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GCY12_CAEEL
ID   GCY12_CAEEL             Reviewed;        1679 AA.
AC   Q19187;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 3.
DT   03-AUG-2022, entry version 178.
DE   RecName: Full=Receptor-type guanylate cyclase gcy-12 {ECO:0000305};
DE            EC=4.6.1.2 {ECO:0000269|PubMed:9096403};
DE   Flags: Precursor;
GN   Name=gcy-12 {ECO:0000312|WormBase:F08B1.2a};
GN   ORFNames=F08B1.2 {ECO:0000312|WormBase:F08B1.2a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=9096403; DOI=10.1073/pnas.94.7.3384;
RA   Yu S., Avery L., Baude E., Garbers D.L.;
RT   "Guanylyl cyclase expression in specific sensory neurons: a new family of
RT   chemosensory receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3384-3387(1997).
RN   [3] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21124861; DOI=10.1371/journal.pgen.1001211;
RA   Fujiwara M., Teramoto T., Ishihara T., Ohshima Y., McIntire S.L.;
RT   "A novel zf-MYND protein, CHB-3, mediates guanylyl cyclase localization to
RT   sensory cilia and controls body size of Caenorhabditis elegans.";
RL   PLoS Genet. 6:E1001211-E1001211(2010).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=26434723; DOI=10.1534/genetics.115.177543;
RA   Fujiwara M., Hino T., Miyamoto R., Inada H., Mori I., Koga M., Miyahara K.,
RA   Ohshima Y., Ishihara T.;
RT   "The importance of cGMP signaling in sensory cilia for body size regulation
RT   in Caenorhabditis elegans.";
RL   Genetics 201:1497-1510(2015).
CC   -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC       messenger cGMP (PubMed:9096403). Acts upstream of cGMP-dependent
CC       protein kinase egl-4, most likely by providing cGMP to the kinase in
CC       chemosensory neurons to regulate body size (PubMed:21124861,
CC       PubMed:26434723). {ECO:0000269|PubMed:21124861,
CC       ECO:0000269|PubMed:26434723, ECO:0000269|PubMed:9096403}.
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:0000269|PubMed:9096403};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 20-25 degrees Celsius. Loses activity at
CC         temperatures above 35 degrees Celsius. {ECO:0000269|PubMed:9096403};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Cell projection, cilium
CC       {ECO:0000269|PubMed:21124861, ECO:0000269|PubMed:26434723}. Perikaryon
CC       {ECO:0000269|PubMed:26434723}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:26434723}. Note=Localization in cilium of sensory
CC       neurons is regulated by daf-25 (PubMed:21124861). Cilia localization
CC       may be important for regulating body size (PubMed:21124861). Localizes
CC       to small puncta around the nucleus in the perikaryon (PubMed:26434723).
CC       Enriched at the proximal segment of the cilia or at the distal dendrite
CC       tip close to the cilia (PubMed:26434723). {ECO:0000269|PubMed:21124861,
CC       ECO:0000269|PubMed:26434723}.
CC   -!- TISSUE SPECIFICITY: Expressed in PHA sensory neurons and in head
CC       muscles (PubMed:9096403, PubMed:21124861). Expressed in chemosensory
CC       neurons AWC, ASE, ASJ, AUA, PHA and PHB, interneuron PVQ, several other
CC       unidentified head neurons, an excretory gland cell and head muscles
CC       (PubMed:26434723). Highly expressed in the sensory cila at the nose tip
CC       (PubMed:26434723). {ECO:0000269|PubMed:21124861,
CC       ECO:0000269|PubMed:26434723, ECO:0000269|PubMed:9096403}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Increased body size and increased formation of
CC       dauer larvae. Double knockout with che-2 rescues the locomotion defect
CC       in the single che-2 mutant. {ECO:0000269|PubMed:26434723}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR   EMBL; FO081082; CCD68976.2; -; Genomic_DNA.
DR   RefSeq; NP_494995.2; NM_062594.2.
DR   AlphaFoldDB; Q19187; -.
DR   STRING; 6239.F08B1.2; -.
DR   EPD; Q19187; -.
DR   PaxDb; Q19187; -.
DR   EnsemblMetazoa; F08B1.2a.1; F08B1.2a.1; WBGene00001538.
DR   GeneID; 173902; -.
DR   KEGG; cel:CELE_F08B1.2; -.
DR   UCSC; F08B1.2; c. elegans.
DR   CTD; 173902; -.
DR   WormBase; F08B1.2a; CE01900; WBGene00001538; gcy-12.
DR   eggNOG; KOG1023; Eukaryota.
DR   GeneTree; ENSGT00940000168507; -.
DR   HOGENOM; CLU_001072_0_0_1; -.
DR   InParanoid; Q19187; -.
DR   OMA; PTDEPMC; -.
DR   OrthoDB; 229634at2759; -.
DR   PhylomeDB; Q19187; -.
DR   PRO; PR:Q19187; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00001538; Expressed in larva and 3 other tissues.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR   GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IDA:WormBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0061067; P:negative regulation of dauer larval development; IMP:UniProtKB.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR   GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IGI:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IGI:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; -; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
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   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cell projection; cGMP biosynthesis;
KW   Coiled coil; Glycoprotein; GTP-binding; Lyase; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..1679
FT                   /note="Receptor-type guanylate cyclase gcy-12"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000433281"
FT   TOPO_DOM        45..592
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        593..613
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        614..1679
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          639..955
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          1027..1158
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   REGION          1412..1434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1534..1580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1623..1679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          961..997
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1412..1430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1534..1560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1565..1580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1636..1679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         645..653
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         696
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1032
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         1032
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         1033
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         1076
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         1076
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        516
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1679 AA;  189973 MW;  35828FA6A77EAB2E CRC64;
     MWPTSVEALR FYHTFAFSPG RRRRLFGLSI VFVIAALCVT SCDADAVPAP SPEAEPSLGA
     GANPYLLDSL VKRLPKKGDK KEILISYLAA VPTLMGEIDQ YLLNLSASNS AQNSSKDRES
     FSKKLNQIVH CLTTDAYVSV VSGALVAAIV EINQDKDLIP AYQLKYVFGN TCGNDSHSTR
     LFMEHWQAGA RVFIGPEKNC KTEAAMAASQ NLPIISYRCN DQDISRDDYH YRTFARTVPP
     AGEIFKAFMS LMKQYNWRKF SVVYDVKKGQ VKNELFETLK RMVETENKFE EHKFEIMNVS
     KLEFSKMDIS SQQDIQSIEN AIKSTMQTTR IYLTFDNVRL FRTMLSIMGE MGLTQQDYML
     IYVDTNYDWL NVYHSMNNHF LRNTMTYLHH SWDANNSSDR KMLDYARSAL SIIPTPVKLN
     SQRFYNFWKK AGDYMHHFGV QKADNLKGNR IACYLYDAVY LYAKAIHELV EEYGNDDSYD
     PTADGKAIID RIVNKKYRSI QGFDMRIDER GNSKGNFSLL SWQKVAPIMN KSDPSYYPLD
     HALDLTAIFV EAPDKDRLPN LQFKSSRIQW LKGEPPPDEP VCGFHGENCR KKGIFSYLTV
     VVMILIAVFS LVLTGFTLNY IRSRRFEKEL SMIWKIDPYE VRRVVGGVNN ESTASLMQSD
     VMQFAKTKTP WWSKAPVQGT GMRGLASYKG TLVGLKDLMY GRKPKDLTRE AKKELRAMRQ
     LAHPNVNNFL GIIVCQYSVT VVREYCSKGS LHDILRNENL KLDHMYVASF VDDLVKGMVY
     IHDSELKMHG NLKSTNCLIT SRWTLQIADF GLRELREGIM YDSSYNIWEN FLWTAPEAMT
     INGSLAISNP PTPKADAYSF GIIFHEIFTR EGPYKIYVQR GDVNGEAAPK KDSVECRALV
     EKTVRRVYSD PYFRPDTSDL EVQNYVKEVM AACWHHDPYQ RPEFKTIKNK LKPLFHQIYK
     QNIMDHMVLM MEKYQTQLED LVDERTIELK DEQRRSQHLL QRMLPSSVAE QLLAGQDVIP
     EAFPPVTIYF SDIVGFTTIS GESTPMEVVT FLNKLYTLFD SIIRRYDVYK VETIGDAYMV
     VSGVPQYKTM EYHAEQIAMM AIHILSAVRS FSIPHRSCEP LMIRIGMHTG PCVAGVVGKT
     MPRYTLFGDT VNTASRMESN GEALRIHCSS STQKVLTSID QGFLLEERGS LAIKGKGQMT
     TYWLNGRAGY EFTETIEDKM VVPDIFPRPN LKNRGSSWGV NRESSLSLAT EKSSQIMKRQ
     SAAMNRNNQD VIYYNQPLNS GGFTSRGTSN REMPKLYEED RESLLNQSAS LLGSRTSGRK
     KSTASKYNGF SASRMFSSTI SNASSSRPSR PSTFDHDTLA LRKRSTSLPD GEKLNLEFIE
     TTNLANNSVP AIPNNISSLE PVFRKASIID GYSSQSESPS QSQYPSYRDL TTGPHQRKRG
     IATVFPVRKR SLSCGDAVPL KINENGASGS ITTAVSPRSS CRALDPTMKL AARASSPDEI
     IFQEDDEDAL IDNDSLLTSN GNSKSEDVLR TCPQPRRKNK HSFLRDPSPL AKRFRDASPF
     GKKKPFWNSN KSNEHTSSPA DSISRLFRRF RGGSVNEYAD LNHYCDDEDE SGRANGYEMQ
     EMGKMTGRQR EQRNGSRTNR SVSCSPDECG TLTDSSDPHL TIPSSSIGDS SASTSLSCS
 
 
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