ID   CY42_TRYBB              Reviewed;         572 AA.
AC   Q99396;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Receptor-type adenylate cyclase GRESAG 4.2;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase;
DE   AltName: Full=Adenylyl cyclase;
DE   Flags: Fragment;
GN   Name=GRESAG 4.2;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=EATRO 1125;
RX   PubMed=1982555; DOI=10.1016/0166-6851(90)90152-c;
RA   Alexandre S., Paindavione P., Tebabi P., Pays A., Halleux S., Steinert M.,
RA   Pays E.;
RT   "Differential expression of a family of putative adenylate/guanylate
RT   cyclase genes in Trypanosoma brucei.";
RL   Mol. Biochem. Parasitol. 43:279-288(1990).
CC   -!- FUNCTION: Could act as a receptor for an unknown ligand.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000305}.
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DR   EMBL; X52120; CAA36365.1; -; mRNA.
DR   PIR; S14200; S14200.
DR   AlphaFoldDB; Q99396; -.
DR   SMR; Q99396; -.
DR   PRIDE; Q99396; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   Gene3D; 3.30.70.1230; -; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; cAMP biosynthesis; Cell membrane; Glycoprotein; Lyase;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Receptor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..572
FT                   /note="Receptor-type adenylate cyclase GRESAG 4.2"
FT                   /id="PRO_0000195738"
FT   TOPO_DOM        <1..225
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..572
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          269..424
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   572 AA;  63683 MW;  1F3EE304E091AFDD CRC64;
     RKTLLTFGLN LSSSVVLTPG DSVGEHLPKS GITFIIGLVV DDIVVIEEHL RIHTKARVLV
     QFSDIALLYN EFVQAFNNSD GAKHLLFATS LPHWADVDTT SETVRRFHEA VPEVEKWTPL
     SLLGFATGRL MQRNLQRMDL ATSDLLSGLF FNETFITVDD MQYGAYKDAE GVATAEESLS
     NFGATDISVW SMARALRSDE PVLQDPMSPS MVYTVPNGNA LTPAQLDWCG WCRFACADTG
     SRLTVFLCCI MRNKRDNDNA PKELADPVTL IFTDIESSTA QWATQPELMP DAVATHHSMV
     RSLIENYDCY EVKTVGDSFM IACKSPFAAV QLAQELQLRF LRLDWGTTVF DEFYREFEER
     HAEEGDGKYK PPTARLDPEV YRQLWNGLRV RVGIHTGLCD IRYDEVTKGY DYYGQTANTA
     ARTESVGNGG QVLMTCETYH SLSTAERSQF DVTPLGGVPL RGVSEPVEVY QLNAVPGRSF
     AELRLDRVLD VLDIFGEGTA ASTSDYSSTL AELSETAQAI AVSLQSLMGV FTQAQRQGTL
     MPFCERWRVR CPRKVHPRGT TATVRRLSVA LQ