GUCY1A1
entrez
2982
canonical
uniprot
Q02108
canonical
ensembl
ENSG00000164116
resolver
ensp
ENSP00000296518
resolver
ensp
ENSP00000377418
resolver
ensp
ENSP00000412201
resolver
ensp
ENSP00000421493
resolver
ensp
ENSP00000424361
resolver
ensp
ENSP00000426040
resolver
ensp
ENSP00000426968
resolver
ensp
ENSP00000526314
resolver
ensp
ENSP00000526315
resolver
ensp
ENSP00000526316
resolver
ensp
ENSP00000526317
resolver
ensp
ENSP00000526318
resolver
ensp
ENSP00000526322
resolver
ensp
ENSP00000526325
resolver
ensp
ENSP00000526328
resolver
ensp
ENSP00000635223
resolver
ensp
ENSP00000635227
resolver
ensp
ENSP00000672940
resolver
genesymbol
GUCY1A1
resolver
genesymbol_syn
GUC1A3
resolver
genesymbol_syn
GUCSA3
resolver
genesymbol_syn
GUCY1A3
resolver
hgnc
HGNC:4685
resolver
uniprot
B3KU69
resolver
uniprot
D3DP19
resolver
uniprot
D6RDW3
resolver
uniprot
O43843
resolver
uniprot
Q8TAH3
resolver
uniprot_entry
B3KU69_HUMAN
resolver
uniprot_entry
GCYA1_HUMAN
resolver
uniprot_sec
D3DP19
resolver
uniprot_sec
D6RDW3
resolver
uniprot_sec
O43843
resolver
uniprot_sec
Q8TAH3
resolver
activity_regulation
ACTIVITY REGULATION: Activated by nitric oxide in the presence of magnesium or manganese ions (PubMed:23505436, PubMed:24669844, PubMed:9742212). NO binding to the haem of the beta subunit GUCY1B1 induces a conformational change that allosterically activates the catalytic domain (PubMed:31514202). {ECO:0000269|PubMed:23505436, ECO:0000269|PubMed:24669844, ECO:0000269|PubMed:31514202, ECO:0000269|PubMed:9742212}.
uniprot
proteins
amino_acid_sequence
MFCTKLKDLKITGECPFSLLAPGQVPNESSEEAAGSSESCKATVPICQDIPEKNIQESLPQRKTSRSRVYLHTLAESICKLIFPEFERLNVALQRTLAKHKIKESRKSLEREDFEKTIAEQAVAAGVPVEVIKESLGEEVFKICYEEDENILGVVGGTLKDFLNSFSTLLKQSSHCQEAGKRGRLEDASILCLDKEDDFLHVYYFFPKRTTSLILPGIIKAAAHVLYETEVEVSLMPPCFHNDCSEFVNQPYLLYSVHMKSTKPSLSPSKPQSSLVIPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPNFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRRWDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVLIGEQARAQDGLKKRLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQLWQGQVVQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDCPGFVFTPRSREELPPNFPSEIPGICHFLDAYQQGTNSKPCFQKKDVEDGNANFLGKASGID
uniprot
proteins
disease_involvement
DISEASE: Moyamoya disease 6 with or without achalasia (MYMY6) [MIM:615750]: A form of Moyamoya disease, a progressive cerebral angiopathy characterized by bilateral intracranial carotid artery stenosis and telangiectatic vessels in the region of the basal ganglia. The abnormal vessels resemble a 'puff of smoke' (moyamoya) on cerebral angiogram. Affected individuals can develop transient ischemic attacks and/or cerebral infarction, and rupture of the collateral vessels can cause intracranial hemorrhage. Hemiplegia of sudden onset and epileptic seizures constitute the prevailing presentation in childhood, while subarachnoid bleeding occurs more frequently in adults. MYMY6 is characterized by severe cerebral angiopathy and onset of severe achalasia in infancy or early childhood. {ECO:0000269|PubMed:24581742}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
4.6.1.2
uniprot
proteins
function
FUNCTION: Alpha subunit of soluble guanylate cyclase (sGC), a key enzyme in nitric oxide (NO) signaling. sGC functions as a heterodimer consisting of one alpha and one beta subunit. It serves as the primary intracellular receptor for NO, which binds to a heme prosthetic group located on the beta subunit. Upon NO binding, sGC catalyzes the conversion of GTP into cyclic GMP (cGMP), thereby transmitting the NO signal into an ubiquitous intracellular second messenger. {ECO:0000269|PubMed:23505436, ECO:0000269|PubMed:24669844, ECO:0000269|PubMed:9742212}.
uniprot
proteins
mass_dalton
77452
uniprot
proteins
mutagenesis
MUTAGEN 423; /note="D->A: Abolishes activation by NO."; /evidence="ECO:0000269|PubMed:31514202"; MUTAGEN 423; /note="D->P: Does not affect the response to NO."; /evidence="ECO:0000269|PubMed:31514202
uniprot
proteins
protein_family
Adenylyl cyclase class-4/guanylyl cyclase family
uniprot
proteins
pubmed
1352257
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
23505436
uniprot
proteins
pubmed
24581742
uniprot
proteins
pubmed
24669844
uniprot
proteins
pubmed
31514202
uniprot
proteins
pubmed
34535643
uniprot
proteins
pubmed
36972843
uniprot
proteins
pubmed
9742212
uniprot
proteins
sequence_length
690
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
uniprot
proteins