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Protein

Guanylate cyclase soluble subunit alpha-3

Gene

GUCY1A3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

GTP = 3',5'-cyclic GMP + diphosphate.3 Publications

Cofactori

Mg2+2 Publications, Mn2+2 PublicationsNote: Has also activity with Mn2+ (in vitro).2 Publications

Enzyme regulationi

Activated by nitric oxide in the presence of magnesium or manganese ions.1 Publication

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • guanylate cyclase activity Source: UniProtKB
  • heme binding Source: InterPro
  • receptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cGMP biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.2. 2681.
ReactomeiR-HSA-392154. Nitric oxide stimulates guanylate cyclase.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate cyclase soluble subunit alpha-3 (EC:4.6.1.23 Publications)
Short name:
GCS-alpha-3
Alternative name(s):
GCS-alpha-1
Soluble guanylate cyclase large subunit
Gene namesi
Name:GUCY1A3
Synonyms:GUC1A3, GUCSA3, GUCY1A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:4685. GUCY1A3.

Subcellular locationi

GO - Cellular componenti

  • guanylate cyclase complex, soluble Source: UniProtKB
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Moyamoya disease 6 with achalasia (MYMY6)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615750

Organism-specific databases

MalaCardsiGUCY1A3.
MIMi615750. phenotype.
Orphaneti401945. Moyamoya disease with early-onset achalasia.
PharmGKBiPA29067.

Chemistry

ChEMBLiCHEMBL3137281.

Polymorphism and mutation databases

BioMutaiGUCY1A3.
DMDMi7404351.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 690690Guanylate cyclase soluble subunit alpha-3PRO_0000074110Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02108.
PaxDbiQ02108.
PeptideAtlasiQ02108.
PRIDEiQ02108.

PTM databases

iPTMnetiQ02108.
PhosphoSiteiQ02108.

Expressioni

Tissue specificityi

Detected in brain cortex and lung (at protein level).1 Publication

Gene expression databases

BgeeiQ02108.
CleanExiHS_GUCY1A3.
ExpressionAtlasiQ02108. baseline and differential.
GenevisibleiQ02108. HS.

Organism-specific databases

HPAiCAB010887.

Interactioni

Subunit structurei

The active enzyme is formed by a heterodimer of an alpha and a beta subunit. Heterodimer with GUCY1B3 (PubMed:9742212, PubMed:23505436, PubMed:24669844).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GUCY1B3Q021532EBI-3910037,EBI-6911707

Protein-protein interaction databases

BioGridi109237. 9 interactions.
IntActiQ02108. 3 interactions.
STRINGi9606.ENSP00000296518.

Structurei

Secondary structure

1
690
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi472 – 48716Combined sources
Helixi490 – 4967Combined sources
Helixi499 – 51921Combined sources
Beta strandi523 – 5253Combined sources
Beta strandi533 – 5408Combined sources
Helixi545 – 56016Combined sources
Beta strandi568 – 5703Combined sources
Beta strandi573 – 58715Combined sources
Beta strandi589 – 5913Combined sources
Beta strandi593 – 5986Combined sources
Helixi599 – 60911Combined sources
Beta strandi616 – 6183Combined sources
Helixi620 – 6267Combined sources
Beta strandi632 – 6365Combined sources
Beta strandi655 – 6606Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UVJX-ray2.08A/C468-690[»]
4NI2X-ray1.90A468-662[»]
ProteinModelPortaliQ02108.
SMRiQ02108. Positions 281-387, 406-466, 471-662.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini481 – 608128Guanylate cyclasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4171. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000220903.
HOVERGENiHBG106603.
InParanoidiQ02108.
KOiK12318.
OMAiSEIPGIC.
OrthoDBiEOG7VX8Z6.
PhylomeDBiQ02108.
TreeFamiTF351403.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011644. Heme_NO-bd.
IPR011645. HNOB_dom_associated.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q02108-1) [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
MFCTKLKDLK ITGECPFSLL APGQVPNESS EEAAGSSESC KATVPICQDI
60 70 80 90 100
PEKNIQESLP QRKTSRSRVY LHTLAESICK LIFPEFERLN VALQRTLAKH
110 120 130 140 150
KIKESRKSLE REDFEKTIAE QAVAAGVPVE VIKESLGEEV FKICYEEDEN
160 170 180 190 200
ILGVVGGTLK DFLNSFSTLL KQSSHCQEAG KRGRLEDASI LCLDKEDDFL
210 220 230 240 250
HVYYFFPKRT TSLILPGIIK AAAHVLYETE VEVSLMPPCF HNDCSEFVNQ
260 270 280 290 300
PYLLYSVHMK STKPSLSPSK PQSSLVIPTS LFCKTFPFHF MFDKDMTILQ
310 320 330 340 350
FGNGIRRLMN RRDFQGKPNF EEYFEILTPK INQTFSGIMT MLNMQFVVRV
360 370 380 390 400
RRWDNSVKKS SRVMDLKGQM IYIVESSAIL FLGSPCVDRL EDFTGRGLYL
410 420 430 440 450
SDIPIHNALR DVVLIGEQAR AQDGLKKRLG KLKATLEQAH QALEEEKKKT
460 470 480 490 500
VDLLCSIFPC EVAQQLWQGQ VVQAKKFSNV TMLFSDIVGF TAICSQCSPL
510 520 530 540 550
QVITMLNALY TRFDQQCGEL DVYKVETIGD AYCVAGGLHK ESDTHAVQIA
560 570 580 590 600
LMALKMMELS DEVMSPHGEP IKMRIGLHSG SVFAGVVGVK MPRYCLFGNN
610 620 630 640 650
VTLANKFESC SVPRKINVSP TTYRLLKDCP GFVFTPRSRE ELPPNFPSEI
660 670 680 690
PGICHFLDAY QQGTNSKPCF QKKDVEDGNA NFLGKASGID
Length:690
Mass (Da):77,452
Last modified:May 30, 2000 - v2
Checksum:iDA1E14A5E11451CF
GO
Isoform 2 (identifier: Q02108-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     625-690: Missing.

Note: No experimental confirmation available.
Show »
Length:624
Mass (Da):70,184
Checksum:i73DD3A95B1CDC339
GO

Sequence cautioni

The sequence CAA47145.1 differs from that shown. Reason: Frameshift at positions 123, 127, 131, 162, 184, 529, 535, 678 and 680. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441V → M in AAH28384 (PubMed:15489334).Curated
Sequence conflicti124 – 1274AAGV → QQS in CAA47145 (PubMed:1352257).Curated
Sequence conflicti322 – 3221Missing in CAA47145 (PubMed:1352257).Curated
Sequence conflicti497 – 4971C → R in AK309950 (PubMed:14702039).Curated
Sequence conflicti554 – 5541L → V in AAH28384 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251V → I.
Corresponds to variant rs2170646 [ dbSNP | Ensembl ].
VAR_049257

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei625 – 69066Missing in isoform 2. 1 PublicationVSP_045477Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66534 mRNA. Translation: CAA47145.1. Frameshift.
U58855 mRNA. Translation: AAB94794.1.
Y15723 mRNA. Translation: CAA75738.1.
AK309950 mRNA. No translation available.
AC104083 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04892.1.
CH471056 Genomic DNA. Translation: EAX04895.1.
CH471056 Genomic DNA. Translation: EAX04896.1.
CH471056 Genomic DNA. Translation: EAX04897.1.
BC028384 mRNA. Translation: AAH28384.1.
CCDSiCCDS34085.1. [Q02108-1]
CCDS54812.1. [Q02108-2]
PIRiS23098.
RefSeqiNP_000847.2. NM_000856.5. [Q02108-1]
NP_001124154.1. NM_001130682.2. [Q02108-1]
NP_001124155.1. NM_001130683.3. [Q02108-1]
NP_001124156.1. NM_001130684.2. [Q02108-1]
NP_001124159.1. NM_001130687.2. [Q02108-2]
NP_001243378.1. NM_001256449.1. [Q02108-1]
XP_005263012.1. XM_005262955.1. [Q02108-1]
XP_006714259.1. XM_006714196.1. [Q02108-1]
XP_006714260.1. XM_006714197.1. [Q02108-1]
XP_011530201.1. XM_011531899.1. [Q02108-1]
UniGeneiHs.24258.
Hs.740815.

Genome annotation databases

EnsembliENST00000296518; ENSP00000296518; ENSG00000164116. [Q02108-1]
ENST00000455639; ENSP00000412201; ENSG00000164116. [Q02108-1]
ENST00000506455; ENSP00000424361; ENSG00000164116. [Q02108-1]
ENST00000511108; ENSP00000421493; ENSG00000164116. [Q02108-1]
ENST00000511507; ENSP00000426968; ENSG00000164116. [Q02108-2]
ENST00000513574; ENSP00000426040; ENSG00000164116. [Q02108-1]
GeneIDi2982.
KEGGihsa:2982.
UCSCiuc003iov.4. human. [Q02108-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66534 mRNA. Translation: CAA47145.1. Frameshift.
U58855 mRNA. Translation: AAB94794.1.
Y15723 mRNA. Translation: CAA75738.1.
AK309950 mRNA. No translation available.
AC104083 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04892.1.
CH471056 Genomic DNA. Translation: EAX04895.1.
CH471056 Genomic DNA. Translation: EAX04896.1.
CH471056 Genomic DNA. Translation: EAX04897.1.
BC028384 mRNA. Translation: AAH28384.1.
CCDSiCCDS34085.1. [Q02108-1]
CCDS54812.1. [Q02108-2]
PIRiS23098.
RefSeqiNP_000847.2. NM_000856.5. [Q02108-1]
NP_001124154.1. NM_001130682.2. [Q02108-1]
NP_001124155.1. NM_001130683.3. [Q02108-1]
NP_001124156.1. NM_001130684.2. [Q02108-1]
NP_001124159.1. NM_001130687.2. [Q02108-2]
NP_001243378.1. NM_001256449.1. [Q02108-1]
XP_005263012.1. XM_005262955.1. [Q02108-1]
XP_006714259.1. XM_006714196.1. [Q02108-1]
XP_006714260.1. XM_006714197.1. [Q02108-1]
XP_011530201.1. XM_011531899.1. [Q02108-1]
UniGeneiHs.24258.
Hs.740815.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UVJX-ray2.08A/C468-690[»]
4NI2X-ray1.90A468-662[»]
ProteinModelPortaliQ02108.
SMRiQ02108. Positions 281-387, 406-466, 471-662.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109237. 9 interactions.
IntActiQ02108. 3 interactions.
STRINGi9606.ENSP00000296518.

Chemistry

ChEMBLiCHEMBL3137281.

PTM databases

iPTMnetiQ02108.
PhosphoSiteiQ02108.

Polymorphism and mutation databases

BioMutaiGUCY1A3.
DMDMi7404351.

Proteomic databases

MaxQBiQ02108.
PaxDbiQ02108.
PeptideAtlasiQ02108.
PRIDEiQ02108.

Protocols and materials databases

DNASUi2982.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296518; ENSP00000296518; ENSG00000164116. [Q02108-1]
ENST00000455639; ENSP00000412201; ENSG00000164116. [Q02108-1]
ENST00000506455; ENSP00000424361; ENSG00000164116. [Q02108-1]
ENST00000511108; ENSP00000421493; ENSG00000164116. [Q02108-1]
ENST00000511507; ENSP00000426968; ENSG00000164116. [Q02108-2]
ENST00000513574; ENSP00000426040; ENSG00000164116. [Q02108-1]
GeneIDi2982.
KEGGihsa:2982.
UCSCiuc003iov.4. human. [Q02108-1]

Organism-specific databases

CTDi2982.
GeneCardsiGUCY1A3.
HGNCiHGNC:4685. GUCY1A3.
HPAiCAB010887.
MalaCardsiGUCY1A3.
MIMi139396. gene.
615750. phenotype.
neXtProtiNX_Q02108.
Orphaneti401945. Moyamoya disease with early-onset achalasia.
PharmGKBiPA29067.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4171. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000220903.
HOVERGENiHBG106603.
InParanoidiQ02108.
KOiK12318.
OMAiSEIPGIC.
OrthoDBiEOG7VX8Z6.
PhylomeDBiQ02108.
TreeFamiTF351403.

Enzyme and pathway databases

BRENDAi4.6.1.2. 2681.
ReactomeiR-HSA-392154. Nitric oxide stimulates guanylate cyclase.

Miscellaneous databases

ChiTaRSiGUCY1A3. human.
GeneWikiiGUCY1A3.
GenomeRNAii2982.
PROiQ02108.
SOURCEiSearch...

Gene expression databases

BgeeiQ02108.
CleanExiHS_GUCY1A3.
ExpressionAtlasiQ02108. baseline and differential.
GenevisibleiQ02108. HS.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR011644. Heme_NO-bd.
IPR011645. HNOB_dom_associated.
IPR024096. NO_sig/Golgi_transp_ligand-bd.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 1 hit.
PF07700. HNOB. 1 hit.
PF07701. HNOBA. 1 hit.
[Graphical view]
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF111126. SSF111126. 1 hit.
SSF55073. SSF55073. 1 hit.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the cDNAs coding for the two subunits of soluble guanylyl cyclase from human brain."
    Giuili G., Scholl U., Bulle F., Guellaeen G.
    FEBS Lett. 304:83-88(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Human soluble guanylate cyclase large subunit mRNA, alpha3-like."
    Gansemans Y., Brouckaert P., Fiers W.
    Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  3. "Human soluble guanylate cyclase: functional expression and revised isoenzyme family."
    Zabel U., Weeger M., La M., Schmidt H.H.
    Biochem. J. 335:51-57(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, INTERACTION WITH GUCY1B3, TISSUE SPECIFICITY.
    Tissue: Brain.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  8. "Crystal structures of the catalytic domain of human soluble guanylate cyclase."
    Allerston C.K., von Delft F., Gileadi O.
    PLoS ONE 8:E57644-E57644(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 468-690 IN COMPLEX WITH GUCY1B3, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, INTERACTION WITH GUCY1B3.
  9. Cited for: INVOLVEMENT IN MYMY6.
  10. "Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity."
    Seeger F., Quintyn R., Tanimoto A., Williams G.J., Tainer J.A., Wysocki V.H., Garcin E.D.
    Biochemistry 53:2153-2165(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 468-662 IN COMPLEX WITH GUCY1B3, INTERACTION WITH GUCY1B3, CATALYTIC ACTIVITY, COFACTOR.

Entry informationi

Entry nameiGCYA3_HUMAN
AccessioniPrimary (citable) accession number: Q02108
Secondary accession number(s): D3DP19
, D6RDW3, O43843, Q8TAH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 30, 2000
Last modified: July 6, 2016
This is version 155 of the entry and version 2 of the sequence. [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

Miscellaneous

There are two types of guanylate cyclases: soluble forms and membrane-associated receptor forms.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.