UniProt: A0A1W4XT11

Database: UniProt
Entry: A0A1W4XT11_AGRPL

LinkDB:  A0A1W4XT11_AGRPL 
Original site:  A0A1W4XT11_AGRPL

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (17)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (3)   
   SMART (1)   
All databases (26)   

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ID   A0A1W4XT11_AGRPL        Unreviewed;      1502 AA.
AC   A0A1W4XT11;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Guanylate cyclase {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
GN   Name=LOC108744353 {ECO:0000313|RefSeq:XP_018335565.1};
OS   Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC   Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX   NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018335565.1};
RN   [1] {ECO:0000313|RefSeq:XP_018335565.1}
RP   IDENTIFICATION.
RC   TISSUE=Entire body {ECO:0000313|RefSeq:XP_018335565.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00001436,
CC         ECO:0000256|RuleBase:RU003431};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   RefSeq; XP_018335565.1; XM_018480063.2.
DR   STRING; 224129.A0A1W4XT11; -.
DR   EnsemblMetazoa; XM_018480063.2; XP_018335565.1; LOC108744353.
DR   GeneID; 108744353; -.
DR   KEGG; apln:108744353; -.
DR   InParanoid; A0A1W4XT11; -.
DR   OrthoDB; 3683909at2759; -.
DR   Proteomes; UP000192223; Unplaced.
DR   GO; GO:0005886; C:plasma 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:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd06370; PBP1_SAP_GC-like; 1.
DR   CDD; cd14042; PK_GC-A_B; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 6.10.250.780; -; 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; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR011645; HNOB_dom_associated.
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; GUANYLYL CYCLASE; 1.
DR   PANTHER; PTHR11920:SF474; RECEPTOR-TYPE GUANYLATE CYCLASE GYC76C; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00044; CYCc; 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; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_018335565.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1502
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010714518"
FT   DOMAIN          639..931
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1003..1133
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1233..1254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          940..967
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1502 AA;  168503 MW;  1B922686EE83E271 CRC64;
     MRLGPALLVA LLLPLIARAV LSNTSLKNES APSSEFGAPS GFNTISSHSA PKSSSGFSKT
     PNPVNSIPFT DKQNVLHIRG GNVTSNWSKS FDDDGLDIRY QNVSNNTNKP SLTVESLKVA
     PLYKKKNITV GYLTAAKGDL KERQGLLISG AFTMALEEIN NDPNLLPNVT LVYRWYDTRG
     DTVLATRAMT DMICDGVTAF FGPEGSCHVE AIVAQSRNIP MISYKCSDHT ASSVPTFART
     EPPNTQVTKS VIALLSYYGW QKFSIIYDQA WETVAESLVD QAVKKNMTIN VKKSVGDNHE
     CCERKLPCCS SSYWYQFIQD TKNRTRIYIF LGTSMALIDL MNTMQTAQLF DKGEYMVIYV
     DMNTYSSKEA LKYLWKPETF TKYSNCISHQ KDFLKRGRSL LVVVSTQPSQ NFQEFANRVN
     EYNKREPFGF DVPDKFALRN YSKHVSIYAA YLYDSVKLYA KALHKLLSEE KILNDSIIEE
     IASNGTRIIQ TIIESGTYQS ITGATMRLDK NGDSEGNFSV LALKKVPDSQ SHVRSNFTCH
     FQMVPVGQFQ QGDFPKYKIN RQIDWPGGVK PDDEPSCGFN NEMCPKNDTH LNSIIAAGTL
     AIMLFCAGVI TMSIYRKWKI EQEIEGLLWK IDPNEIRDYY EHDIVQSPSK ASLYSASATS
     FESHGGAQVF ATTATYRGVI VRIKELSFSR KKDISRDVMK EMRLLRELRH DNINSFIGAC
     VEPMALLLVT DYCAKGSLYD IIENEDIKLD KMFIASLVHD LIKGMLYIHN SMLICHGNLK
     SSNCVVTSRW VLQVTDFGLA EMRACAENDS IGEHQYYRSL FWKAPEILRN PQGYIRGTQK
     GDVYAFAIIL YEIIGRKGPF GATGYEPKEI IEFVKNSGEN CDEPFRPNLD ALLDTEMGRE
     DYVLQCVKDC WAENPDNRPD FASVRGRLKR MKDGKNRNIM DQMMDMMEKY ANNLEDLVTE
     RTRLLDEEKK KTEDLLHRML PKPVANRLTM GYGVEPESFD QVTIYFSDIV GFTSMSAEST
     PLQVVNFLND LYTVFDRIIK GYDVYKVETI GDAYMVVSGL PLRNGDKHAG EIASMSLDLL
     NAVRNYSIAH RPKDTLKLRI GIHTGPVVAG VVGLTMPRYC LFGDTVNTAS RMESNGEPLK
     IHISVQCKEA LEKLGGYVVE ERGQVYMKGK GEVLTYWLLG ATDKAIQRRE VDIGDLPPLF
     CRPRKSPKLN NESRQASICG ALGFSGFGSR RHSSVPRGTS IDSTSTVHNA SPVPSRFSSF
     KASNRLALQV PDSGSRLTIN SAISQAFENV EQLGGRRGIR PRRVLSSIAS SCDEPVKSQG
     FLNKIRESRS LDPLPLVKTK QKELSSQFIE ALRRSTRSLE NCDKYGEVQI IAIPEDRLVN
     NNFPNGNVLN PQQQEEDFCL KEDVKEPLLQ SNPNTTILHR RKANDAGNEQ LQKKWRSLET
     VPASGDQISA DNNKKKLLPK NSIRTWLAGI FNGNGLRSSN ASLGKAVMPD YNNLQAEKES
     IV
//

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