GUC2G_RAT
ID GUC2G_RAT Reviewed; 1100 AA.
AC P55205; O54884;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Guanylate cyclase 2G;
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q6TL19};
DE AltName: Full=Guanylyl cyclase receptor G;
DE Short=GC-G;
DE AltName: Full=Kinase-like domain-containing soluble guanylyl cyclase;
DE Short=ksGC;
DE Flags: Precursor;
GN Name=Gucy2g; Synonyms=Ksgc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8554626; DOI=10.1006/bbrc.1995.2868;
RA Kojima M., Hisaki K., Matsuo H., Kangawa K.;
RT "A new type soluble guanylyl cyclase, which contains a kinase-like domain:
RT its structure and expression.";
RL Biochem. Biophys. Res. Commun. 217:993-1000(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9422765; DOI=10.1074/jbc.273.2.1032;
RA Schulz S., Wedel B.J., Matthews A., Garbers D.L.;
RT "The cloning and expression of a new guanylyl cyclase orphan receptor.";
RL J. Biol. Chem. 273:1032-1037(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q6TL19};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC Evidence={ECO:0000250|UniProtKB:Q6TL19};
CC -!- SUBUNIT: Homooligomer (By similarity). May interact with NPR1/GC-A (By
CC similarity). {ECO:0000250|UniProtKB:Q6TL19}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000250|UniProtKB:Q6TL19}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55205-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55205-2; Sequence=VSP_015787;
CC -!- TISSUE SPECIFICITY: Expressed in lung, kidney and skeletal muscle. Low
CC levels in intestine. {ECO:0000269|PubMed:8554626}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6TL19}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AF024622; AAC01752.1; -; mRNA.
DR EMBL; U33847; AAC52417.1; -; mRNA.
DR PIR; T42260; T42260.
DR AlphaFoldDB; P55205; -.
DR SMR; P55205; -.
DR STRING; 10116.ENSRNOP00000021744; -.
DR GlyGen; P55205; 5 sites.
DR PhosphoSitePlus; P55205; -.
DR PaxDb; P55205; -.
DR PRIDE; P55205; -.
DR UCSC; RGD:621853; rat. [P55205-1]
DR RGD; 621853; Gucy2g.
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; P55205; -.
DR PhylomeDB; P55205; -.
DR PRO; PR:P55205; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR001170; ANPR/GUC.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00255; NATPEPTIDER.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; cGMP biosynthesis; Cytoplasm;
KW Glycoprotein; GTP-binding; Lyase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..1100
FT /note="Guanylate cyclase 2G"
FT /id="PRO_0000042179"
FT TOPO_DOM 44..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..1100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 549..826
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 901..1031
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..666
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9422765"
FT /id="VSP_015787"
FT CONFLICT 738..744
FT /note="WSGTPQG -> GPAPRR (in Ref. 1; AAC52417)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="P -> S (in Ref. 1; AAC52417)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="V -> F (in Ref. 1; AAC52417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1100 AA; 122497 MW; E487701031EF9965 CRC64;
MASRARSEPP LEHRFYGGAE SHAGHSSLVL TLFVVMLMTC LEAAKLTVGF HAPWNISHPF
SVQRLGAGLQ IAVDKLNSEP VGPGNLSWEF TYTNATCNAK ESLAAFIDQV QREHISVLIG
PACPEAAEVI GLLASEWDIP LFDFVGQMTA LEDHFWCDTC VTLVPPKQEI GTVLRESLQY
LGWEYIGVFG GSSAGSSWGE VNELWKAVED ELQLHFTITA RVRYSSGHSD LLQEGLRSMS
SVARVIILIC SSEDAKHILQ AAEDLGLNSG EFVFLLLQQL EDSFWKEVLA EDKVTRFPKV
YESVFLIAPS TYGGSAGDDD FRKQVYQRLR RPPFQSSISS EDQVSPYSAY LHDALLLYAQ
TVEEMMKAEK DFRDGRQLIS TLRADQVTLQ GITGPVLLDA QGKRHMDYSV YALQKSGNGS
RFLPFLHYDS FQKVIRPWRD DLNASGPHGS HPEYKPDCGF HEDLCRTKPP TGAGMTASVT
AVIPTVTLLV VASAAAITGL MLWRLRGKVQ NHPGDTWWQI HYDSITLLPQ HKPSHRGTPM
SRCNVSNAST VKISADCGSF AKTHQDEELF YAPVGLYQGN HVALCYIGEE AEARIKKPTV
LREVWLMCEL KHENIVPFFG VCTEPPNICI VTQYCKKGSL KDVLRNSDHE MDWIFKLSFV
YDIVNGMLFL HGSPLRSHGN LKPSNCLVDS HMQLKLAGFG LWEFKHGSTC RIYNQEATDH
SELYWTAPEL LRLRELPWSG TPQGDVYSFA ILLRDLIHQQ AHGPFEDLEA APEEIISCIK
DPRAPVPLRP SLLEDKGDER IVALVRACWA ESPEQRPAFP SIKKTLREAS PRGRVSILDS
MMGKLEMYAS HLEEVVEERT CQLVAEKRKV EKLLSTMLPS FVGEQLIAGK SVEPEHFESV
TIFFSDIVGF TKLCSLSSPL QVVKLLNDLY SLFDHTIQTH DVYKVETIGD AYMVASGLPI
RNGAQHADEI ATMSLHLLSV TTNFQIGHMP EERLKLRIGL HTGPVVAGVV GITMPRYCLF
GDTVNMASRM ESSSLPLRIH VSQSTARALL VAGGYHLQKR GTISVKGKGE QTTFWLTGKD
GFAVPLPEFT EEEAKVPEIL
