ADCYA_RABIT
ID ADCYA_RABIT Reviewed; 1610 AA.
AC Q866F4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Adenylate cyclase type 10;
DE EC=4.6.1.1;
DE AltName: Full=Germ cell soluble adenylyl cyclase;
DE Short=sAC;
DE AltName: Full=Testicular soluble adenylyl cyclase;
GN Name=ADCY10; Synonyms=SAC;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=15322879; DOI=10.1007/s00427-004-0432-2;
RA Kobayashi M., Buck J., Levin L.R.;
RT "Conservation of functional domain structure in bicarbonate-regulated
RT 'soluble' adenylyl cyclases in bacteria and eukaryotes.";
RL Dev. Genes Evol. 214:503-509(2004).
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP. May
CC function as sensor that mediates responses to changes in cellular
CC bicarbonate and CO(2) levels (By similarity). Has a critical role in
CC mammalian spermatogenesis by producing the cAMP which regulates cAMP-
CC responsive nuclear factors indispensable for sperm maturation in the
CC epididymis. Induces capacitation, the maturational process that sperm
CC undergo prior to fertilization (By similarity). Involved in ciliary
CC beat regulation (By similarity). {ECO:0000250|UniProtKB:Q8C0T9,
CC ECO:0000250|UniProtKB:Q96PN6}.
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 Evidence={ECO:0000250|UniProtKB:Q96PN6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96PN6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96PN6};
CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC (in vitro). {ECO:0000250|UniProtKB:Q96PN6};
CC -!- ACTIVITY REGULATION: Activated by manganese or magnesium ions. In the
CC presence of magnesium ions, the enzyme is activated by bicarbonate.
CC Calcium mildly increases the enzyme activity, also in the presence of
CC magnesium ions. {ECO:0000250|UniProtKB:Q96PN6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96PN6};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q96PN6}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q96PN6}. Nucleus {ECO:0000250|UniProtKB:Q96PN6}.
CC Cell projection, cilium {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96PN6}. Note=Distributed to subcellular
CC compartments containing cAMP targets. Found as a plasma membrane-
CC associated protein, protein concentrated in the perinuclear region and
CC protein colocalized with actin or tubulin.
CC {ECO:0000250|UniProtKB:Q96PN6}.
CC -!- DOMAIN: The N-terminal guanylate cyclase domains are required for
CC enzyme activity. Fragments containing the first 470 amino acid residues
CC are fully active. {ECO:0000250|UniProtKB:Q96PN6}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AY212921; AAO38673.1; -; mRNA.
DR RefSeq; NP_001075622.1; NM_001082153.1.
DR AlphaFoldDB; Q866F4; -.
DR SMR; Q866F4; -.
DR STRING; 9986.ENSOCUP00000001957; -.
DR PRIDE; Q866F4; -.
DR GeneID; 100008902; -.
DR KEGG; ocu:100008902; -.
DR CTD; 55811; -.
DR eggNOG; ENOG502QPPT; Eukaryota.
DR InParanoid; Q866F4; -.
DR OrthoDB; 37924at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0071890; F:bicarbonate binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006171; P:cAMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0071241; P:cellular response to inorganic substance; ISS:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:InterPro.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR016577; Adenylate_cyclase_typ10.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR PIRSF; PIRSF011131; Soluble_adenylyl_cyclase; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55073; SSF55073; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; cAMP biosynthesis; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Lyase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1610
FT /note="Adenylate cyclase type 10"
FT /id="PRO_0000317103"
FT DOMAIN 42..179
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 293..418
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 47..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 95
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 167
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 176
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 337
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT BINDING 412..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96PN6"
SQ SEQUENCE 1610 AA; 185520 MW; B86C2B4E8A4E3207 CRC64;
MNTRKEELQD RAIVRIAAHL PDLIVYGDFS PQRPSVDYFD GVLMFVDISG FTAMTEKFST
AMYMDRGAEQ LVEILNYYIS AIVEKVLIFG GDILKFAGDA LLALWKVERK QLKNIITVVI
KCSLEIHGLF GTQESEEGLD IRVKIGLAAG HISMLVFGDE TRNHFLVIGQ AVDDVRLAQN
MARMNDVILS PNCWQLCDRS MIEIERIPDQ RAVKVNFLKP PPSFNFDEFF NKCMTFMDYY
PSGDHKNLLR LACMLESDPD LELSLQKYVM ESILKQIDDK QLRGYLSELR PVTIVFVNLM
FQDQNKAEVI GSAIQDACVH ISSVLKVFRG QINKVFMFDK GCSFLCVFGF PGEKAPDEVT
HALESAVDIF DFCSQVHKIH TVSIGVASGI VFCGIVGHTV RHEYTVIGQK VNIAARMMMY
YPGIVTCDSV TYNGSNLPPY FFKELPKKLM KGVGDSGPVY QCLGLNEKVM FGMAYLTCNR
NEGYPLLGRD KEIKYFMCTM KEFLMSNCSR VLMYEGLSGF GKSRILMEIE YLAQGENHRT
IAIALTKVSF HQNFYTIQIL MANVLGLDTC KHYKERQTNL QNKVKTLLDE KFHCLLNDIF
HVQFPISREI SKMSTFRKQK QLEALFMKIL EQTVKEERII FIIDEAQFVD YASWIFMEKL
IRTVPIFIIM SLSPFTEIPC AAASAIMKNR NTTYVTLGAV QPNDIRNKVC LDLNVSSIPK
ELDLYLVEGS CGIPFYCEEL VKNLDHHRVL VFQQMETEEK TKVTWNNLFK NFIKPTEEFK
MSGLGNEEGT EEICKLASGV RLKNLSPPAS LKEISLVQLD SMSLSHQMLV RCAAIIGLTF
TTELLFEILP CWNMKMMIKA LATLVESNIF DCFRDGKDLR LALKQNAASF EVHNRSLSLQ
PTEGIAHGEE EELRELESEV IECHIIRFCK PMMQKTAYEL WLKDQKKAMH LKCARFLEEN
AHRCDHCRSG DFIPYHHFTV DIRLNTLDMD TIKKMATSHG FETEEEIKIS RAGIPKNSEL
FSENLSPEEI GERILGFFDV ILTKMKTSKE DIIPLESCQC EEILEIVILP LAQHFLALGE
NNKALYYFLE ITSAYLTLGD NYMAYMYLNE GERLLKTLKK EKSWSQTFES ATFYSLKGQV
CFNMGQMVLA KKMLRKALKL LNRIFPYNLI SLFLHTHMEK NRHFHYVTQQ AQESSPPGKK
RLAHLYQQTA CFSLLWQIYS LNYFFHHKYY GHLAAMMELN TALETQNDFQ IIKAYLDYAM
YHHLAGYQGV WFKYEVKAME QIFNLPLKGE GIEIVAYVAG KLSYIKLMMG YLDLAIELGA
RAHKMWALLQ NPNQHYVVLC RLSKSLFLKN RYKHLIQMLR RLWDLSVAEG HIISKAFFYL
VCLDIMLYSG FVYRTFEECL EFIIQNEDNR ILKFQSGLLL GLYSSIAIWY GRLQEWDNFY
VFSNRAKTLV SRRTPTILYY DGVSRYMEGQ VLQLQKQIEE QSETAQDSGV ELLKSLESLV
AQNTTGPVFY PRLYHLMAYI CILMGDGQNC DLFLNTALKL SEIQGNVLEK CWLNMSKEWW
YSNCTLTEDQ WLHTILSLPA WEKIVSGKVN IHDVQKNKFL MRVNILDNPF
