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Soluble calcium-activated nucleotidase 1 (SCAN-1) (EC 3.6.1.6) (Apyrase homolog) (Putative MAPK-activating protein PM09) (Putative NF-kappa-B-activating protein 107)

 CANT1_HUMAN             Reviewed;         401 AA.
Q8WVQ1; B4DJ54; Q7Z2J7; Q8NG05; Q8NHP0; Q9BSD5;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
12-SEP-2018, entry version 144.
RecName: Full=Soluble calcium-activated nucleotidase 1;
Short=SCAN-1;
EC=3.6.1.6 {ECO:0000269|PubMed:12234496, ECO:0000269|PubMed:15006348, ECO:0000269|PubMed:15248776, ECO:0000269|PubMed:16835225};
AltName: Full=Apyrase homolog;
AltName: Full=Putative MAPK-activating protein PM09;
AltName: Full=Putative NF-kappa-B-activating protein 107;
Name=CANT1; Synonyms=SHAPY;
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), FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE
SPECIFICITY.
TISSUE=Mammary tumor;
PubMed=12234496; DOI=10.1016/S0003-9861(02)00420-4;
Smith T., Hicks-Berger C., Kim S., Kirley T.;
"Cloning, expression, and characterization of a soluble calcium-
activated nucleotidase, a human enzyme belonging to a new family of
extracellular nucleotidases.";
Arch. Biochem. Biophys. 406:105-115(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung fibroblast;
PubMed=12761501; DOI=10.1038/sj.onc.1206406;
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
Sugano S.;
"Large-scale identification and characterization of human genes that
activate NF-kappaB and MAPK signaling pathways.";
Oncogene 22:3307-3318(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Mammary gland, and Substantia nigra;
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 MRNA] (ISOFORM 1).
TISSUE=Ovary, Pancreas, and Skin;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 141-401 (ISOFORM 1).
TISSUE=Brain;
PubMed=12167635; DOI=10.1074/jbc.M201656200;
Failer B.U., Braun N., Zimmermann H.;
"Cloning, expression, and functional characterization of a Ca2+-
dependent endoplasmic reticulum nucleoside diphosphatase.";
J. Biol. Chem. 277:36978-36986(2002).
[6]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF ASP-114;
GLY-152; GLU-160; ARG-163; ASP-181; ASP-205 AND ARG-301.
PubMed=15248776; DOI=10.1021/bi049565o;
Yang M., Kirley T.L.;
"Site-directed mutagenesis of human soluble calcium-activated
nucleotidase 1 (hSCAN-1): identification of residues essential for
enzyme activity and the Ca(2+)-induced conformational change.";
Biochemistry 43:9185-9194(2004).
[7]
INVOLVEMENT IN DBQD1.
PubMed=20425819; DOI=10.1002/ajmg.a.33404;
Faden M., Al-Zahrani F., Arafah D., Alkuraya F.S.;
"Mutation of CANT1 causes Desbuquois dysplasia.";
Am. J. Med. Genet. A 152:1157-1160(2010).
[8]
FUNCTION IN PROTEOGLYCAN SYNTHESIS, AND VARIANTS DBQD1 HIS-300;
ARG-303 AND ASN-374.
PubMed=22539336; DOI=10.1002/humu.22104;
Nizon M., Huber C., De Leonardis F., Merrina R., Forlino A.,
Fradin M., Tuysuz B., Abu-Libdeh B.Y., Alanay Y., Albrecht B.,
Al-Gazali L., Basaran S.Y., Clayton-Smith J., Desir J., Gill H.,
Greally M.T., Koparir E., van Maarle M.C., Mackay S., Mortier G.,
Morton J., Sillence D., Vilain C., Young I., Zerres K., Le Merrer M.,
Munnich A., Le Goff C., Rossi A., Cormier-Daire V.;
"Further delineation of CANT1 phenotypic spectrum and demonstration of
its role in proteoglycan synthesis.";
Hum. Mutat. 33:1261-1266(2012).
[9]
INVOLVEMENT IN EDM7, AND VARIANTS EDM7 PHE-171 AND MET-226.
PubMed=28742282; DOI=10.1002/ajmg.a.38349;
Balasubramanian K., Li B., Krakow D., Nevarez L., Ho P.J.,
Ainsworth J.A., Nickerson D.A., Bamshad M.J., Immken L., Lachman R.S.,
Cohn D.H.;
"MED resulting from recessively inherited mutations in the gene
encoding calcium-activated nucleotidase CANT1.";
Am. J. Med. Genet. A 173:2415-2421(2017).
[10]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 71-401 IN COMPLEX WITH
SUBSTRATE ANALOG AND CALCIUM IONS, CATALYTIC ACTIVITY, COFACTOR,
SUBUNIT, AND MUTAGENESIS OF ASP-112; ASP-114; GLU-166; SER-168;
ASP-169; ASP-182; GLU-215; GLU-246 AND ARG-301.
PubMed=15006348; DOI=10.1016/S0092-8674(04)00172-2;
Dai J., Liu J., Deng Y., Smith T.M., Lu M.;
"Structure and protein design of a human platelet function
inhibitor.";
Cell 116:649-659(2004).
[11]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 69-401 IN COMPLEX WITH
CALCIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DIMERIZATION,
SUBCELLULAR LOCATION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-60;
SER-139; GLU-160; ILE-200; SER-202; SER-256; CYS-287; SER-308 AND
ALA-317.
PubMed=16835225; DOI=10.1074/jbc.M604413200;
Yang M., Horii K., Herr A.B., Kirley T.L.;
"Calcium-dependent dimerization of human soluble calcium activated
nucleotidase: characterization of the dimer interface.";
J. Biol. Chem. 281:28307-28317(2006).
[12]
VARIANTS DBQD1 LEU-299; CYS-300 AND HIS-300.
PubMed=19853239; DOI=10.1016/j.ajhg.2009.10.001;
Huber C., Oules B., Bertoli M., Chami M., Fradin M., Alanay Y.,
Al-Gazali L.I., Ausems M.G., Bitoun P., Cavalcanti D.P., Krebs A.,
Le Merrer M., Mortier G., Shafeghati Y., Superti-Furga A.,
Robertson S.P., Le Goff C., Muda A.O., Paterlini-Brechot P.,
Munnich A., Cormier-Daire V.;
"Identification of CANT1 mutations in Desbuquois dysplasia.";
Am. J. Hum. Genet. 85:706-710(2009).
[13]
VARIANT DBQD1 GLU-112.
PubMed=21654728; DOI=10.1038/ejhg.2011.101;
Laccone F., Schoner K., Krabichler B., Kluge B., Schwerdtfeger R.,
Schulze B., Zschocke J., Rehder H.;
"Desbuquois dysplasia type I and fetal hydrops due to novel mutations
in the CANT1 gene.";
Eur. J. Hum. Genet. 19:1133-1137(2011).
[14]
VARIANT DBQD1 MET-226.
PubMed=21412251; DOI=10.1038/jhg.2011.28;
Dai J., Kim O.H., Cho T.J., Miyake N., Song H.R., Karasugi T.,
Sakazume S., Ikema M., Matsui Y., Nagai T., Matsumoto N., Ohashi H.,
Kamatani N., Nishimura G., Furuichi T., Takahashi A., Ikegawa S.;
"A founder mutation of CANT1 common in Korean and Japanese Desbuquois
dysplasia.";
J. Hum. Genet. 56:398-400(2011).
[15]
VARIANTS DBQD1 CYS-125; THR-165; PRO-224; MET-226 AND ASP-360,
CHARACTERIZATION OF VARIANTS DBQD1 CYS-125; THR-165; PRO-224; MET-226;
CYS-300 AND ASP-360, AND CHARACTERIZATION OF VARIANTS THR-323 AND
GLU-391.
PubMed=21037275; DOI=10.1136/jmg.2010.080226;
Furuichi T., Dai J., Cho T.J., Sakazume S., Ikema M., Matsui Y.,
Baynam G., Nagai T., Miyake N., Matsumoto N., Ohashi H., Unger S.,
Superti-Furga A., Kim O.H., Nishimura G., Ikegawa S.;
"CANT1 mutation is also responsible for Desbuquois dysplasia, type 2
and Kim variant.";
J. Med. Genet. 48:32-37(2011).
-!- FUNCTION: Calcium-dependent nucleotidase with a preference for
UDP. The order of activity with different substrates is UDP > GDP
> UTP > GTP. Has very low activity towards ADP and even lower
activity towards ATP. Does not hydrolyze AMP and GMP
(PubMed:12234496, PubMed:15248776, PubMed:15006348,
PubMed:16835225). Involved in proteoglycan synthesis
(PubMed:22539336). {ECO:0000269|PubMed:12234496,
ECO:0000269|PubMed:15006348, ECO:0000269|PubMed:15248776,
ECO:0000269|PubMed:16835225, ECO:0000269|PubMed:22539336}.
-!- CATALYTIC ACTIVITY: A nucleoside diphosphate + H(2)O = a
nucleoside phosphate + phosphate. {ECO:0000269|PubMed:12234496,
ECO:0000269|PubMed:15248776, ECO:0000269|PubMed:16835225}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:12234496,
ECO:0000269|PubMed:15006348, ECO:0000269|PubMed:15248776,
ECO:0000269|PubMed:16835225};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.8.;
-!- SUBUNIT: Monomer (PubMed:12234496, PubMed:15006348). Homodimer;
dimerization is Ca(2+)-dependent (PubMed:16835225). Homodimer;
disulfide-linked (membrane form) (PubMed:16835225).
{ECO:0000269|PubMed:12234496, ECO:0000269|PubMed:15006348,
ECO:0000269|PubMed:16835225}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12234496}; Single-pass type II membrane
protein {ECO:0000269|PubMed:12234496}. Golgi apparatus, Golgi
stack membrane {ECO:0000269|PubMed:12234496}; Single-pass type II
membrane protein {ECO:0000269|PubMed:12234496}. Cell membrane
{ECO:0000269|PubMed:16835225}. Note=Processed form: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8WVQ1-1; Sequence=Displayed;
Name=2;
IsoId=Q8WVQ1-2; Sequence=VSP_013760, VSP_013761;
Name=3;
IsoId=Q8WVQ1-3; Sequence=VSP_054260;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:12234496}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12234496}.
-!- DISEASE: Desbuquois dysplasia 1 (DBQD1) [MIM:251450]: A
chondrodysplasia characterized by severe prenatal and postnatal
growth retardation (less than -5 SD), joint laxity, short
extremities, progressive scoliosis, round face, midface
hypoplasia, prominent bulging eyes. The main radiologic features
are short long bones with metaphyseal splay, a 'Swedish key'
appearance of the proximal femur (exaggerated trochanter), and
advance carpal and tarsal bone age. Two forms of Desbuquois
dysplasia are distinguished on the basis of the presence or
absence of characteristic hand anomalies: an extra ossification
center distal to the second metacarpal, delta phalanx, bifid
distal thumb phalanx, and phalangeal dislocations.
{ECO:0000269|PubMed:19853239, ECO:0000269|PubMed:20425819,
ECO:0000269|PubMed:21037275, ECO:0000269|PubMed:21412251,
ECO:0000269|PubMed:21654728, ECO:0000269|PubMed:22539336}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Epiphyseal dysplasia, multiple, 7 (EDM7) [MIM:617719]: A
form of multiple epiphyseal dysplasia, a generalized skeletal
dysplasia associated with significant morbidity. Joint pain, joint
deformity, waddling gait, and short stature are the main clinical
signs and symptoms. Radiological examination of the skeleton shows
delayed, irregular mineralization of the epiphyseal ossification
centers and of the centers of the carpal and tarsal bones.
Multiple epiphyseal dysplasia is broadly categorized into the more
severe Fairbank and the milder Ribbing types. The Fairbank type is
characterized by shortness of stature, short and stubby fingers,
small epiphyses in several joints, including the knee, ankle,
hand, and hip. The Ribbing type is confined predominantly to the
hip joints and is characterized by hands that are normal and
stature that is normal or near-normal. EDM7 inheritance is
autosomal recessive. {ECO:0000269|PubMed:28742282}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: Not inhibited by azide.
-!- SIMILARITY: Belongs to the apyrase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM94564.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF328554; AAM94564.1; ALT_INIT; mRNA.
EMBL; AB097006; BAC77359.1; -; mRNA.
EMBL; AB097033; BAC77386.1; -; mRNA.
EMBL; AK074687; BAC11139.1; -; mRNA.
EMBL; AK295930; BAG58716.1; -; mRNA.
EMBL; BC005104; AAH05104.1; -; mRNA.
EMBL; BC017655; AAH17655.1; -; mRNA.
EMBL; BC065038; AAH65038.1; -; mRNA.
EMBL; AJ312208; CAC85468.1; -; mRNA.
CCDS; CCDS11760.1; -. [Q8WVQ1-1]
RefSeq; NP_001153244.1; NM_001159772.1. [Q8WVQ1-1]
RefSeq; NP_001153245.1; NM_001159773.1. [Q8WVQ1-1]
RefSeq; NP_620148.1; NM_138793.3. [Q8WVQ1-1]
RefSeq; XP_005257078.1; XM_005257021.1. [Q8WVQ1-1]
RefSeq; XP_005257079.1; XM_005257022.1. [Q8WVQ1-1]
RefSeq; XP_006721746.1; XM_006721683.1. [Q8WVQ1-1]
RefSeq; XP_011522593.1; XM_011524291.1. [Q8WVQ1-1]
RefSeq; XP_011522595.1; XM_011524293.1. [Q8WVQ1-1]
RefSeq; XP_011522596.1; XM_011524294.1. [Q8WVQ1-1]
RefSeq; XP_011522597.1; XM_011524295.2. [Q8WVQ1-1]
UniGene; Hs.8859; -.
PDB; 1S18; X-ray; 1.70 A; A/B=71-401.
PDB; 1S1D; X-ray; 1.60 A; A/B=71-401.
PDB; 2H2N; X-ray; 2.30 A; A/B=69-401.
PDB; 2H2U; X-ray; 2.40 A; A/B=69-401.
PDBsum; 1S18; -.
PDBsum; 1S1D; -.
PDBsum; 2H2N; -.
PDBsum; 2H2U; -.
ProteinModelPortal; Q8WVQ1; -.
SMR; Q8WVQ1; -.
BioGrid; 125875; 22.
IntAct; Q8WVQ1; 3.
STRING; 9606.ENSP00000307674; -.
DrugBank; DB03486; Phosphomethylphosphonic Acid Guanosyl Ester.
DrugBank; DB03754; Tris.
iPTMnet; Q8WVQ1; -.
PhosphoSitePlus; Q8WVQ1; -.
BioMuta; CANT1; -.
DMDM; 66774052; -.
EPD; Q8WVQ1; -.
MaxQB; Q8WVQ1; -.
PaxDb; Q8WVQ1; -.
PeptideAtlas; Q8WVQ1; -.
PRIDE; Q8WVQ1; -.
ProteomicsDB; 74813; -.
ProteomicsDB; 74814; -. [Q8WVQ1-2]
Ensembl; ENST00000302345; ENSP00000307674; ENSG00000171302. [Q8WVQ1-1]
Ensembl; ENST00000392446; ENSP00000376241; ENSG00000171302. [Q8WVQ1-1]
Ensembl; ENST00000591773; ENSP00000467437; ENSG00000171302. [Q8WVQ1-1]
Ensembl; ENST00000620915; ENSP00000477798; ENSG00000171302. [Q8WVQ1-1]
GeneID; 124583; -.
KEGG; hsa:124583; -.
UCSC; uc002jwj.4; human. [Q8WVQ1-1]
CTD; 124583; -.
DisGeNET; 124583; -.
EuPathDB; HostDB:ENSG00000171302.16; -.
GeneCards; CANT1; -.
HGNC; HGNC:19721; CANT1.
HPA; HPA019627; -.
HPA; HPA019639; -.
HPA; HPA022818; -.
MalaCards; CANT1; -.
MIM; 251450; phenotype.
MIM; 613165; gene.
MIM; 617719; phenotype.
neXtProt; NX_Q8WVQ1; -.
OpenTargets; ENSG00000171302; -.
Orphanet; 1425; Desbuquois syndrome.
PharmGKB; PA134984439; -.
eggNOG; KOG4494; Eukaryota.
eggNOG; ENOG410XS4T; LUCA.
GeneTree; ENSGT00390000012872; -.
HOGENOM; HOG000008129; -.
HOVERGEN; HBG059824; -.
InParanoid; Q8WVQ1; -.
KO; K12304; -.
OMA; GSMGKEW; -.
OrthoDB; EOG091G0DL5; -.
PhylomeDB; Q8WVQ1; -.
TreeFam; TF315248; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; CANT1; human.
EvolutionaryTrace; Q8WVQ1; -.
GeneWiki; CANT1; -.
GenomeRNAi; 124583; -.
PRO; PR:Q8WVQ1; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000171302; Expressed in 214 organ(s), highest expression level in colonic mucosa.
CleanEx; HS_CANT1; -.
ExpressionAtlas; Q8WVQ1; baseline and differential.
Genevisible; Q8WVQ1; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0043262; F:adenosine-diphosphatase activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:UniProtKB.
Gene3D; 2.120.10.100; -; 1.
InterPro; IPR009283; Apyrase.
InterPro; IPR036258; Apyrase_sf.
PANTHER; PTHR13023; PTHR13023; 1.
Pfam; PF06079; Apyrase; 1.
SUPFAM; SSF101887; SSF101887; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell membrane;
Complete proteome; Disease mutation; Disulfide bond; Dwarfism;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase;
Membrane; Metal-binding; Polymorphism; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 401 Soluble calcium-activated nucleotidase 1.
/FTId=PRO_0000209925.
TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.
TRANSMEM 45 62 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 63 401 Lumenal. {ECO:0000255}.
METAL 168 168 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1S18,
ECO:0000244|PDB:1S1D,
ECO:0000244|PDB:2H2N,
ECO:0000244|PDB:2H2U,
ECO:0000269|PubMed:15006348,
ECO:0000269|PubMed:16835225}.
METAL 169 169 Calcium. {ECO:0000244|PDB:1S18,
ECO:0000244|PDB:2H2N,
ECO:0000244|PDB:2H2U,
ECO:0000269|PubMed:15006348,
ECO:0000269|PubMed:16835225}.
METAL 215 215 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1S18,
ECO:0000244|PDB:1S1D,
ECO:0000244|PDB:2H2N,
ECO:0000244|PDB:2H2U,
ECO:0000269|PubMed:15006348,
ECO:0000269|PubMed:16835225}.
METAL 284 284 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1S18,
ECO:0000244|PDB:1S1D,
ECO:0000244|PDB:2H2N,
ECO:0000244|PDB:2H2U,
ECO:0000269|PubMed:15006348,
ECO:0000269|PubMed:16835225}.
METAL 345 345 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1S18,
ECO:0000244|PDB:1S1D,
ECO:0000244|PDB:2H2N,
ECO:0000244|PDB:2H2U,
ECO:0000269|PubMed:15006348,
ECO:0000269|PubMed:16835225}.
METAL 396 396 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1S18,
ECO:0000244|PDB:1S1D,
ECO:0000244|PDB:2H2N,
ECO:0000244|PDB:2H2U,
ECO:0000269|PubMed:15006348,
ECO:0000269|PubMed:16835225}.
SITE 160 160 Important for dimer formation.
{ECO:0000269|PubMed:16835225}.
SITE 200 200 Important for dimer formation.
{ECO:0000269|PubMed:16835225}.
SITE 202 202 Important for dimer formation.
{ECO:0000269|PubMed:16835225}.
SITE 256 256 Important for dimer formation.
{ECO:0000269|PubMed:16835225}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 60 60 Interchain.
{ECO:0000269|PubMed:16835225}.
VAR_SEQ 41 91 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054260.
VAR_SEQ 220 245 KDERLYVGGLGKEWTTTTGDVVNENP -> REIVRKRWRLV
KQVSHVGVLGQWIQR (in isoform 2).
{ECO:0000303|PubMed:12761501}.
/FTId=VSP_013760.
VAR_SEQ 246 401 Missing (in isoform 2).
{ECO:0000303|PubMed:12761501}.
/FTId=VSP_013761.
VARIANT 112 112 D -> E (in DBQD1; dbSNP:rs749246739).
{ECO:0000269|PubMed:21654728}.
/FTId=VAR_068655.
VARIANT 125 125 W -> C (in DBQD1; severely affects
activity; dbSNP:rs587776898).
{ECO:0000269|PubMed:21037275}.
/FTId=VAR_068656.
VARIANT 165 165 M -> T (in DBQD1; severely affects
activity). {ECO:0000269|PubMed:21037275}.
/FTId=VAR_068657.
VARIANT 171 171 I -> F (in EDM7; unknown pathological
significance; dbSNP:rs1014317450).
{ECO:0000269|PubMed:28742282}.
/FTId=VAR_080400.
VARIANT 224 224 L -> P (in DBQD1; affects protein
stability and secretion;
dbSNP:rs150181226).
{ECO:0000269|PubMed:21037275}.
/FTId=VAR_068658.
VARIANT 226 226 V -> M (in DBQD1 and EDM7; severely
affects activity; dbSNP:rs377546036).
{ECO:0000269|PubMed:21037275,
ECO:0000269|PubMed:21412251,
ECO:0000269|PubMed:28742282}.
/FTId=VAR_068659.
VARIANT 299 299 P -> L (in DBQD1; dbSNP:rs267606700).
{ECO:0000269|PubMed:19853239}.
/FTId=VAR_062980.
VARIANT 300 300 R -> C (in DBQD1; severely affects
activity; dbSNP:rs267606701).
{ECO:0000269|PubMed:19853239,
ECO:0000269|PubMed:21037275}.
/FTId=VAR_062981.
VARIANT 300 300 R -> H (in DBQD1; dbSNP:rs267606699).
{ECO:0000269|PubMed:19853239,
ECO:0000269|PubMed:22539336}.
/FTId=VAR_062982.
VARIANT 303 303 S -> R (in DBQD1).
{ECO:0000269|PubMed:22539336}.
/FTId=VAR_068660.
VARIANT 323 323 A -> T (polymorphism; does not affect
activity; dbSNP:rs9903215).
{ECO:0000269|PubMed:21037275}.
/FTId=VAR_068661.
VARIANT 360 360 A -> D (in DBQD1; affects protein
secretion; dbSNP:rs387907081).
{ECO:0000269|PubMed:21037275}.
/FTId=VAR_068662.
VARIANT 374 374 I -> N (in DBQD1).
{ECO:0000269|PubMed:22539336}.
/FTId=VAR_068663.
VARIANT 391 391 G -> E (polymorphism; does not affect
activity; dbSNP:rs34082669).
{ECO:0000269|PubMed:21037275}.
/FTId=VAR_068664.
MUTAGEN 60 60 C->S: Loss of dimer formation.
{ECO:0000269|PubMed:16835225}.
MUTAGEN 112 112 D->A: Reduces activity by 99%.
{ECO:0000269|PubMed:15006348}.
MUTAGEN 114 114 D->A: Reduces activity by 99%.
{ECO:0000269|PubMed:15006348,
ECO:0000269|PubMed:15248776}.
MUTAGEN 139 139 S->C: Reduces GDPase and ADPase
activities 1.7-fold. Severe loss of dimer
formation; when associated with S-287.
{ECO:0000269|PubMed:16835225}.
MUTAGEN 152 152 G->E: Slightly reduced activity.
{ECO:0000269|PubMed:15248776}.
MUTAGEN 160 160 E->Y: Increases GDPase activity 2-fold
and ADPase activity 5-fold. Forms dimer
even at suboptimal Ca(2+) concentrations.
{ECO:0000269|PubMed:15248776,
ECO:0000269|PubMed:16835225}.
MUTAGEN 163 163 R->A: Reduces activity by 98%.
{ECO:0000269|PubMed:15248776}.
MUTAGEN 166 166 E->Q: Reduces activity by 95%.
{ECO:0000269|PubMed:15006348}.
MUTAGEN 168 168 S->A: Reduces activity by over 99.9%.
{ECO:0000269|PubMed:15006348}.
MUTAGEN 169 169 D->N: Reduces activity by 96%.
{ECO:0000269|PubMed:15006348}.
MUTAGEN 181 181 D->A: Loss of activity.
{ECO:0000269|PubMed:15248776}.
MUTAGEN 182 182 D->N: Reduces activity by over 99.9%.
{ECO:0000269|PubMed:15006348}.
MUTAGEN 200 200 I->C: Reduces GDPase activity 2-fold and
ADPase activity 2.5-fold. No effect on
dimer formation; when associated with S-
287. {ECO:0000269|PubMed:16835225}.
MUTAGEN 202 202 S->C: Reduces GDPase activity 1.7-fold
and ADPase activity 1.5-fold. No effect
on dimer formation; when associated with
S-287. {ECO:0000269|PubMed:16835225}.
MUTAGEN 205 205 D->A: Slightly reduced activity.
{ECO:0000269|PubMed:15248776}.
MUTAGEN 215 215 E->Q: Reduces activity by 99%.
{ECO:0000269|PubMed:15006348}.
MUTAGEN 246 246 E->M: Increases activity 5-fold.
{ECO:0000269|PubMed:15006348}.
MUTAGEN 256 256 S->C: No effect on GDPase and ADPase
activities. No effect on dimer formation;
when associated with S-287.
{ECO:0000269|PubMed:16835225}.
MUTAGEN 287 287 C->S: Reduces GDPase and ADPase
activities 1.3-fold.
{ECO:0000269|PubMed:16835225}.
MUTAGEN 301 301 R->A: Reduces activity by 99%.
{ECO:0000269|PubMed:15006348,
ECO:0000269|PubMed:15248776}.
MUTAGEN 308 308 S->C: Reduces GDPase activity 1.3-fold
and ADPase activity 2-fold. Severe loss
of dimer formation; when associated with
S-287. {ECO:0000269|PubMed:16835225}.
MUTAGEN 317 317 A->C: Reduces GDPase activity 1.7-fold
and ADPase activity 1.5-fold. Severe loss
of dimer formation; when associated with
S-287. {ECO:0000269|PubMed:16835225}.
STRAND 92 94 {ECO:0000244|PDB:1S1D}.
STRAND 97 99 {ECO:0000244|PDB:1S1D}.
STRAND 102 112 {ECO:0000244|PDB:1S1D}.
HELIX 114 117 {ECO:0000244|PDB:1S1D}.
STRAND 125 137 {ECO:0000244|PDB:1S1D}.
STRAND 143 147 {ECO:0000244|PDB:1S1D}.
STRAND 152 157 {ECO:0000244|PDB:1S1D}.
STRAND 158 160 {ECO:0000244|PDB:2H2U}.
STRAND 167 173 {ECO:0000244|PDB:1S1D}.
STRAND 176 181 {ECO:0000244|PDB:1S1D}.
TURN 182 184 {ECO:0000244|PDB:1S1D}.
STRAND 186 191 {ECO:0000244|PDB:1S1D}.
STRAND 194 200 {ECO:0000244|PDB:1S1D}.
TURN 204 207 {ECO:0000244|PDB:1S1D}.
STRAND 208 211 {ECO:0000244|PDB:1S1D}.
STRAND 216 220 {ECO:0000244|PDB:1S1D}.
STRAND 223 227 {ECO:0000244|PDB:1S1D}.
STRAND 240 242 {ECO:0000244|PDB:1S1D}.
HELIX 244 246 {ECO:0000244|PDB:1S1D}.
STRAND 247 251 {ECO:0000244|PDB:1S1D}.
STRAND 257 261 {ECO:0000244|PDB:1S1D}.
HELIX 263 272 {ECO:0000244|PDB:1S1D}.
STRAND 280 282 {ECO:0000244|PDB:1S1D}.
STRAND 286 289 {ECO:0000244|PDB:1S1D}.
TURN 290 293 {ECO:0000244|PDB:1S1D}.
STRAND 294 297 {ECO:0000244|PDB:1S1D}.
STRAND 300 305 {ECO:0000244|PDB:1S1D}.
HELIX 309 312 {ECO:0000244|PDB:1S1D}.
STRAND 319 323 {ECO:0000244|PDB:1S1D}.
STRAND 330 334 {ECO:0000244|PDB:1S1D}.
STRAND 342 349 {ECO:0000244|PDB:1S1D}.
STRAND 357 366 {ECO:0000244|PDB:1S1D}.
STRAND 369 378 {ECO:0000244|PDB:1S1D}.
STRAND 383 400 {ECO:0000244|PDB:1S1D}.
SEQUENCE 401 AA; 44840 MW; 5B78EB24C0B2C4CA CRC64;
MPVQLSEHPE WNESMHSLRI SVGGLPVLAS MTKAADPRFR PRWKVILTFF VGAAILWLLC
SHRPAPGRPP THNAHNWRLG QAPANWYNDT YPLSPPQRTP AGIRYRIAVI ADLDTESRAQ
EENTWFSYLK KGYLTLSDSG DKVAVEWDKD HGVLESHLAE KGRGMELSDL IVFNGKLYSV
DDRTGVVYQI EGSKAVPWVI LSDGDGTVEK GFKAEWLAVK DERLYVGGLG KEWTTTTGDV
VNENPEWVKV VGYKGSVDHE NWVSNYNALR AAAGIQPPGY LIHESACWSD TLQRWFFLPR
RASQERYSEK DDERKGANLL LSASPDFGDI AVSHVGAVVP THGFSSFKFI PNTDDQIIVA
LKSEEDSGRV ASYIMAFTLD GRFLLPETKI GSVKYEGIEF I


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