Q5SDA5

PR
Gene name
Gucy2f
Protein name
Retinal guanylyl cyclase 2
Names
Guanylate cyclase 2F
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:245650
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)

813-904 (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 Q5SDA5

Entry ID Method Resolution Chain Position Source
AF-Q5SDA5-F1 Predicted AlphaFoldDB

57 variants for Q5SDA5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs265931291 34 R>K No EVA
rs236787527 46 R>Q No EVA
rs3389581189 169 L>V No EVA
rs3389588126 210 R>P No EVA
rs3389573359 247 M>V No EVA
rs3411770430 258 T>S No EVA
rs3389590133 269 L>Q No EVA
rs3412005145 283 V>I No EVA
rs3389571412 297 V>L No EVA
rs3389581087 301 N>K No EVA
rs3389570928 330 A>G No EVA
rs3389585809 348 L>* No EVA
rs3389590054 349 F>S No EVA
rs3389581167 366 A>V No EVA
rs3389485927 370 N>T No EVA
rs3412332693 392 Q>* No EVA
rs3412106540 392 Q>R No EVA
rs3389581191 399 N>S No EVA
rs3389577201 418 L>R No EVA
rs3389588068 421 T>S No EVA
rs3389556105 422 Y>C No EVA
rs3389535027 434 R>K No EVA
rs260078958 455 A>S No EVA
rs1133327538 526 S>N No EVA
rs3411348538 566 Y>T No EVA
rs3389585765 568 G>V No EVA
rs3389577227 573 L>P No EVA
rs3389544302 594 V>A No EVA
rs3389527376 617 G>* No EVA
rs3389590040 618 M>V No EVA
rs3410851236 658 M>T No EVA
rs3412106032 667 I>V No EVA
rs3389573382 685 K>I No EVA
rs3389573355 686 V>A No EVA
rs3389577793 688 D>V No EVA
rs3389527380 689 Y>C No EVA
rs3412104766 707 E>* No EVA
rs3410851208 707 E>A No EVA
rs29289031 710 L>M No EVA
rs3389485955 763 R>K No EVA
rs3389570971 817 K>R No EVA
rs3389577226 843 T>S No EVA
rs3389585733 859 Q>* No EVA
rs3409461761 867 E>K No EVA
rs3389527406 901 E>D No EVA
rs3389573331 902 P>R No EVA
rs3389590115 917 D>E No EVA
rs3389585727 936 M>I No EVA
rs3412332170 1022 I>Q No EVA
rs3412234327 1022 I>T No EVA
rs3389590136 1030 T>I No EVA
rs29291436 1033 Q>R No EVA
rs3389556155 1054 T>I No EVA
rs3411094291 1060 L>I No EVA
rs3389588063 1060 L>P No EVA
rs3389575090 1073 P>A No EVA
rs29288642 1082 V>M No EVA

No associated diseases with Q5SDA5

3 regional properties for Q5SDA5

Type Name Position InterPro Accession
domain Protein kinase domain 4 - 255 IPR000719
active_site Serine/threonine-protein kinase, active site 120 - 132 IPR008271
binding_site Protein kinase, ATP binding site 10 - 33 IPR017441

Functions

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

4 GO annotations of cellular component

Name Definition
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
rod photoreceptor outer segment The outer segment of a vertebrate rod photoreceptor that contains sealed membrane discs that are not connected to the ciliary membrane and containing rhodopsin photoreceptor proteins.

7 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 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.
detection of light stimulus involved in visual perception The series of events involved in visual perception in which a light stimulus is received and converted into a molecular signal.
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.

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
Q02846 GUCY2D Retinal guanylyl cyclase 1 Homo sapiens (Human) PR
P20594 NPR2 Atrial natriuretic peptide receptor 2 Homo sapiens (Human) PR
P51841 GUCY2F Retinal guanylyl cyclase 2 Homo sapiens (Human) PR
P52785 Gucy2e Retinal guanylyl cyclase 1 Mus musculus (Mouse) PR
Q6VVW5 Npr2 Atrial natriuretic peptide receptor 2 Mus musculus (Mouse) PR
P51840 Gucy2e Retinal guanylyl cyclase 1 Rattus norvegicus (Rat) 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
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
MFLGPWPFSR LLSWFAISSR LSGQHGLPSS KFLRCLCLLA LLPLLRWGQA LPYKIGVIGP
70 80 90 100 110 120
WTCDPFFSKA LPEVAAALAI ERISRDKTFD RSYSFEYVIL NEDCQTSKAL ASFISHQQMA
130 140 150 160 170 180
SGFVGPANPG FCEAASLLGT SWDKGIFSWA CVNHELDNKH SFPTFSRTLP SPIRVLVTVM
190 200 210 220 230 240
KYFQWAHAGV ISSDEDIWMH TANRVSSALR SQGLPVGVVL TSGRDSQSIQ KALQQIRQAD
250 260 270 280 290 300
RIRIIIMCMH SALIGGETQT HFLELAHDLK MTDGTYVFVP YDVLLYSLPY KHSPYQVLRN
310 320 330 340 350 360
NPKLREAYDA VLTITVESHE KTFYEAYAEA AARGEIPEKP DSNQVSPLFG TIYNSIYFIA
370 380 390 400 410 420
QAMNNAMKKN GRASAASLVQ HSRNMQFYGF NQLIKTDSNG NGISEYVILD TNGKEWELRG
430 440 450 460 470 480
TYTVDMETEL LRFRGTPIHF PGGRPTSADA KCWFAERKIC QGGIDPALAM MVCFALLIAL
490 500 510 520 530 540
LSINGFAYFI RRRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQIISEVQS
550 560 570 580 590 600
GRSPRLSFSS GSLTPATYEN SNIAIYEGDW VWLKKFPPGD FGDIKSIKSS ASDVFEMMKD
610 620 630 640 650 660
LRHENVNPLL GFFYDSGMFA IVSEFCSRRS LEDILTNDDV KLDWMFKSSL LLDLIKGMKY
670 680 690 700 710 720
LHHREFIHGR LKSRNCVVDG RFVLKVTDYG FNDILEMLRL SEEEPSEEEL LWTAPELLRA
730 740 750 760 770 780
PGGIRLGSFA GDVYSFAIIM QEVMVRGAPF CMMDLPAKEI IDRLKMPPPV YRPVVSPEYA
790 800 810 820 830 840
PAECLQLMKQ CWAEASEQRP TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR
850 860 870 880 890 900
ERTEELEIEK QKTEKLLTQM LPLSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS
910 920 930 940 950 960
EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA AEIANMSLDI
970 980 990 1000 1010 1020
LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY
1030 1040 1050 1060 1070 1080
RIHVSLSTVT ILQTLSEGYE VELRGRTELK GKGTEETFWL VGKKGFTKPL PVPPPVGKDG
1090 1100
QVGHGLQPAE IAAFQRRKAE RQLVRNKP