889}.
-!- DOMAIN: The PRB domain is involved in receptor binding, and may be
responsible for the cytokine-like growth factor activity due to
it's sharing of several structural properties with chemokines.
{ECO:0000269|PubMed:20147294}.
-!- DOMAIN: High-affinity binding to heparin/glycosaminoclycan (GAG)
is mediated by a large, highly positively charged surface at the
interface of dimer's subunits involving approximately residues 30-
45, 389-396, and 422-428. {ECO:0000269|PubMed:20147294}.
-!- DISEASE: Polyarteritis nodosa (PAN) [MIM:615688]: A systemic
necrotizing vasculitis that affects medium and small arteries. The
ensuing tissue ischemia can affect any organ, including the skin,
musculoskeletal system, kidneys, gastrointestinal tract, and the
cardiovascular and nervous systems. Organ involvement and disease
severity are highly variable. Clinical features include recurrent
ischemic stroke affecting the small vessels of the brain and
resulting in neurologic dysfunction, recurrent fever, myalgias,
livedoid rash, gastrointestinal pain and hepatosplenomegaly.
{ECO:0000269|PubMed:24552284, ECO:0000269|PubMed:24552285}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Sneddon syndrome (SNDDS) [MIM:182410]: A systemic non-
inflammatory thrombotic vasculopathy characterized by the
association of livedo racemosa, and in some cases livedo
reticularis, with cerebrovascular disease. Livedo racemosa is a
persistent net-like violaceous-cyanotic, mottled discoloration of
the skin affecting the legs, the arms, the buttocks and the trunk;
livedo reticularis is limited to the extremities and is visible
only in the cold. Cerebrovascular features include recurrent
transient ischemic attacks, infarcts, and rarely spinal strokes or
intracranial or subarachnoid hemorrhages. Headache and vertigo may
precede the onset of livedo racemosa and cerebrovascular
manifestations by several years. Rare neurologic symptoms include
seizures, chorea, or myelopathies. {ECO:0000269|PubMed:25075847}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Candidate gene for the Cat Eye Syndrome (CES), a
developmental disorder associated with the duplication of a 2 Mb
region of 22q11.2. Duplication usually takes in the form of a
surpernumerary bisatellited isodicentric chromosome, resulting in
four copies of the region (represents an inv dup(22)(q11)). CES is
characterized clinically by the combination of coloboma of the
iris and anal atresia with fistula, downslanting palpebral
fissures, preauricular tags and/or pits, frequent occurrence of
heart and renal malformations, and normal or near-normal mental
development.
-!- SIMILARITY: Belongs to the metallo-dependent hydrolases
superfamily. Adenosine and AMP deaminases family. ADGF subfamily.
{ECO:0000305}.
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EMBL; AF190746; AAF65941.1; -; mRNA.
EMBL; CR456417; CAG30303.1; -; mRNA.
EMBL; AK027682; BAB55293.1; -; mRNA.
EMBL; AK292689; BAF85378.1; -; mRNA.
EMBL; AK074702; BAC11148.1; -; mRNA.
EMBL; AC005300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471193; EAW57750.1; -; Genomic_DNA.
EMBL; BC051755; AAH51755.1; -; mRNA.
CCDS; CCDS13742.1; -. [Q9NZK5-1]
CCDS; CCDS13743.1; -. [Q9NZK5-2]
RefSeq; NP_001269154.1; NM_001282225.1. [Q9NZK5-1]
RefSeq; NP_001269155.1; NM_001282226.1. [Q9NZK5-1]
RefSeq; NP_001269156.1; NM_001282227.1.
RefSeq; NP_001269157.1; NM_001282228.1.
RefSeq; NP_001269158.1; NM_001282229.1.
RefSeq; NP_803124.1; NM_177405.2. [Q9NZK5-2]
RefSeq; XP_011544435.1; XM_011546133.1. [Q9NZK5-1]
UniGene; Hs.170310; -.
UniGene; Hs.637274; -.
PDB; 3LGD; X-ray; 2.00 A; A/B=29-511.
PDB; 3LGG; X-ray; 2.50 A; A/B=29-511.
PDBsum; 3LGD; -.
PDBsum; 3LGG; -.
ProteinModelPortal; Q9NZK5; -.
SMR; Q9NZK5; -.
BioGrid; 119736; 1.
STRING; 9606.ENSP00000262607; -.
iPTMnet; Q9NZK5; -.
PhosphoSitePlus; Q9NZK5; -.
DMDM; 122065151; -.
EPD; Q9NZK5; -.
MaxQB; Q9NZK5; -.
PaxDb; Q9NZK5; -.
PeptideAtlas; Q9NZK5; -.
PRIDE; Q9NZK5; -.
TopDownProteomics; Q9NZK5-1; -. [Q9NZK5-1]
DNASU; 51816; -.
Ensembl; ENST00000262607; ENSP00000262607; ENSG00000093072. [Q9NZK5-1]
Ensembl; ENST00000330232; ENSP00000332871; ENSG00000093072. [Q9NZK5-2]
Ensembl; ENST00000399837; ENSP00000382731; ENSG00000093072. [Q9NZK5-1]
Ensembl; ENST00000399839; ENSP00000382733; ENSG00000093072. [Q9NZK5-1]
GeneID; 51816; -.
KEGG; hsa:51816; -.
UCSC; uc002zmj.3; human. [Q9NZK5-1]
CTD; 51816; -.
DisGeNET; 51816; -.
EuPathDB; HostDB:ENSG00000093072.15; -.
GeneCards; ADA2; -.
HGNC; HGNC:1839; ADA2.
HPA; HPA007888; -.
MalaCards; ADA2; -.
MIM; 182410; phenotype.
MIM; 607575; gene.
MIM; 615688; phenotype.
neXtProt; NX_Q9NZK5; -.
OpenTargets; ENSG00000093072; -.
Orphanet; 820; Sneddon syndrome.
Orphanet; 404553; Vasculitis due to ADA2 deficiency.
PharmGKB; PA26382; -.
eggNOG; KOG1097; Eukaryota.
eggNOG; COG1816; LUCA.
GeneTree; ENSGT00390000012118; -.
HOGENOM; HOG000044097; -.
HOVERGEN; HBG050883; -.
InParanoid; Q9NZK5; -.
KO; K19572; -.
OMA; LPELFWF; -.
OrthoDB; EOG091G0CQY; -.
PhylomeDB; Q9NZK5; -.
TreeFam; TF324524; -.
BRENDA; 3.5.4.4; 2681.
Reactome; R-HSA-5683826; Surfactant metabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; Q9NZK5; -.
GeneWiki; CECR1; -.
GenomeRNAi; 51816; -.
PRO; PR:Q9NZK5; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000093072; -.
CleanEx; HS_CECR1; -.
ExpressionAtlas; Q9NZK5; baseline and differential.
Genevisible; Q9NZK5; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0004000; F:adenosine deaminase activity; IDA:UniProtKB.
GO; GO:0031685; F:adenosine receptor binding; IDA:UniProtKB.
GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0043394; F:proteoglycan binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006154; P:adenosine catabolic process; IDA:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; NAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
InterPro; IPR001365; A/AMP_deaminase_dom.
InterPro; IPR013659; A_deaminase_N.
InterPro; IPR006331; ADGF.
InterPro; IPR032466; Metal_Hydrolase.
Pfam; PF00962; A_deaminase; 1.
Pfam; PF08451; A_deaminase_N; 1.
SUPFAM; SSF51556; SSF51556; 1.
TIGRFAMs; TIGR01431; adm_rel; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Heparin-binding;
Hydrolase; Metal-binding; Polymorphism; Reference proteome; Secreted;
Signal; Zinc.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 511 Adenosine deaminase 2.
/FTId=PRO_0000006725.
REGION 30 100 Dimerization.
REGION 127 185 PRB domain.
REGION 204 211 Substrate binding.
ACT_SITE 359 359 Proton donor. {ECO:0000305}.
ACT_SITE 384 384 Proton acceptor. {ECO:0000305}.
METAL 112 112 Zinc; catalytic.
METAL 114 114 Zinc; catalytic.
METAL 356 356 Zinc; catalytic.
METAL 441 441 Zinc; catalytic.
BINDING 115 115 Substrate.
BINDING 293 293 Substrate.
BINDING 326 326 Substrate; via amide nitrogen.
BINDING 442 442 Substrate.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20147294}.
CARBOHYD 174 174 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20147294}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20147294}.
DISULFID 137 159 {ECO:0000269|PubMed:20147294}.
VAR_SEQ 1 241 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041509.
VAR_SEQ 242 251 YMEIRARLLP -> MDSLEWNWAL (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041510.
VARIANT 47 47 G -> R (in PAN; there is a decreased
expression of the mutant protein compared
to wild-type; dbSNP:rs202134424).
{ECO:0000269|PubMed:24552284,
ECO:0000269|PubMed:24552285}.
/FTId=VAR_071137.
VARIANT 47 47 G -> V (in PAN; dbSNP:rs200930463).
{ECO:0000269|PubMed:24552285}.
/FTId=VAR_071138.
VARIANT 109 109 A -> D (in PAN; dbSNP:rs587777240).
{ECO:0000269|PubMed:24552284}.
/FTId=VAR_071139.
VARIANT 112 112 H -> Q (in PAN; dbSNP:rs587777241).
{ECO:0000269|PubMed:24552284}.
/FTId=VAR_071140.
VARIANT 119 119 V -> A (in SNDDS).
{ECO:0000269|PubMed:25075847}.
/FTId=VAR_072562.
VARIANT 142 142 G -> S (in SNDDS).
{ECO:0000269|PubMed:25075847}.
/FTId=VAR_072563.
VARIANT 169 169 R -> Q (in PAN; dbSNP:rs77563738).
{ECO:0000269|PubMed:24552284,
ECO:0000269|PubMed:24552285}.
/FTId=VAR_071141.
VARIANT 251 251 P -> L (in PAN; dbSNP:rs148936893).
{ECO:0000269|PubMed:24552285}.
/FTId=VAR_071142.
VARIANT 264 264 W -> S (in PAN; dbSNP:rs587777242).
{ECO:0000269|PubMed:24552285}.
/FTId=VAR_071143.
VARIANT 335 335 H -> R (in dbSNP:rs2231495).
{ECO:0000269|PubMed:10756095,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_029802.
VARIANT 453 453 Y -> C (in PAN; dbSNP:rs376785840).
{ECO:0000269|PubMed:24552284}.
/FTId=VAR_071144.
MUTAGEN 137 137 C->G: Abolishes secretion.
{ECO:0000269|PubMed:20147294}.
MUTAGEN 362 362 W->G: Reduces dimerization and enzyme
activity. {ECO:0000269|PubMed:20147294}.
CONFLICT 359 359 E -> G (in Ref. 3; BAC11148).
{ECO:0000305}.
CONFLICT 394 394 V -> L (in Ref. 6; AAH51755).
{ECO:0000305}.
HELIX 30 44 {ECO:0000244|PDB:3LGD}.
TURN 46 49 {ECO:0000244|PDB:3LGD}.
HELIX 54 77 {ECO:0000244|PDB:3LGD}.
HELIX 81 83 {ECO:0000244|PDB:3LGD}.
HELIX 86 93 {ECO:0000244|PDB:3LGD}.
HELIX 97 104 {ECO:0000244|PDB:3LGD}.
STRAND 108 114 {ECO:0000244|PDB:3LGD}.
STRAND 117 119 {ECO:0000244|PDB:3LGD}.
HELIX 121 126 {ECO:0000244|PDB:3LGD}.
HELIX 128 130 {ECO:0000244|PDB:3LGD}.
STRAND 134 138 {ECO:0000244|PDB:3LGD}.
STRAND 144 148 {ECO:0000244|PDB:3LGD}.
HELIX 165 170 {ECO:0000244|PDB:3LGD}.
STRAND 171 173 {ECO:0000244|PDB:3LGG}.
HELIX 175 185 {ECO:0000244|PDB:3LGD}.
HELIX 193 196 {ECO:0000244|PDB:3LGD}.
HELIX 200 218 {ECO:0000244|PDB:3LGD}.
HELIX 221 237 {ECO:0000244|PDB:3LGD}.
STRAND 240 247 {ECO:0000244|PDB:3LGD}.
HELIX 262 279 {ECO:0000244|PDB:3LGD}.
STRAND 285 293 {ECO:0000244|PDB:3LGD}.
HELIX 298 314 {ECO:0000244|PDB:3LGD}.
TURN 316 318 {ECO:0000244|PDB:3LGD}.
STRAND 319 326 {ECO:0000244|PDB:3LGD}.
TURN 328 330 {ECO:0000244|PDB:3LGD}.
HELIX 335 337 {ECO:0000244|PDB:3LGD}.
HELIX 338 341 {ECO:0000244|PDB:3LGD}.
HELIX 343 346 {ECO:0000244|PDB:3LGD}.
TURN 366 369 {ECO:0000244|PDB:3LGD}.
HELIX 370 376 {ECO:0000244|PDB:3LGD}.
STRAND 380 384 {ECO:0000244|PDB:3LGD}.
HELIX 388 390 {ECO:0000244|PDB:3LGD}.
HELIX 392 400 {ECO:0000244|PDB:3LGD}.
STRAND 405 407 {ECO:0000244|PDB:3LGD}.
HELIX 409 414 {ECO:0000244|PDB:3LGD}.
HELIX 421 423 {ECO:0000244|PDB:3LGD}.
HELIX 426 431 {ECO:0000244|PDB:3LGD}.
STRAND 436 438 {ECO:0000244|PDB:3LGD}.
HELIX 443 446 {ECO:0000244|PDB:3LGD}.
HELIX 452 460 {ECO:0000244|PDB:3LGD}.
HELIX 469 481 {ECO:0000244|PDB:3LGD}.
STRAND 483 485 {ECO:0000244|PDB:3LGD}.
HELIX 487 509 {ECO:0000244|PDB:3LGD}.
SEQUENCE 511 AA; 58934 MW; A4AB0A83E8A0611E CRC64;
MLVDGPSERP ALCFLLLAVA MSFFGSALSI DETRAHLLLK EKMMRLGGRL VLNTKEELAN
ERLMTLKIAE MKEAMRTLIF PPSMHFFQAK HLIERSQVFN ILRMMPKGAA LHLHDIGIVT
MDWLVRNVTY RPHCHICFTP RGIMQFRFAH PTPRPSEKCS KWILLEDYRK RVQNVTEFDD
SLLRNFTLVT QHPEVIYTNQ NVVWSKFETI FFTISGLIHY APVFRDYVFR SMQEFYEDNV
LYMEIRARLL PVYELSGEHH DEEWSVKTYQ EVAQKFVETH PEFIGIKIIY SDHRSKDVAV
IAESIRMAMG LRIKFPTVVA GFDLVGHEDT GHSLHDYKEA LMIPAKDGVK LPYFFHAGET
DWQGTSIDRN ILDALMLNTT RIGHGFALSK HPAVRTYSWK KDIPIEVCPI SNQVLKLVSD
LRNHPVATLM ATGHPMVISS DDPAMFGAKG LSYDFYEVFM GIGGMKADLR TLKQLAMNSI
KYSTLLESEK NTFMEIWKKR WDKFIADVAT K


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