CYAA_TRYEQ
ID CYAA_TRYEQ Reviewed; 469 AA.
AC P26338;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Receptor-type adenylate cyclase;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
DE Flags: Fragment;
GN Name=ESAG4C;
OS Trypanosoma equiperdum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5694;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CL;
RX PubMed=2065652; DOI=10.1002/j.1460-2075.1991.tb07735.x;
RA Ross D.T., Raibaud A., Florent I.C., Sather S., Gross M.K., Storm D.R.,
RA Eisen H.;
RT "The trypanosome VSG expression site encodes adenylate cyclase and a
RT leucine-rich putative regulatory gene.";
RL EMBO J. 10:2047-2053(1991).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59386; CAA42029.1; -; Genomic_DNA.
DR PIR; S16359; S16359.
DR AlphaFoldDB; P26338; -.
DR SMR; P26338; -.
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 3: Inferred from homology;
KW ATP-binding; cAMP biosynthesis; Cell membrane; Glycoprotein; Lyase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Receptor;
KW Transmembrane; Transmembrane helix.
FT CHAIN <1..469
FT /note="Receptor-type adenylate cyclase"
FT /id="PRO_0000195741"
FT TOPO_DOM <1..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 103..257
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 469 AA; 50819 MW; F87638C3152DEA3A CRC64;
VDTAEKLSKN GCASNYGATQ ISVWSMARAL NASIPPLTNP MTPSMTFRNS NAGRISGVAL
VGVIIGGALA LFLVVALGVV PYFFLHNTRD NNLAPKELTD PVTLIFTDIE SSTALWAAHP
ELMPDAVATH HRLIRSLIGR YGCYEVKTVG DSFMIASKSP FAAVQLAQEL QLCFLHHDWG
TNAIDESYQQ LEQQRAEEDA KYTPPTARLD LKVYSRLWNG LRVRVGIHTG LCDIRRDEVT
KGYDYYGRTS NMAARTESVG NGGQVLMTTA AYMSLSAEER EQIDVTALGD VPLRGVAKPV
EMYQLNAVPG RTFAGLRLEH ELLNDDEDQT TTSCSDHSSS RTDLSVAAQT IAASLQSLLG
TFTPAQRQKA LIPFCERWRV PLPQKVGNVW DNDGCQEAIR RVAAKVGRVM DFGTRKASSS
VTSLERGGSL FSAGGATVAT VASSSNFSCV DGRCGTVQLI DLENDSTTS