CYA4_TRYBB
ID CYA4_TRYBB Reviewed; 1235 AA.
AC Q26721;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Receptor-type adenylate cyclase ESAG 4;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
DE AltName: Full=Antigen 4;
DE AltName: Full=Expression site-associated protein 4;
GN Name=ESAG4;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EATRO 1125;
RX PubMed=2720787; DOI=10.1016/0092-8674(89)90798-8;
RA Pays E., Tebabi P., Pays A., Coquelet H., Revelard P., Salmon D.,
RA Steinert M.;
RT "The genes and transcripts of an antigen gene expression site from T.
RT brucei.";
RL Cell 57:835-845(1989).
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
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DR EMBL; M33720; AAA30158.1; -; Genomic_DNA.
DR PIR; D32433; D32433.
DR AlphaFoldDB; Q26721; -.
DR SMR; Q26721; -.
DR PRIDE; Q26721; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Receptor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1235
FT /note="Receptor-type adenylate cyclase ESAG 4"
FT /id="PRO_0000195736"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..1235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 900..1054
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 905
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 948
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1235 AA; 136458 MW; CCAC3E2D78D3DC7A CRC64;
MNMLHLSDRN ASLAPSGGEH SLPTGGAVCR DAMDILPVIL RAPVALLLLL VVLPQLSVGA
EANVTVKVLS ATWNWYMPRK YVTAINAGFN ASLKSRNWTV AGSVNVQVVY PSNLDLMPED
FIKKQLELET DQNKIVIVYG PLGDKSVMHS IPHLMNHRVV AFGLITGSTF IRQWNPYLYF
LRADPAAETL VLIRYSLCQL RVLRLGFMYL QGVHYGDEEY ALTVNVMSRM GYELHGVFTV
MSPDGKPAPD AEFKEVFERF ATALPQAIIV FGAPVDDTAK FLMMMAVDER IARSYILSPS
SVQLSLIEMW QLALEAAGAS FAPGQLLFTG TNPLAKDSQY TAIKRFQEVM SEYLKAHVGE
TNITEADYFL THDLEGELMV YGWISGEVLS QALSNLEWLK DRATFVRSLY DQRRYVINDI
VIGDYGGTCE GDAAKHGATC ECNQGSKAVY VKEMLENGQK TSVRSGFTVL KASLCYTDSS
ELHGPLDGLV VFMKDDDIAS KAAALWQKGT SHLVGKGDLG YSDRFFLHAF NTTIAEAAND
LRRDQGERIV TAVFGPVTEA MLDTPNITFI DPLELKPRLN KFRRNVIHLS PTLEQQLYVL
SSYLAGAGVG NVDAVICSNE ADGIADFLRS SLTEFAVSLR SAVIREDGED VGKYLPMSGT
VFVIGLSVPD VKEIARKLEE RNDLRVIVLF GEFSFLYDLF ATALNNTAGA ARLVFATSLP
HWGDTETSSK TAQLFHDVEK DSRLWTPLSV LAFATGRLMR VILLHVEEMS PETLVNFFYT
DSSIVSDDMR YGVFDDTKCV DTANKLSKNG CASNYGATQI SVWSMARALN ASIPPLTNPM
TPSMTFRNSN AGRISGASLV GIIIGGALAL FLVVALGVVP YFFLRNTVIT ICTKDDRPVT
LIFTDIESST ALWAAHPEVM PDAVATHHRL IRTLISKYEC YEVKTVGDSF MIASKSPFAA
VQLAQELQLC FLHHDWGTNA IDESYQQFEQ QRAEDDSDYT PPTARLDPKV YSRLWNGLRV
RVGIHTGLCD IRRDEVTKGY DYYGRTSNMA ARTESVANGG QVLMTHAAYM SLSAEERQQI
DVTALGDVPL RGVPKPVEMY RLNAVPGRTF SVLRLELELL NDDEDQTTTS CSDHSSSRTD
LSVAAQTIAA SLQSLLGTFT PAQRQKALIP FCERWRVPLP QKVGNVWDDD GCQEVVRRVA
AKVGRVMDFG TRKPSSSVTS WKGVEVSSQV EERLL
