P90895

PR
Gene name
F56F10.1
Protein name
Soluble guanylate cyclase gcy-33
Names
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_F57F5.2
EC number
4.6.1.2: Phosphorus-oxygen lyases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

698-945 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P90895

Entry ID Method Resolution Chain Position Source
AF-P90895-F1 Predicted AlphaFoldDB

No variants for P90895

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P90895

No associated diseases with P90895

4 regional properties for P90895

Type Name Position InterPro Accession
domain Adenylyl cyclase class-3/4/guanylyl cyclase 400 - 616 IPR001054
domain Heme NO-binding 2 - 164 IPR011644
domain Haem NO binding associated 205 - 420 IPR011645
conserved_site Adenylyl cyclase class-4/guanylyl cyclase, conserved site 544 - 567 IPR018297

Functions

Description
EC Number 4.6.1.2 Phosphorus-oxygen lyases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
guanylate cyclase complex, soluble Complex that possesses guanylate cyclase activity and is not bound to a membrane.

7 GO annotations of molecular function

Name Definition
carbon monoxide sensor activity Binding to and responding, e.g. by conformational change, to changes in the cellular level of carbon monoxide (CO).
GTP binding Binding to GTP, guanosine triphosphate.
guanylate cyclase activity Catalysis of the reaction: GTP = 3',5'-cyclic GMP + diphosphate.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.
nitric oxide binding Binding to nitric oxide (NO).
oxygen sensor activity Binding to and responding, e.g. by conformational change, to changes in the cellular level of oxygen (O2).

5 GO annotations of biological process

Name Definition
cGMP-mediated signaling Any intracellular signal transduction in which the signal is passed on within the cell via cyclic GMP (cGMP). Includes production of cGMP, and downstream effectors that further transmit the signal within the cell.
chemosensory behavior Behavior that is dependent upon the sensation of chemicals.
nitric oxide-cGMP-mediated signaling pathway Any intracellular signal transduction in which the signal is passed on within the cell by nitric oxide (NO) activating soluble guanylyl cyclase (sGC). Includes synthesis of nitric oxide, guanylyl cyclase activity, and downstream effectors that further transmit the signal within the cell following activation by cGMP.
response to oxygen levels Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of oxygen.
sensory perception of bitter taste The series of events required to receive a bitter taste stimulus, convert it to a molecular signal, and recognize and characterize the signal. This is a neurological process.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P33402 GUCY1A2 Guanylate cyclase soluble subunit alpha-2 Homo sapiens (Human) PR
10 20 30 40 50 60
MYGLVIEGVR FMIQENWGPQ VLLQVQKLTS LSEKSVSTHD QYSEHVVPQM FKAIHEITGT
70 80 90 100 110 120
PYEQIGVLAG RFFVQFLIRN GYGDLMNVMG RRFSDFIKGL DNIHEYFRFS YPKLRAPSFY
130 140 150 160 170 180
CKSESEDGLI LHYRSRRTGY LSYVIGQLVE LARVFYQLDI GIQVLKKKEK GRFTFVVLKI
190 200 210 220 230 240
SFDNVGLGQD LKLKERVKNL NEYLPVDTKS FLQMFPFHIA FNKKLEILMA GQGLLNLMPN
250 260 270 280 290 300
IQGLLMTDVF DLQRPCIKFT AEGIMVHQNC VFQIESLHPV VKQTEENITV QINDITEDKV
310 320 330 340 350 360
SLEKKTVMDN EYESLPYVTL RGPITVLKSS ETFLLLATCV VDTLDTMFKM GLYLNDFGES
370 380 390 400 410 420
DCNREIIMAT IQKSDTLKTM LENEKRRSEV LTEMTREISE AKKTARTLLT QMMPYEVAQT
430 440 450 460 470 480
MMRSGSVDHC EAFECVSIGF IRVCDFSKIS LFIEAFEVVN LLNTIYSHLD SIVDTHGVYK
490 500 510 520 530 540
VETIGESYMI SAGCPYRDDY DAEMVSDCCL EMVSHIKSFE YQSHDAVKKV LIKCGIFTGP
550 560 570 580 590 600
VVGGVVGVRT PRYCLFGDTV NTASRMESSN QTPMTIQIGQ RTKDRVEKQA SGAFRIKPKG
610 620 630 640 650 660
NVFVKGKGDM RVYEIEKKKG RARYKKSDPL RKKMVAEKKE AEELLDEDNE GHRSSALSRM
670 680 690 700 710 720
SLGESIDSSS SRRGSLSGSQ LELNKTIAQT IELTSKASAA LDLNMQDENN RPPTWSASHS
730 740 750 760 770 780
QDIRKPRKTE SKITLNSRLS SSDLAVSRVE TSKDSDGETP RPTSSELKEV NRIREEALAQ
790 800 810 820 830 840
EKEEERTTKE ENQKIEEVGE DHVSEATSLL DSEVSHGDNN ISFSQMPSDS IPHEDRTSLP
850 860 870 880 890 900
SATPSEIGDA ISKKKLEKED SNSSMSSLDE RTTVSAKPTT TRRLLNQKDL EKEKKRSSMA
910 920 930 940
GSSVTSSSAH SHSIRSKKDT RDKSRCKCED IRADNKLKTK VCSIM