Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P52785

Entry ID Method Resolution Chain Position Source
AF-P52785-F1 Predicted AlphaFoldDB

54 variants for P52785

Variant ID(s) Position Change Description Diseaes Association Provenance
rs26889949 15 G>R No EVA
rs234405523 19 P>S No EVA
rs215178643 21 R>Q No EVA
rs3389170301 37 G>E No EVA
rs3389176374 64 P>S No EVA
rs3389140432 72 A>G No EVA
rs3389173865 72 A>T No EVA
rs3389163151 129 G>D No EVA
rs3389176338 160 A>E No EVA
rs3389173844 173 D>G No EVA
rs3389170085 210 A>G No EVA
rs266246811 217 L>P No EVA
rs3389157376 246 I>N No EVA
rs3389106947 286 Y>N No EVA
rs3401150866 306 R>W No EVA
rs3389168761 347 S>T No EVA
rs3389170021 356 A>D No EVA
rs3389183066 370 A>V No EVA
rs3389106883 380 S>Y No EVA
rs26889967 383 R>H No EVA
rs3389133689 444 P>S No EVA
rs3389140440 453 W>* No EVA
rs3402141438 517 H>L No EVA
rs3402366964 522 S>K No EVA
rs3389133656 547 S>N No EVA
rs3389157355 549 P>A No EVA
rs3389106903 553 T>I No EVA
rs3389145894 558 Y>H No EVA
rs3389166914 564 W>G No EVA
rs3389168735 573 H>N No EVA
rs216124237 613 P>R No EVA
rs238685734 613 P>S No EVA
rs3389173815 618 L>S No EVA
rs3389163115 671 K>R No EVA
rs3389170332 688 H>R No EVA
rs3389180784 711 W>* No EVA
rs3389169850 755 T>S No EVA
rs1134583066 777 D>N No EVA
rs3401772450 828 E>Q No EVA
rs3389173802 842 T>A No EVA
rs3389168742 857 T>A No EVA
rs3389170002 891 G>D No EVA
rs3389180707 899 S>R No EVA
rs3389180706 974 V>L No EVA
rs3389157341 1002 F>Y No EVA
rs3389157323 1004 D>N No EVA
rs3389180718 1031 L>H No EVA
rs50451363 1033 A>S No EVA
rs3389170086 1034 L>M No EVA
rs3389140370 1051 K>N No EVA
rs3389168823 1058 W>L No EVA
rs224067952 1066 N>S No EVA
rs3389169811 1083 G>S No EVA
rs3389157335 1106 T>I No EVA

1 associated diseases with P52785

Without disease ID

1 regional properties for P52785

Type Name Position InterPro Accession
domain Protein kinase domain 69 - 379 IPR000719

Functions

Description
EC Number 4.6.1.2 Phosphorus-oxygen lyases
Subcellular Localization
  • Photoreceptor outer segment membrane ; Single-pass type I membrane protein
  • Endoplasmic reticulum membrane ; Single-pass type I membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
photoreceptor outer segment The outer segment of a vertebrate photoreceptor that contains a stack of membrane discs embedded with photoreceptor proteins.
photoreceptor outer segment membrane The membrane surrounding the outer segment of a vertebrate photoreceptor.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

8 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GTP binding Binding to GTP, guanosine triphosphate.
guanylate cyclase activity Catalysis of the reaction: GTP = 3',5'-cyclic GMP + diphosphate.
identical protein binding Binding to an identical protein or proteins.
peptide receptor activity Combining with an extracellular or intracellular peptide to initiate a change in cell activity.
protein homodimerization activity Binding to an identical protein to form a homodimer.
protein kinase activity Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
protein-containing complex binding Binding to a macromolecular complex.

6 GO annotations of biological process

Name Definition
cGMP biosynthetic process The chemical reactions and pathways resulting in the formation of cyclic GMP, guanosine 3',5'-phosphate.
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.
protein phosphorylation The process of introducing a phosphate group on to a protein.
receptor guanylyl cyclase signaling pathway The series of molecular signals initiated by an extracellular ligand binding to a receptor on the surface of the target cell where the receptor possesses guanylyl cyclase activity, and ending with the regulation of a downstream cellular process, e.g. transcription.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.
visual perception The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.

17 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P46197 NPR2 Atrial natriuretic peptide receptor 2 Bos taurus (Bovine) PR
O02740 GUCY2F Retinal guanylyl cyclase 2 Bos taurus (Bovine) PR
P51841 GUCY2F Retinal guanylyl cyclase 2 Homo sapiens (Human) PR
P20594 NPR2 Atrial natriuretic peptide receptor 2 Homo sapiens (Human) PR
Q02846 GUCY2D Retinal guanylyl cyclase 1 Homo sapiens (Human) PR
Q5SDA5 Gucy2f Retinal guanylyl cyclase 2 Mus musculus (Mouse) PR
Q6VVW5 Npr2 Atrial natriuretic peptide receptor 2 Mus musculus (Mouse) PR
P18910 Npr1 Atrial natriuretic peptide receptor 1 Rattus norvegicus (Rat) PR
P16067 Npr2 Atrial natriuretic peptide receptor 2 Rattus norvegicus (Rat) PR
P51842 Gucy2f Retinal guanylyl cyclase 2 Rattus norvegicus (Rat) PR
P51840 Gucy2e Retinal guanylyl cyclase 1 Rattus norvegicus (Rat) PR
Q09435 gcy-1 Receptor-type guanylate cyclase gcy-1 Caenorhabditis elegans PR
O16544 gcy-19 Receptor-type guanylate cyclase gcy-19 Caenorhabditis elegans PR
Q18331 gcy-11 Receptor-type guanylate cyclase gcy-11 Caenorhabditis elegans PR
Q10029 gcy-2 Receptor-type guanylate cyclase gcy-2 Caenorhabditis elegans PR
X5M8U1 gcy-17 Receptor-type guanylate cyclase gcy-17 Caenorhabditis elegans PR
Q23682 gcy-5 Receptor-type guanylate cyclase gcy-5 Caenorhabditis elegans PR
10 20 30 40 50 60
MSAWLLPAGG LPGAGFCVPA RQSPSSFSRV LRWPRPGLPG LLLLLLLPSP SALSAVFKVG
70 80 90 100 110 120
VLGPWACDPI FARARPDLAA RLAANRLNRD FALDGGPRFE VALLPEPCLT PGSLGAVSSA
130 140 150 160 170 180
LSRVSGLVGP VNPAACRPAE LLAQEAGVAL VPWGCPGTRA AGTTAPAVTP AADALYVLLR
190 200 210 220 230 240
AFRWARVALI TAPQDLWVEA GRALSTALRA RGLPVALVTS METSDRSGAR EALGRIRDGP
250 260 270 280 290 300
RVRVVIMVMH SVLLGGEEQR YLLEAAEELA LTDGSLVFLP FDTLHYALSP GPEALAAFVN
310 320 330 340 350 360
SSQLRRAHDA VLTLTRRCPP GGSVQDSLRR AQEHQELPLD LNLKQVSPLF GTIYDAVFLL
370 380 390 400 410 420
AGGVKRARTA VGGGWVSGAS VARQVREAQV SGFCGVLGRT EEPSFVLLDT DASGEQLFAT
430 440 450 460 470 480
HLLDPVLGSL RSAGTPMHFP RGGPAPGPDP SCWFDPDVIC NGGVEPGLVF VGFLLVIGMG
490 500 510 520 530 540
LTGAFLAHYL RHRLLHMQMA SGPNKIILTL EDVTFLHPPG GSSRKVVQGS RSSLATRSAS
550 560 570 580 590 600
DIRSVPSQPQ ESTNVGLYEG DWVWLKKFPG EHHMAIRPAT KTAFSKLREL RHENVALYLG
610 620 630 640 650 660
LFLAGTADSP ATPGEGILAV VSEHCARGSL HDLLAQREIK LDWMFKSSLL LDLIKGMRYL
670 680 690 700 710 720
HHRGVAHGRL KSRNCVVDGR FVLKVTDHGH GRLLEAQRVL PEPPSAEDQL WTAPELLRDP
730 740 750 760 770 780
SLERRGTLAG DVFSLAIIMQ EVVCRSTPYA MLELTPEEVI QRVRSPPPLC RPLVSMDQAP
790 800 810 820 830 840
MECIQLMTQC WAEHPELRPS MDLTFDLFKS INKGRKTNII DSMLRMLEQY SSNLEDLIRE
850 860 870 880 890 900
RTEELEQEKQ KTDRLLTQML PPSVAEALKM GTSVEPEYFE EVTLYFSDIV GFTTISAMSE
910 920 930 940 950 960
PIEVVDLLND LYTLFDAIIG AHDVYKVETI GDAYMVASGL PQRNGQRHAA EIANMSLDIL
970 980 990 1000 1010 1020
SAVGSFRMRH MPEVPVRIRI GLHSGPCVAG VVGLTMPRYC LFGDTVNTAS RMESTGLPYR
1030 1040 1050 1060 1070 1080
IHVNMSTVRI LRALDQGFQM ECRGRTELKG KGIEDTYWLV GRLGFNKPIP KPPDLQPGAS
1090 1100
NHGISLQEIP PERRKKLEKA RPGQFTGK