RD3_HUMAN
ID RD3_HUMAN Reviewed; 195 AA.
AC Q7Z3Z2; A8K595;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein RD3;
DE AltName: Full=Retinal degeneration protein 3;
GN Name=RD3; Synonyms=C1orf36;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT CYS-47.
RX PubMed=12914764; DOI=10.1016/s0006-291x(03)01410-4;
RA Lavorgna G., Lestingi M., Ziviello C., Testa F., Simonelli F.,
RA Manitto M.P., Brancato R., Ferrari M., Rinaldi E., Ciccodicola A.,
RA Banfi S.;
RT "Identification and characterization of C1orf36, a transcript highly
RT expressed in photoreceptor cells, and mutation analysis in retinitis
RT pigmentosa.";
RL Biochem. Biophys. Res. Commun. 308:414-421(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INVOLVEMENT IN LCA12, AND VARIANTS ARG-6; ASP-23; ARG-35; CYS-47; VAL-57;
RP TRP-68; MET-130; LYS-167 AND VAL-195.
RX PubMed=17186464; DOI=10.1086/510021;
RA Friedman J.S., Chang B., Kannabiran C., Chakarova C., Singh H.P.,
RA Jalali S., Hawes N.L., Branham K., Othman M., Filippova E., Thompson D.A.,
RA Webster A.R., Andreasson S., Jacobson S.G., Bhattacharya S.S.,
RA Heckenlively J.R., Swaroop A.;
RT "Premature truncation of a novel protein, RD3, exhibiting subnuclear
RT localization is associated with retinal degeneration.";
RL Am. J. Hum. Genet. 79:1059-1070(2006).
RN [6]
RP INTERACTION WITH GUCY2D, AND FUNCTION.
RX PubMed=21078983; DOI=10.1073/pnas.1010460107;
RA Azadi S., Molday L.L., Molday R.S.;
RT "RD3, the protein associated with Leber congenital amaurosis type 12, is
RT required for guanylate cyclase trafficking in photoreceptor cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21158-21163(2010).
RN [7]
RP FUNCTION, AND CHARACTERIZATION OF VARIANTS ARG-6; ARG-35; VAL-57; TRP-68
RP AND MET-130.
RX PubMed=21928830; DOI=10.1021/bi201342b;
RA Peshenko I.V., Olshevskaya E.V., Azadi S., Molday L.L., Molday R.S.,
RA Dizhoor A.M.;
RT "Retinal degeneration 3 (RD3) protein inhibits catalytic activity of
RT retinal membrane guanylyl cyclase (RetGC) and its stimulation by activating
RT proteins.";
RL Biochemistry 50:9511-9519(2011).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GUCY2D.
RX PubMed=26100624; DOI=10.1074/jbc.m115.661371;
RA Peshenko I.V., Olshevskaya E.V., Dizhoor A.M.;
RT "Dimerization Domain of Retinal Membrane Guanylyl Cyclase 1 (RetGC1) Is an
RT Essential Part of Guanylyl Cyclase-activating Protein (GCAP) Binding
RT Interface.";
RL J. Biol. Chem. 290:19584-19596(2015).
RN [9]
RP FUNCTION, MUTAGENESIS OF 87-LYS--PRO-90; 93-CYS--ILE-97; CYS-93;
RP 99-ARG--GLN-102 AND 119-ARG--LEU-122, AND INTERACTION WITH GUCY2D.
RX PubMed=27471269; DOI=10.1074/jbc.m116.742288;
RA Peshenko I.V., Olshevskaya E.V., Dizhoor A.M.;
RT "Functional Study and Mapping Sites for Interaction with the Target Enzyme
RT in Retinal Degeneration 3 (RD3) Protein.";
RL J. Biol. Chem. 291:19713-19723(2016).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=29030614; DOI=10.1038/s41598-017-13337-9;
RA Aravindan S., Somasundaram D.B., Kam K.L., Subramanian K., Yu Z.,
RA Herman T.S., Fung K.M., Aravindan N.;
RT "Retinal Degeneration Protein 3 (RD3) in normal human tissues: Novel
RT insights.";
RL Sci. Rep. 7:13154-13154(2017).
RN [11]
RP FUNCTION, AND INTERACTION WITH GUK1.
RX PubMed=29515371; DOI=10.3389/fnmol.2018.00052;
RA Wimberg H., Janssen-Bienhold U., Koch K.W.;
RT "Control of the Nucleotide Cycle in Photoreceptor Cell Extracts by Retinal
RT Degeneration Protein 3.";
RL Front. Mol. Neurosci. 11:52-52(2018).
RN [12]
RP STRUCTURE BY NMR OF 19-153, MUTAGENESIS OF LEU-29; GLU-32; CYS-85; CYS-93
RP AND GLU-108, FUNCTION, AND INTERACTION WITH GUCY2D.
RX PubMed=30559291; DOI=10.1074/jbc.ra118.006106;
RA Peshenko I.V., Yu Q., Lim S., Cudia D., Dizhoor A.M., Ames J.B.;
RT "Retinal degeneration 3 (RD3) protein, a retinal guanylyl cyclase
RT regulator, forms a monomeric and elongated four-helix bundle.";
RL J. Biol. Chem. 294:2318-2328(2019).
CC -!- FUNCTION: Plays a critical role in the regulation of enzymes involved
CC in nucleotide cycle in photoreceptors (PubMed:29515371,
CC PubMed:21928830, PubMed:21078983, PubMed:27471269, PubMed:30559291).
CC Inhibits the basal catalytic activity and the GCAP-stimulated activity
CC of GUCY2D and GUCY2F, two retinal guanylyl cyclases involved in the
CC production of cGMP in photoreceptors (PubMed:21928830, PubMed:27471269,
CC PubMed:29515371, PubMed:30559291). Involved in the transport of GUCY2D
CC and GUCY2F to their target sites in the photoreceptor outer segment
CC (PubMed:21078983). Up-regulates the activity of GUK1, a kinase that
CC also plays an essential role for recycling GMP and indirectly, cGMP
CC (PubMed:29515371). Plays an important role for the survival of rods and
CC cones in the retina (By similarity). {ECO:0000250|UniProtKB:Q8BRE0,
CC ECO:0000269|PubMed:21078983, ECO:0000269|PubMed:21928830,
CC ECO:0000269|PubMed:27471269, ECO:0000269|PubMed:29515371,
CC ECO:0000269|PubMed:30559291}.
CC -!- SUBUNIT: Monomer (PubMed:30559291). Interacts with GUCY2D; negatively
CC regulates its activity (PubMed:21928830, PubMed:26100624,
CC PubMed:27471269, PubMed:30559291). The interaction with GUCY2D promotes
CC the exit of GUCY2D from the endoplasmic reticulum and its trafficking
CC to the photoreceptor outer segments (PubMed:21078983). Interacts with
CC GUCY2F (By similarity). The interaction with GUCY2F negatively
CC regulates GUCY2F activity (PubMed:29515371). The interaction with
CC GUCY2F promotes the exit of GUCY2F from the endoplasmic reticulum and
CC its trafficking to the photoreceptor outer segments (PubMed:21078983).
CC Interacts with GUK1; up-regulates GUK1 activity (PubMed:29515371).
CC {ECO:0000250|UniProtKB:Q8BRE0, ECO:0000269|PubMed:21078983,
CC ECO:0000269|PubMed:21928830, ECO:0000269|PubMed:26100624,
CC ECO:0000269|PubMed:27471269, ECO:0000269|PubMed:29515371,
CC ECO:0000269|PubMed:30559291}.
CC -!- INTERACTION:
CC Q7Z3Z2; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-10257497, EBI-12011224;
CC Q7Z3Z2; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-10257497, EBI-10174566;
CC Q7Z3Z2; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-10257497, EBI-744366;
CC Q7Z3Z2; Q14232: EIF2B1; NbExp=10; IntAct=EBI-10257497, EBI-491065;
CC Q7Z3Z2; Q02846: GUCY2D; NbExp=3; IntAct=EBI-10257497, EBI-1756902;
CC Q7Z3Z2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-10257497, EBI-741158;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000250|UniProtKB:Q8BRE0}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q8BRE0}. Endosome
CC {ECO:0000250|UniProtKB:Q8BRE0}. Nucleus {ECO:0000269|PubMed:26100624,
CC ECO:0000269|PubMed:29030614}. Cytoplasm {ECO:0000269|PubMed:26100624,
CC ECO:0000269|PubMed:29030614}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:29030614}. Note=Colocalizes with GUCY2E and GUCY2F
CC in rods and cones photoreceptors. Colocalizes with GUK1 in
CC photoreceptor inner segments and to a lesser extent in the outer
CC plexiform layer (By similarity). Strong dot-like perinuclear staining
CC in the epithelial cells (PubMed:29030614).
CC {ECO:0000250|UniProtKB:Q8BRE0, ECO:0000269|PubMed:29030614}.
CC -!- TISSUE SPECIFICITY: Expressed in retina (PubMed:12914764). Widely
CC expressed (at protein level) (PubMed:29030614). In the retina the
CC strongest immunoreactivity is detected in the inner half of the
CC cytoplasmic portion of the photoreceptor layer, where rods and cones
CC are found, and the external half of the outer plexiform layer (at
CC protein level) (PubMed:29030614). {ECO:0000269|PubMed:12914764,
CC ECO:0000269|PubMed:29030614}.
CC -!- DISEASE: Leber congenital amaurosis 12 (LCA12) [MIM:610612]: A severe
CC dystrophy of the retina, typically becoming evident in the first years
CC of life. Visual function is usually poor and often accompanied by
CC nystagmus, sluggish or near-absent pupillary responses, photophobia,
CC high hyperopia and keratoconus. {ECO:0000269|PubMed:17186464}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; AY191519; AAP12678.1; -; mRNA.
DR EMBL; AK291210; BAF83899.1; -; mRNA.
DR EMBL; CH471100; EAW93414.1; -; Genomic_DNA.
DR EMBL; BC065541; AAH65541.1; -; mRNA.
DR CCDS; CCDS1498.1; -.
DR RefSeq; NP_001158160.1; NM_001164688.1.
DR RefSeq; NP_898882.1; NM_183059.2.
DR PDB; 6DRF; NMR; -; A=19-153.
DR PDBsum; 6DRF; -.
DR AlphaFoldDB; Q7Z3Z2; -.
DR SMR; Q7Z3Z2; -.
DR BioGRID; 131222; 29.
DR IntAct; Q7Z3Z2; 10.
DR STRING; 9606.ENSP00000355969; -.
DR iPTMnet; Q7Z3Z2; -.
DR PhosphoSitePlus; Q7Z3Z2; -.
DR BioMuta; RD3; -.
DR DMDM; 71152353; -.
DR MassIVE; Q7Z3Z2; -.
DR PaxDb; Q7Z3Z2; -.
DR PeptideAtlas; Q7Z3Z2; -.
DR PRIDE; Q7Z3Z2; -.
DR ProteomicsDB; 69099; -.
DR Antibodypedia; 47112; 69 antibodies from 17 providers.
DR DNASU; 343035; -.
DR Ensembl; ENST00000367002.5; ENSP00000355969.4; ENSG00000198570.7.
DR Ensembl; ENST00000680073.1; ENSP00000505312.1; ENSG00000198570.7.
DR GeneID; 343035; -.
DR KEGG; hsa:343035; -.
DR MANE-Select; ENST00000680073.1; ENSP00000505312.1; NM_001164688.2; NP_001158160.1.
DR UCSC; uc001him.2; human.
DR CTD; 343035; -.
DR DisGeNET; 343035; -.
DR GeneCards; RD3; -.
DR HGNC; HGNC:19689; RD3.
DR HPA; ENSG00000198570; Tissue enriched (retina).
DR MalaCards; RD3; -.
DR MIM; 180040; gene.
DR MIM; 610612; phenotype.
DR neXtProt; NX_Q7Z3Z2; -.
DR OpenTargets; ENSG00000198570; -.
DR Orphanet; 65; Leber congenital amaurosis.
DR PharmGKB; PA162400998; -.
DR VEuPathDB; HostDB:ENSG00000198570; -.
DR eggNOG; ENOG502QTP1; Eukaryota.
DR GeneTree; ENSGT00390000002089; -.
DR HOGENOM; CLU_107621_0_0_1; -.
DR InParanoid; Q7Z3Z2; -.
DR OMA; FRSRIKI; -.
DR OrthoDB; 1505645at2759; -.
DR PhylomeDB; Q7Z3Z2; -.
DR TreeFam; TF331573; -.
DR PathwayCommons; Q7Z3Z2; -.
DR SignaLink; Q7Z3Z2; -.
DR BioGRID-ORCS; 343035; 10 hits in 1058 CRISPR screens.
DR ChiTaRS; RD3; human.
DR GenomeRNAi; 343035; -.
DR Pharos; Q7Z3Z2; Tbio.
DR PRO; PR:Q7Z3Z2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z3Z2; protein.
DR Bgee; ENSG00000198570; Expressed in buccal mucosa cell and 68 other tissues.
DR Genevisible; Q7Z3Z2; HS.
DR GO; GO:0120199; C:cone photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0120200; C:rod photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0031283; P:negative regulation of guanylate cyclase activity; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0060041; P:retina development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR InterPro; IPR028092; RD3.
DR PANTHER; PTHR28489; PTHR28489; 1.
DR Pfam; PF14473; RD3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm; Endosome;
KW Leber congenital amaurosis; Nucleus; Reference proteome;
KW Sensory transduction; Vision.
FT CHAIN 1..195
FT /note="Protein RD3"
FT /id="PRO_0000089248"
FT REGION 170..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..52
FT /evidence="ECO:0000255"
FT VARIANT 6
FT /note="W -> R (in an individual with an atypical late-onset
FT form of retinitis pigmentosa; does not affect ability to
FT suppress GUCY2D activity induced by GCAPA;
FT dbSNP:rs35649846)"
FT /evidence="ECO:0000269|PubMed:17186464,
FT ECO:0000269|PubMed:21928830"
FT /id="VAR_031510"
FT VARIANT 23
FT /note="E -> D (in an individual with an atypical late-onset
FT form of retinitis pigmentosa; dbSNP:rs34422496)"
FT /evidence="ECO:0000269|PubMed:17186464"
FT /id="VAR_031511"
FT VARIANT 35
FT /note="G -> R (does not affect ability to suppress GUCY2D
FT activity induced by GCAPA; dbSNP:rs530024772)"
FT /evidence="ECO:0000269|PubMed:17186464,
FT ECO:0000269|PubMed:21928830"
FT /id="VAR_031512"
FT VARIANT 47
FT /note="R -> C (in dbSNP:rs34049451)"
FT /evidence="ECO:0000269|PubMed:12914764,
FT ECO:0000269|PubMed:17186464"
FT /id="VAR_023050"
FT VARIANT 57
FT /note="G -> V (in an individual with cone-rod degeneration;
FT abolishes protein expression; less effective in suppressing
FT GUCY2D activity by GCAPA; dbSNP:rs767481165)"
FT /evidence="ECO:0000269|PubMed:17186464,
FT ECO:0000269|PubMed:21928830"
FT /id="VAR_031513"
FT VARIANT 68
FT /note="R -> W (less effective in suppressing GUCY2D
FT activity induced by GCAPA; dbSNP:rs144697496)"
FT /evidence="ECO:0000269|PubMed:17186464,
FT ECO:0000269|PubMed:21928830"
FT /id="VAR_031514"
FT VARIANT 130
FT /note="K -> M (in an individual with cone-rod dystrophy
FT features; less effective in suppressing GUCY2D activity by
FT GCAPA; dbSNP:rs766015590)"
FT /evidence="ECO:0000269|PubMed:17186464,
FT ECO:0000269|PubMed:21928830"
FT /id="VAR_031515"
FT VARIANT 167
FT /note="R -> K (in dbSNP:rs74782684)"
FT /evidence="ECO:0000269|PubMed:17186464"
FT /id="VAR_031516"
FT VARIANT 195
FT /note="D -> V (in dbSNP:rs143207434)"
FT /evidence="ECO:0000269|PubMed:17186464"
FT /id="VAR_031517"
FT MUTAGEN 29
FT /note="L->F: Reduced the affinity of RD3 for GUCY2D."
FT /evidence="ECO:0000269|PubMed:30559291"
FT MUTAGEN 32
FT /note="E->K: Reduced the affinity of RD3 for GUCY2D."
FT /evidence="ECO:0000269|PubMed:30559291"
FT MUTAGEN 85
FT /note="C->L: Reduced the affinity of RD3 for GUCY2D."
FT /evidence="ECO:0000269|PubMed:30559291"
FT MUTAGEN 87..90
FT /note="KIHP->PHRL: Strongly affects RD3 ability to suppress
FT GUCY2D activity."
FT /evidence="ECO:0000269|PubMed:27471269"
FT MUTAGEN 93..97
FT /note="CGPAI->PALSL: Strongly affects RD3 ability to
FT suppress GUCY2D activity."
FT /evidence="ECO:0000269|PubMed:27471269"
FT MUTAGEN 93
FT /note="C->P: Reduced RD3 affinity for GUCY2D by 80-fold."
FT /evidence="ECO:0000269|PubMed:27471269"
FT MUTAGEN 93
FT /note="C->V: Increased the affinity of RD3 for GUCY2D."
FT /evidence="ECO:0000269|PubMed:30559291"
FT MUTAGEN 99..102
FT /note="RFRQ->FRQR: Strongly affects RD3 ability to suppress
FT GUCY2D activity."
FT /evidence="ECO:0000269|PubMed:27471269"
FT MUTAGEN 108
FT /note="E->K: Does not affect affinity of RD3 for GUCY2D."
FT /evidence="ECO:0000269|PubMed:30559291"
FT MUTAGEN 119..122
FT /note="RSVL->LAER: Strongly affects RD3 ability to suppress
FT GUCY2D activity."
FT /evidence="ECO:0000269|PubMed:27471269"
FT HELIX 21..51
FT /evidence="ECO:0007829|PDB:6DRF"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6DRF"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:6DRF"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6DRF"
FT HELIX 93..107
FT /evidence="ECO:0007829|PDB:6DRF"
FT HELIX 111..139
FT /evidence="ECO:0007829|PDB:6DRF"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:6DRF"
SQ SEQUENCE 195 AA; 22704 MW; F9AB60B761E55779 CRC64;
MSLISWLRWN EAPSRLSTRS PAEMVLETLM MELTGQMREA ERQQRERSNA VRKVCTGVDY
SWLASTPRST YDLSPIERLQ LEDVCVKIHP SYCGPAILRF RQLLAEQEPE VQEVSQLFRS
VLQEVLERMK QEEEAHKLTR QWSLRPRGSL ATFKTRARIS PFASDIRTIS EDVERDTPPP
LRSWSMPEFR APKAD
