ID I3K4Z7_ORENI Unreviewed; 1127 AA.
AC I3K4Z7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU000515, ECO:0000256|RuleBase:RU003431};
DE Includes:
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
DE Includes:
DE RecName: Full=Guanylate cyclase {ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|RuleBase:RU003431};
GN Name=LOC100699899 {ECO:0000313|Ensembl:ENSONIP00000016192.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000016192.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000016192.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles.
CC Binds two molecules of 5-aminolevulinate per subunit, each at a
CC distinct site, and catalyzes their condensation to form
CC porphobilinogen. {ECO:0000256|ARBA:ARBA00025628}.
CC -!- FUNCTION: Receptor for the C-type natriuretic peptide NPPC/CNP hormone.
CC Has guanylate cyclase activity upon binding of its ligand. May play a
CC role in the regulation of skeletal growth.
CC {ECO:0000256|ARBA:ARBA00043880}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen;
CC Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00001227,
CC ECO:0000256|RuleBase:RU000515};
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 Evidence={ECO:0000256|RuleBase:RU003431};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004694}.
CC -!- SUBUNIT: Homooctamer; active form. Homohexamer; low activity form.
CC {ECO:0000256|ARBA:ARBA00025861}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC ECO:0000256|RuleBase:RU004161}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR AlphaFoldDB; I3K4Z7; -.
DR Ensembl; ENSONIT00000016207.2; ENSONIP00000016192.2; ENSONIG00000012850.2.
DR eggNOG; KOG2794; Eukaryota.
DR GeneTree; ENSGT00940000156223; -.
DR HOGENOM; CLU_035731_0_1_1; -.
DR InParanoid; I3K4Z7; -.
DR TreeFam; TF300665; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000005207; Linkage group LG7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07302; CHD; 1.
DR CDD; cd04824; eu_ALAD_PBGS_cysteine_rich; 1.
DR CDD; cd14042; PK_GC-A_B; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR030656; ALAD_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
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 PANTHER; PTHR11920:SF508; ATRIAL NATRIURETIC PEPTIDE RECEPTOR 2; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR Pfam; PF00490; ALAD; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW ECO:0000256|RuleBase:RU003431}; Coiled coil {ECO:0000256|SAM:Coils};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Osteogenesis {ECO:0000256|ARBA:ARBA00022855};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 594..867
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 942..1072
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 879..906
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1127 AA; 126643 MW; CF4C13334C52B860 CRC64;
MQTPAESILH SGYFHPTLRY WQTCIADLRP DNLIYPIFVT DGADAVEPIG SLPGQARYGV
NKLEGMLRPL VDNGLKCVLI FGVPAKIAKD ERGSGADTND TPAVLAVKKI RSLFPELLVA
CDVCLCPYTS HGHCGILNDD GTLNNDASCL RLAEVALAYA RAGCHIIAPS DMMDGRVRAI
KQALISNGLG NKVSVLSYSA KFASCYYGPF RDAAQSKPAF GDRRCYQLPP GARGLAIRAV
ERDVREGADM LMVKPGLPYL DIMREVKDKF PTHPLAVYNV SGEFAMIWHG AQAGAFDLKA
AVMEAMTAFR RAVVYICGPL DTFMTIMEQF QNDIQDPENY AIFYLDVFAE ILADRKPWQK
ADWADPIKVF KSVFVITYRP PDNPEYKDFQ KKLHARAQRD FGVHLEPSLM DYIAGSFYDG
FILYAMALQE TLAEGGAQND GINITMRTQN RQFWGVTGLV STDEKNARNI DVDLWAMTNQ
ETGEYGVVAY YNGTTKDIIW SQTEKIHWPS GGPPLDNPPC VFSTDDPSCN DGHLPVLGIV
AVGSGLALII FGISSFLIYR KLKLEKELAG MLWRIRWEDL QFESPNKYHK RAGSRLTLSQ
RGSSYGSLIT AHGKYQLFAK TGYFKGNLVA IKHVNKKRIE LTRQVLMELK HMRDVQFNHL
TRFIGACIDP PNVCIVTEYC PRGSLQDILE NESINLDWMF RYSLINDIVK GMNYLHNSYF
GCHGNLKSSN CVVDSRFVLK ITDFGLVSFR TSSENDDSHS LYAKKLWTAP ELLIYDHHPP
QGTQKGDVYS FGIILQEIAL RNGPFYVEGM DLSPKEIVQK VRNGQKPYFR PTTDMRYHSE
ELTILMEGCW AEDPAERPDF SHIKIYMAKL NKEGSTSILN NLLSRMEQYA NNLENLVEER
TQAYLEEKRK AENLLYQILP HSVAEQLKRG ETVQAEAFDS VTIYFSDIVG FTSMSAESTP
LQVVTLLNDL YTCFDAIIDN FDVYKVETIG DAYMVVSGLP VRNGKLHARE IAGMSLALLE
QVKTFKIRHR PNDQLRLRIG IHTGPVCAGV VGLKMPRYCL FGDTVNTASR MESNGEALKI
HVSSATKEVL DEFGYFDLQL RGDVEMKGKG KMRTYWLLGE KTDVYVI
//
