GCY_STRPU
ID GCY_STRPU Reviewed; 1125 AA.
AC P16065;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Speract receptor;
DE EC=4.6.1.2;
DE AltName: Full=Guanylate cyclase;
DE Flags: Precursor;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2564849; DOI=10.1016/s0021-9258(18)83382-8;
RA Thorpe D.S., Garbers D.L.;
RT "The membrane form of guanylate cyclase. Homology with a subunit of the
RT cytoplasmic form of the enzyme.";
RL J. Biol. Chem. 264:6545-6549(1989).
CC -!- FUNCTION: Implicated as a cell-surface receptor on spermatozoa for
CC 'speract' a chemotactic peptide, and on various other cells as a
CC receptor for atrial natriuretic peptide.
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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; M22444; AAA30051.1; -; mRNA.
DR PIR; A33535; OYURCP.
DR RefSeq; NP_999705.1; NM_214540.1.
DR AlphaFoldDB; P16065; -.
DR SMR; P16065; -.
DR STRING; 7668.SPU_024339-tr; -.
DR EnsemblMetazoa; NM_214540; NP_999705; LOC373321.
DR GeneID; 373321; -.
DR KEGG; spu:373321; -.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_2_1; -.
DR OMA; DNRWVLQ; -.
DR OrthoDB; 463769at2759; -.
DR PhylomeDB; P16065; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
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; IPR011645; HNOB_dom_associated.
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; PF07701; HNOBA; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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 cGMP biosynthesis; Glycoprotein; GTP-binding; Lyase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1125
FT /note="Speract receptor"
FT /id="PRO_0000012391"
FT TOPO_DOM 22..510
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..1125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 571..839
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 914..1044
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1125 AA; 126257 MW; EAE76757BCF92782 CRC64;
MAHARHLFLF MVAFTITMVI ARLDFNPTII NEDRGRTKIH VGLLAEWTTA DGDQGTLGFP
ALGALPLAIS LANQDSNILN GFDVQFEWVD THCDINIGMH AVSDWWKRGF VGVIGPGCGC
TYEGRLASAL NIPMIDYVCD ENPVSDKSIY PTFLRTIPPS IQVVEAIILT LQRYELDQVS
VVVENITKYR NIFNTMKDKF DERDYEILHE EYYAGFDPWD YEMDDPFSEI IQRTKETTRI
YVFFGDASDL RQFAMTALDE GILDSGDYVI LGAVVDLEVR DSQDYHSLDY ILDTSEYLNQ
INPDYARLFK NREYTRSDND RALEALKSVI IVTGAPVLKT RNWDRFSTFV IDNALDAPFN
GELELRAEID FASVYMFDAT MQLLEALDRT HAAGGDIYDG EEVVSTLLNS TYRSKTDTFY
QFDENGDGVK PYVLLHLIPI PKGDGGATKD SLGMYPIGTF NRENGQWGFE EALDEDANVL
KPVWHNRDEP PLDMPPCGFH GELCTNWALY LGASIPTFLI IFGGLIGFFI YRKRAYEAAL
DSLVWKVDWS EVQTKATDTN SQGFSMKNMV MSAISVISNA EKQQIFATIG TYRGTVCALH
AVHKNHIDLT RAVRTELKIM RDMRHDNICP FIGACIDRPH ISILMHYCAK GSLQDILEND
DIKLDSMFLS SLIADLVKGI VYLHSSEIKS HGHLKSSNCV VDNRWVLQIT DYGLNEFKKG
QKQDVDLGDH AKLARQLWTS PEHLRQEGSM PTAGSPQGDI YSFAIILTEL YSRQEPFHEN
EMDLADIIGR VKSGEVPPYR PILNAVNAAA PDCVLSAIRA CWPEDPADRP NIMAVRTMLA
PLQKGLKPNI LDNMIAIMER YTNNLEELVD ERTQELQKEK TKTEQLLHRM LPPSIASQLI
KGIAVLPETF EMVSIFFSDI VGFTALSAAS TPIQVVNLLN DLYTLFDAII SNYDVYKVET
IGDAYMLVSG LPLRNGDRHA GQIASTAHHL LESVKGFIVP HKPEVFLKLR IGIHSGSCVA
GVVGLTMPRY CLFGDTVNTA SRMESNGLAL RIHVSPWCKQ VLDKLGGYEL EDRGLVPMNG
KGEIHTFWLL GQDPSYKITK VKPPPQKLTQ EAIEIAANRV IPDDV
