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UniProtKB - Q8WVQ1 (CANT1_HUMAN)

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Protein

Soluble calcium-activated nucleotidase 1

Gene

CANT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).5 Publications

Miscellaneous

Not inhibited by azide.

Catalytic activityi

A nucleoside diphosphate + H2O = a nucleoside phosphate + phosphate.3 Publications

Cofactori

Ca2+4 Publications

pH dependencei

Optimum pH is 6.8.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei160Important for dimer formation1 Publication1
Metal bindingi168Calcium; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi169CalciumCombined sources2 Publications1
Sitei200Important for dimer formation1 Publication1
Sitei202Important for dimer formation1 Publication1
Metal bindingi215Calcium; via carbonyl oxygenCombined sources2 Publications1
Sitei256Important for dimer formation1 Publication1
Metal bindingi284Calcium; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi345Calcium; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi396Calcium; via carbonyl oxygenCombined sources2 Publications1

GO - Molecular functioni

  • adenosine-diphosphatase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • guanosine-diphosphatase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • uridine-diphosphatase activity Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • neutrophil degranulation Source: Reactome
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • proteoglycan biosynthetic process Source: UniProtKB
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHydrolase
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-6798695 Neutrophil degranulation

Names & Taxonomyi

Protein namesi
Recommended name:
Soluble calcium-activated nucleotidase 1 (EC:3.6.1.64 Publications)
Short name:
SCAN-1
Alternative name(s):
Apyrase homolog
Putative MAPK-activating protein PM09
Putative NF-kappa-B-activating protein 107
Gene namesi
Name:CANT1
Synonyms:SHAPY
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000171302.16
HGNCiHGNC:19721 CANT1
MIMi613165 gene
neXtProtiNX_Q8WVQ1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 44CytoplasmicSequence analysisAdd BLAST44
Transmembranei45 – 62Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST18
Topological domaini63 – 401LumenalSequence analysisAdd BLAST339

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Desbuquois dysplasia 1 (DBQD1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:251450
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_068655112D → E in DBQD1. 1 PublicationCorresponds to variant dbSNP:rs749246739Ensembl.1
Natural variantiVAR_068656125W → C in DBQD1; severely affects activity. 1 PublicationCorresponds to variant dbSNP:rs587776898EnsemblClinVar.1
Natural variantiVAR_068657165M → T in DBQD1; severely affects activity. 1 Publication1
Natural variantiVAR_068658224L → P in DBQD1; affects protein stability and secretion. 1 PublicationCorresponds to variant dbSNP:rs150181226EnsemblClinVar.1
Natural variantiVAR_062980299P → L in DBQD1. 1 PublicationCorresponds to variant dbSNP:rs267606700EnsemblClinVar.1
Natural variantiVAR_062981300R → C in DBQD1; severely affects activity. 2 PublicationsCorresponds to variant dbSNP:rs267606701EnsemblClinVar.1
Natural variantiVAR_062982300R → H in DBQD1. 2 PublicationsCorresponds to variant dbSNP:rs267606699EnsemblClinVar.1
Natural variantiVAR_068660303S → R in DBQD1. 1 Publication1
Natural variantiVAR_068662360A → D in DBQD1; affects protein secretion. 1 PublicationCorresponds to variant dbSNP:rs387907081EnsemblClinVar.1
Natural variantiVAR_068663374I → N in DBQD1. 1 Publication1
Epiphyseal dysplasia, multiple, 7 (EDM7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:617719
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_080400171I → F in EDM7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1014317450Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi60C → S: Loss of dimer formation. 1 Publication1
Mutagenesisi112D → A: Reduces activity by 99%. 1 Publication1
Mutagenesisi114D → A: Reduces activity by 99%. 2 Publications1
Mutagenesisi139S → C: Reduces GDPase and ADPase activities 1.7-fold. Severe loss of dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi152G → E: Slightly reduced activity. 1 Publication1
Mutagenesisi160E → Y: Increases GDPase activity 2-fold and ADPase activity 5-fold. Forms dimer even at suboptimal Ca(2+) concentrations. 2 Publications1
Mutagenesisi163R → A: Reduces activity by 98%. 1 Publication1
Mutagenesisi166E → Q: Reduces activity by 95%. 1 Publication1
Mutagenesisi168S → A: Reduces activity by over 99.9%. 1 Publication1
Mutagenesisi169D → N: Reduces activity by 96%. 1 Publication1
Mutagenesisi181D → A: Loss of activity. 1 Publication1
Mutagenesisi182D → N: Reduces activity by over 99.9%. 1 Publication1
Mutagenesisi200I → C: Reduces GDPase activity 2-fold and ADPase activity 2.5-fold. No effect on dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi202S → C: Reduces GDPase activity 1.7-fold and ADPase activity 1.5-fold. No effect on dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi205D → A: Slightly reduced activity. 1 Publication1
Mutagenesisi215E → Q: Reduces activity by 99%. 1 Publication1
Mutagenesisi246E → M: Increases activity 5-fold. 1 Publication1
Mutagenesisi256S → C: No effect on GDPase and ADPase activities. No effect on dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi287C → S: Reduces GDPase and ADPase activities 1.3-fold. 1 Publication1
Mutagenesisi301R → A: Reduces activity by 99%. 2 Publications1
Mutagenesisi308S → C: Reduces GDPase activity 1.3-fold and ADPase activity 2-fold. Severe loss of dimer formation; when associated with S-287. 1 Publication1
Mutagenesisi317A → C: Reduces GDPase activity 1.7-fold and ADPase activity 1.5-fold. Severe loss of dimer formation; when associated with S-287. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi124583
MalaCardsiCANT1
MIMi251450 phenotype
617719 phenotype
OpenTargetsiENSG00000171302
Orphaneti1425 Desbuquois syndrome
PharmGKBiPA134984439

Chemistry databases

DrugBankiDB03486 Phosphomethylphosphonic Acid Guanosyl Ester
DB03754 Tris

Polymorphism and mutation databases

BioMutaiCANT1
DMDMi66774052

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002099251 – 401Soluble calcium-activated nucleotidase 1Add BLAST401

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi60Interchain1 Publication
Glycosylationi88N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8WVQ1
MaxQBiQ8WVQ1
PaxDbiQ8WVQ1
PeptideAtlasiQ8WVQ1
PRIDEiQ8WVQ1
ProteomicsDBi74813
74814 [Q8WVQ1-2]

PTM databases

iPTMnetiQ8WVQ1
PhosphoSitePlusiQ8WVQ1

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000171302
CleanExiHS_CANT1
ExpressionAtlasiQ8WVQ1 baseline and differential
GenevisibleiQ8WVQ1 HS

Organism-specific databases

HPAiHPA019627
HPA019639
HPA022818

Interactioni

Subunit structurei

Monomer (PubMed:12234496, PubMed:15006348). Homodimer; dimerization is Ca2+-dependent (PubMed:16835225). Homodimer; disulfide-linked (membrane form) (PubMed:16835225).3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi125875, 22 interactors
IntActiQ8WVQ1, 3 interactors
STRINGi9606.ENSP00000307674

Structurei

Secondary structure

1401
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi92 – 94Combined sources3
Beta strandi97 – 99Combined sources3
Beta strandi102 – 112Combined sources11
Helixi114 – 117Combined sources4
Beta strandi125 – 137Combined sources13
Beta strandi143 – 147Combined sources5
Beta strandi152 – 157Combined sources6
Beta strandi158 – 160Combined sources3
Beta strandi167 – 173Combined sources7
Beta strandi176 – 181Combined sources6
Turni182 – 184Combined sources3
Beta strandi186 – 191Combined sources6
Beta strandi194 – 200Combined sources7
Turni204 – 207Combined sources4
Beta strandi208 – 211Combined sources4
Beta strandi216 – 220Combined sources5
Beta strandi223 – 227Combined sources5
Beta strandi240 – 242Combined sources3
Helixi244 – 246Combined sources3
Beta strandi247 – 251Combined sources5
Beta strandi257 – 261Combined sources5
Helixi263 – 272Combined sources10
Beta strandi280 – 282Combined sources3
Beta strandi286 – 289Combined sources4
Turni290 – 293Combined sources4
Beta strandi294 – 297Combined sources4
Beta strandi300 – 305Combined sources6
Helixi309 – 312Combined sources4
Beta strandi319 – 323Combined sources5
Beta strandi330 – 334Combined sources5
Beta strandi342 – 349Combined sources8
Beta strandi357 – 366Combined sources10
Beta strandi369 – 378Combined sources10
Beta strandi383 – 400Combined sources18

3D structure databases

ProteinModelPortaliQ8WVQ1
SMRiQ8WVQ1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WVQ1

Family & Domainsi

Sequence similaritiesi

Belongs to the apyrase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4494 Eukaryota
ENOG410XS4T LUCA
GeneTreeiENSGT00390000012872
HOGENOMiHOG000008129
HOVERGENiHBG059824
InParanoidiQ8WVQ1
KOiK12304
OMAiGSMGKEW
OrthoDBiEOG091G0DL5
PhylomeDBiQ8WVQ1
TreeFamiTF315248

Family and domain databases

Gene3Di2.120.10.100, 1 hit
InterProiView protein in InterPro
IPR009283 Apyrase
IPR036258 Apyrase_sf
PANTHERiPTHR13023 PTHR13023, 1 hit
PfamiView protein in Pfam
PF06079 Apyrase, 1 hit
SUPFAMiSSF101887 SSF101887, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WVQ1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPVQLSEHPE WNESMHSLRI SVGGLPVLAS MTKAADPRFR PRWKVILTFF 
        60         70         80         90        100
VGAAILWLLC SHRPAPGRPP THNAHNWRLG QAPANWYNDT YPLSPPQRTP 
       110        120        130        140        150
AGIRYRIAVI ADLDTESRAQ EENTWFSYLK KGYLTLSDSG DKVAVEWDKD 
       160        170        180        190        200
HGVLESHLAE KGRGMELSDL IVFNGKLYSV DDRTGVVYQI EGSKAVPWVI 
       210        220        230        240        250
LSDGDGTVEK GFKAEWLAVK DERLYVGGLG KEWTTTTGDV VNENPEWVKV 
       260        270        280        290        300
VGYKGSVDHE NWVSNYNALR AAAGIQPPGY LIHESACWSD TLQRWFFLPR 
       310        320        330        340        350
RASQERYSEK DDERKGANLL LSASPDFGDI AVSHVGAVVP THGFSSFKFI 
       360        370        380        390        400
PNTDDQIIVA LKSEEDSGRV ASYIMAFTLD GRFLLPETKI GSVKYEGIEF 

I
Length:401
Mass (Da):44,840
Last modified:March 1, 2002 - v1
Checksum:i5B78EB24C0B2C4CA
GO
Isoform 2 (identifier: Q8WVQ1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     220-245: KDERLYVGGLGKEWTTTTGDVVNENP → REIVRKRWRLVKQVSHVGVLGQWIQR
     246-401: Missing.

Show »
Length:245
Mass (Da):27,762
Checksum:i0D53611DA70ADCAF
GO
Isoform 3 (identifier: Q8WVQ1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     41-91: Missing.

Note: No experimental confirmation available.
Show »
Length:350
Mass (Da):38,946
Checksum:i3E074A6D59449646
GO

Sequence cautioni

The sequence AAM94564 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_068655112D → E in DBQD1. 1 PublicationCorresponds to variant dbSNP:rs749246739Ensembl.1
Natural variantiVAR_068656125W → C in DBQD1; severely affects activity. 1 PublicationCorresponds to variant dbSNP:rs587776898EnsemblClinVar.1
Natural variantiVAR_068657165M → T in DBQD1; severely affects activity. 1 Publication1
Natural variantiVAR_080400171I → F in EDM7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1014317450Ensembl.1
Natural variantiVAR_068658224L → P in DBQD1; affects protein stability and secretion. 1 PublicationCorresponds to variant dbSNP:rs150181226EnsemblClinVar.1
Natural variantiVAR_068659226V → M in DBQD1 and EDM7; severely affects activity. 3 PublicationsCorresponds to variant dbSNP:rs377546036EnsemblClinVar.1
Natural variantiVAR_062980299P → L in DBQD1. 1 PublicationCorresponds to variant dbSNP:rs267606700EnsemblClinVar.1
Natural variantiVAR_062981300R → C in DBQD1; severely affects activity. 2 PublicationsCorresponds to variant dbSNP:rs267606701EnsemblClinVar.1
Natural variantiVAR_062982300R → H in DBQD1. 2 PublicationsCorresponds to variant dbSNP:rs267606699EnsemblClinVar.1
Natural variantiVAR_068660303S → R in DBQD1. 1 Publication1
Natural variantiVAR_068661323A → T Polymorphism; does not affect activity. 1 PublicationCorresponds to variant dbSNP:rs9903215EnsemblClinVar.1
Natural variantiVAR_068662360A → D in DBQD1; affects protein secretion. 1 PublicationCorresponds to variant dbSNP:rs387907081EnsemblClinVar.1
Natural variantiVAR_068663374I → N in DBQD1. 1 Publication1
Natural variantiVAR_068664391G → E Polymorphism; does not affect activity. 1 PublicationCorresponds to variant dbSNP:rs34082669EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05426041 – 91Missing in isoform 3. 1 PublicationAdd BLAST51
Alternative sequenceiVSP_013760220 – 245KDERL…VNENP → REIVRKRWRLVKQVSHVGVL GQWIQR in isoform 2. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_013761246 – 401Missing in isoform 2. 1 PublicationAdd BLAST156

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF328554 mRNA Translation: AAM94564.1 Different initiation.
AB097006 mRNA Translation: BAC77359.1
AB097033 mRNA Translation: BAC77386.1
AK074687 mRNA Translation: BAC11139.1
AK295930 mRNA Translation: BAG58716.1
BC005104 mRNA Translation: AAH05104.1
BC017655 mRNA Translation: AAH17655.1
BC065038 mRNA Translation: AAH65038.1
AJ312208 mRNA Translation: CAC85468.1
CCDSiCCDS11760.1 [Q8WVQ1-1]
RefSeqiNP_001153244.1, NM_001159772.1 [Q8WVQ1-1]
NP_001153245.1, NM_001159773.1 [Q8WVQ1-1]
NP_620148.1, NM_138793.3 [Q8WVQ1-1]
XP_005257078.1, XM_005257021.1 [Q8WVQ1-1]
XP_005257079.1, XM_005257022.1 [Q8WVQ1-1]
XP_006721746.1, XM_006721683.1 [Q8WVQ1-1]
XP_011522593.1, XM_011524291.1 [Q8WVQ1-1]
XP_011522595.1, XM_011524293.1 [Q8WVQ1-1]
XP_011522596.1, XM_011524294.1 [Q8WVQ1-1]
XP_011522597.1, XM_011524295.2 [Q8WVQ1-1]
UniGeneiHs.8859

Genome annotation databases

EnsembliENST00000302345; ENSP00000307674; ENSG00000171302 [Q8WVQ1-1]
ENST00000392446; ENSP00000376241; ENSG00000171302 [Q8WVQ1-1]
ENST00000591773; ENSP00000467437; ENSG00000171302 [Q8WVQ1-1]
ENST00000620915; ENSP00000477798; ENSG00000171302 [Q8WVQ1-1]
GeneIDi124583
KEGGihsa:124583
UCSCiuc002jwj.4 human [Q8WVQ1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCANT1_HUMAN
AccessioniPrimary (citable) accession number: Q8WVQ1
Secondary accession number(s): B4DJ54
, Q7Z2J7, Q8NG05, Q8NHP0, Q9BSD5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: March 1, 2002
Last modified: July 18, 2018
This is version 143 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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