CANT1
entrez
124583
canonical
uniprot
Q8WVQ1
canonical
ensembl
ENSG00000171302
resolver
ensp
ENSP00000307674
resolver
ensp
ENSP00000376241
resolver
ensp
ENSP00000467437
resolver
genesymbol
CANT1
resolver
genesymbol_syn
SHAPY
resolver
hgnc
HGNC:19721
resolver
uniprot
B4DJ54
resolver
uniprot
Q7Z2J7
resolver
uniprot
Q8NG05
resolver
uniprot
Q8NHP0
resolver
uniprot
Q9BSD5
resolver
uniprot_entry
CANT1_HUMAN
resolver
uniprot_sec
B4DJ54
resolver
uniprot_sec
Q7Z2J7
resolver
uniprot_sec
Q8NG05
resolver
uniprot_sec
Q8NHP0
resolver
uniprot_sec
Q9BSD5
resolver
amino_acid_sequence
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLCSHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQEENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDVVNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVALKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
uniprot
proteins
disease_involvement
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, ECO:0000269|PubMed:25486376, ECO:0000269|PubMed:31348018, ECO:0000269|PubMed:31988067, ECO:0000269|PubMed:32907608, ECO:0000269|PubMed:34602954, ECO:0000269|PubMed:41675269}. Note=The disease is caused by variants 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, ECO:0000269|PubMed:39618316}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.1.6
uniprot
proteins
function
FUNCTION: Calcium-dependent nucleotidase with a preference for ribonucleosides diphosphate UDP, GDP and IDP, while having very low activity towards ADP and CDP (PubMed:12234496, PubMed:15006348, PubMed:15248776, PubMed:16835225). In vitro, it can also act with low or negligible efficiency on ribonucletides triphosphate UTP, GTP, ITP, ATP and CTP (PubMed:12234496, PubMed:15248776). Does not hydrolyze AMP and GMP (PubMed:12234496). 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}.
uniprot
proteins
mass_dalton
44840
uniprot
proteins
mutagenesis
MUTAGEN 60; /note="C->S: Loss of dimer formation."; /evidence="ECO:0000269|PubMed:16835225"; MUTAGEN 112; /note="D->A: Loss of nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15006348"; MUTAGEN 114; /note="D->A: Loss of nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15006348, ECO:0000269|PubMed:15248776"; MUTAGEN 139; /note="S->C: Reduces GDPase and ADPase activities 1.7-fold. Severe loss of dimer formation; when associated with S-287."; /evidence="ECO:0000269|PubMed:16835225"; MUTAGEN 152; /note="G->E: Decreased nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15248776"; MUTAGEN 160; /note="E->Y: Increased nucleoside-diphosphatase activity. Forms dimer even at suboptimal Ca(2+) concentrations."; /evidence="ECO:0000269|PubMed:15248776, ECO:0000269|PubMed:16835225"; MUTAGEN 163; /note="R->A: Loss of nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15248776"; MUTAGEN 166; /note="E->Q: Decreased nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15006348"; MUTAGEN 168; /note="S->A: Loss of nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15006348"; MUTAGEN 181; /note="D->A: Loss of nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15248776"; MUTAGEN 182; /note="D->N: Loss of nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15006348"; MUTAGEN 200; /note="I->C: Reduces GDPase activity 2-fold and ADPase activity 2.5-fold. No effect on dimer formation; when associated with S-287."; /evidence="ECO:0000269|PubMed:16835225"; MUTAGEN 202; /note="S->C: Reduces GDPase activity 1.7-fold and ADPase activity 1.5-fold. No effect on dimer formation; when associated with S-287."; /evidence="ECO:0000269|PubMed:16835225"; MUTAGEN 205; /note="D->A: Decreased nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15248776"; MUTAGEN 215; /note="E->Q: Loss of nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15006348"; MUTAGEN 246; /note="E->M: Increases activity 5-fold."; /evidence="ECO:0000269|PubMed:15006348"; MUTAGEN 256; /note="S->C: No effect on GDPase and ADPase activities. No effect on dimer formation; when associated with S-287."; /evidence="ECO:0000269|PubMed:16835225"; MUTAGEN 287; /note="C->S: Reduces GDPase and ADPase activities 1.3-fold."; /evidence="ECO:0000269|PubMed:16835225"; MUTAGEN 301; /note="R->A: Severely decreased nucleoside-diphosphatase activity."; /evidence="ECO:0000269|PubMed:15006348, ECO:0000269|PubMed:15248776"; MUTAGEN 308; /note="S->C: Reduces GDPase activity 1.3-fold and ADPase activity 2-fold. Severe loss of dimer formation; when associated with S-287."; /evidence="ECO:0000269|PubMed:16835225"; MUTAGEN 317; /note="A->C: Reduces GDPase activity 1.7-fold and ADPase activity 1.5-fold. Severe loss of dimer formation; when associated with S-287."; /evidence="ECO:0000269|PubMed:16835225
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:12234496}.
uniprot
proteins
protein_family
Apyrase family
uniprot
proteins
pubmed
12167635
uniprot
proteins
pubmed
12234496
uniprot
proteins
pubmed
12761501
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15006348
uniprot
proteins
pubmed
15248776
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16835225
uniprot
proteins
pubmed
19853239
uniprot
proteins
pubmed
20425819
uniprot
proteins
pubmed
21037275
uniprot
proteins
pubmed
21412251
uniprot
proteins
pubmed
21654728
uniprot
proteins
pubmed
22539336
uniprot
proteins
pubmed
25486376
uniprot
proteins
pubmed
28742282
uniprot
proteins
pubmed
31348018
uniprot
proteins
pubmed
31988067
uniprot
proteins
pubmed
32907608
uniprot
proteins
pubmed
34602954
uniprot
proteins
pubmed
39618316
uniprot
proteins
pubmed
41675269
uniprot
proteins
sequence_length
401
uniprot
proteins
subcellular_location
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.
uniprot
proteins
transmembrane_region
TRANSMEM 45..62; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins