GUC2G_MOUSE
ID GUC2G_MOUSE Reviewed; 1100 AA.
AC Q6TL19; Q8BWU7;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Guanylate cyclase 2G;
DE EC=4.6.1.2 {ECO:0000269|PubMed:14713286};
DE AltName: Full=Guanylyl cyclase receptor G;
DE Short=mGC-G {ECO:0000303|PubMed:14713286};
DE Flags: Precursor;
GN Name=Gucy2g;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, HOMOOLIGOMERIZATION,
RP INTERACTION WITH NPR1, TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF CYS-458 AND CYS-465.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=14713286; DOI=10.1042/bj20031624;
RA Kuhn M., Ng C.K., Su Y.H., Kilic A., Mitko D., Bien-Ly N., Komuves L.G.,
RA Yang R.B.;
RT "Identification of an orphan guanylate cyclase receptor selectively
RT expressed in mouse testis.";
RL Biochem. J. 379:385-393(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 662-1100.
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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:0000269|PubMed:14713286};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC Evidence={ECO:0000269|PubMed:14713286};
CC -!- SUBUNIT: Homooligomer. In vitro interacts with NPR1/GC-A.
CC {ECO:0000269|PubMed:14713286}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:14713286};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:14713286}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:14713286}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AY395631; AAR28089.1; -; mRNA.
DR EMBL; AK049940; BAC33995.1; -; mRNA.
DR CCDS; CCDS38026.1; -.
DR RefSeq; NP_001074545.1; NM_001081076.2.
DR AlphaFoldDB; Q6TL19; -.
DR SMR; Q6TL19; -.
DR BioGRID; 216200; 1.
DR STRING; 10090.ENSMUSP00000068253; -.
DR GlyGen; Q6TL19; 9 sites.
DR iPTMnet; Q6TL19; -.
DR PhosphoSitePlus; Q6TL19; -.
DR PaxDb; Q6TL19; -.
DR PRIDE; Q6TL19; -.
DR ProteomicsDB; 269641; -.
DR DNASU; 73707; -.
DR Ensembl; ENSMUST00000069183; ENSMUSP00000068253; ENSMUSG00000055523.
DR GeneID; 73707; -.
DR KEGG; mmu:73707; -.
DR UCSC; uc008hxo.2; mouse.
DR CTD; 73707; -.
DR MGI; MGI:106025; Gucy2g.
DR VEuPathDB; HostDB:ENSMUSG00000055523; -.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000163069; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q6TL19; -.
DR OMA; LYQGNHV; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; Q6TL19; -.
DR TreeFam; TF106338; -.
DR BRENDA; 4.6.1.2; 3474.
DR BioGRID-ORCS; 73707; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Gucy2g; mouse.
DR PRO; PR:Q6TL19; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6TL19; protein.
DR Bgee; ENSMUSG00000055523; Expressed in dentate gyrus of hippocampal formation granule cell and 24 other tissues.
DR Genevisible; Q6TL19; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
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; IDA:MGI.
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 1: Evidence at protein level;
KW Cell membrane; cGMP biosynthesis; Glycoprotein; GTP-binding; Lyase;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..1100
FT /note="Guanylate cyclase 2G"
FT /id="PRO_0000042178"
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 546..837
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 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
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 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 458
FT /note="C->S: Does not affect guanylate cyclase activity;
FT when associated with S-465."
FT /evidence="ECO:0000269|PubMed:14713286"
FT MUTAGEN 465
FT /note="C->S: Does not affect guanylate cyclase activity;
FT when associated with S-458."
FT /evidence="ECO:0000269|PubMed:14713286"
FT CONFLICT 662..665
FT /note="DIVN -> LLLQ (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1100 AA; 122546 MW; C0325B84081595FB CRC64;
MASRTRSESP LEPRLYAGAG SRADHPSLVL MLSVVMLVTC LEAAKLTVGF HAPWNISHPF
SVQRLGAGLQ TVVDKLNSEP VGLGNVSWEF TYTNSTCSAK ESLAVFIDQV QKEHISALFG
PACPEAAEVI GLLASEWNIP LFDFVGQMAA LKDHFWCDTC VTLVPPKQEI SAVLRESLRY
LGWEHIGVFG GSSADSSWEQ VDEMWGAVED GLQFHFNITA SMRYNSSSSD LLQEGLRNMS
YVARVIILIC SSEDARRILQ AAVDLGLDTG EFVFILLQQL EDSFWKEVLT KDKVIRFPKV
YESVFLIAPS AYGGGIGDDG FRKQVSQELR RPPFQSSITS EDQVSPYSAY LHDALLLYAQ
TVEEMRKAEK DFRDGRQLIS TLRAGQVTLQ GITGPVLLDS QGKRHVDYSV YALQESGNRS
LFLPFLHYDS FQKVIRPWRN DSNTSWPHGS LPEYKPGCGF HNDLCKTKPP TVAGMTVTVT
AVIPTVTFLV LASAAAITGL MLWRLRGKVQ SHPGDTWWQI RYDSITLLPQ HKLSHRGTPV
SRRNVSDTST VKASADCGSL VKRHQDEELF FAPVGLYQGN QVALCYIGDE AEAWVKKPTV
RREVCLMCEL KHENIVPFFG VCTEPPNICI VTQYCKKGSL QDVMRNSDHE IDWIFKLSFA
YDIVNGLLFL HGSPLRSHGN LKPSNCLVDS HMQLKLSGFG LWEFKHGSTW RSYNQEATDH
SELYWTAPEL LRLRESPCSG TPQGDVYSFA ILLRDLIHQQ AHGPFEDLEA APEEIISRIK
DPRAPVPLRP SLLEDKGDGR IVALVRECWD ESPELRPIFP SIKKTLREAS PRGHVSILDS
MMGKLETYAN HLEEVVEERT RELVAEKRKV EKLLSTMLPS FVGEQLIAGK SVEPEHFESV
TIFFSDIVGF TKLCSLSSPL QVVKLLNDLY SLFDHTIQSH DVYKVETIGD AYMVASGLPI
RNGAQHADEI ATMALHLLSV TTHFQIGHMP EERLKLRIGL HTGPVVAGVV GITMPRYCLF
GDTVNMASRM ESSSLPLRIH VSQSTAGALL AAGGYHLQKR GTISVKGKGE QTTFWLKGKD
GFPVPLPEFT EEEAKVSEIL
