GCYB_PLABA
ID GCYB_PLABA Reviewed; 3004 AA.
AC A0A509APX1; A0MJN0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Guanylate cyclase beta {ECO:0000303|PubMed:17030505};
DE Short=PfGCbeta {ECO:0000303|PubMed:17030505};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q8IDA0};
DE AltName: Full=Guanylyl cyclase beta {ECO:0000305};
GN Name=GCbeta {ECO:0000303|PubMed:17030505};
GN ORFNames=PBANKA_1136700 {ECO:0000312|EMBL:VUC56788.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN [1] {ECO:0000312|EMBL:ABJ90483.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17030505; DOI=10.1093/jb/mvj205;
RA Hirai M., Arai M., Kawai S., Matsuoka H.;
RT "PbGCbeta is essential for Plasmodium ookinete motility to invade midgut
RT cell and for successful completion of parasite life cycle in mosquitoes.";
RL J. Biochem. 140:747-757(2006).
RN [2] {ECO:0000312|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
RN [3] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19779564; DOI=10.1371/journal.ppat.1000599;
RA Moon R.W., Taylor C.J., Bex C., Schepers R., Goulding D., Janse C.J.,
RA Waters A.P., Baker D.A., Billker O.;
RT "A cyclic GMP signalling module that regulates gliding motility in a
RT malaria parasite.";
RL PLoS Pathog. 5:e1000599-e1000599(2009).
CC -!- FUNCTION: Catalyzes the synthesis of the second messenger cGMP from GTP
CC (By similarity). Probably by regulating cGMP production, required for
CC ookinete gliding motility, which is necessary for the ookinete to
CC traverse the midgut epithelium of the mosquito (PubMed:17030505,
CC PubMed:19779564). {ECO:0000250|UniProtKB:Q8IDA0,
CC ECO:0000269|PubMed:17030505, ECO:0000269|PubMed:19779564}.
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:0000250|UniProtKB:Q8IDA0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8IDA0};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8IDA0};
CC Note=Binds 2 magnesium ions per subunit (By similarity). Is also active
CC with manganese (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P30803, ECO:0000250|UniProtKB:Q8IDA0};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: During the blood stage, specifically expressed in
CC gametocytes. {ECO:0000269|PubMed:19779564}.
CC -!- DOMAIN: The N-terminus contains a P-type ATPase-like domain which is
CC required for guanylate cyclase activity.
CC {ECO:0000250|UniProtKB:Q8IDA0}.
CC -!- DISRUPTION PHENOTYPE: In the mosquito, ookinetes have severe defect in
CC motility and their ability to traverse the midgut epithelium is
CC impaired resulting in complete developmental arrest (PubMed:17030505,
CC PubMed:19779564). Normal development of gametocytes, normal
CC exflagellation and fertilization, and normal development of zygote into
CC ookinete (PubMed:19779564). {ECO:0000269|PubMed:17030505,
CC ECO:0000269|PubMed:19779564}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cation transport
CC ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the adenylyl cyclase
CC class-4/guanylyl cyclase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABJ90483.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ904399; ABJ90483.1; ALT_SEQ; Genomic_DNA.
DR EMBL; LK023126; VUC56788.1; -; Genomic_DNA.
DR STRING; 5823.A0A509APX1; -.
DR VEuPathDB; PlasmoDB:PBANKA_1136700; -.
DR OMA; NNNKYHH; -.
DR Proteomes; UP000074855; Chromosome 11.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:UniProtKB.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 2: Evidence at transcript level;
KW cGMP biosynthesis; Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..3004
FT /note="Guanylate cyclase beta"
FT /id="PRO_0000452807"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..94
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..334
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1013..1022
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1023..1043
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1044..1072
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1073..1093
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1094..1105
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1127..1130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1131..1151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1152..1171
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1172..1192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1193..1297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1298..1318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1319..1327
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1328..1348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1349..1353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1354..1374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1375..1394
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1395..1415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1416..1457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1458..1478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1479..1500
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1501..1521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1522..2563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2564..2584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2585..2594
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2595..2615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2616..2634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2635..2655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2656..2667
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2668..2688
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 2689..2695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2696..2716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2717..2722
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2723..2743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2744..3004
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 1541..1696
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 2793..2927
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 2463..2491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2463..2480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2798
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 2798
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 2799
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 2842
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 2842
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 3004 AA; 354776 MW; E9115F60FC54BF93 CRC64;
MKETDKIKSE VLNLMQLDGK REHINKNNKL YRKVIINPTS EDDLQKFCKN YFRIYQFSLY
NFIRRLISLD AVIVYTLFMT VYIFSEISQG ITKKYLFVDT AISLFLNIGI LVVIESLFEL
KLLKDIKNAN SQHYLRIVPK MSYFEKVMTK DIKVGNIIRV FQGEEFPADV VILYSKKNTN
AVVDSFKIDG LYNKSIKYPV EKYKIDRDYL KMLSEINGVI KCELPNKNVF CFQGTYKLDK
HPRSLHLSYE NFALQSSILK GAEYIDGVVV YTGADTKKNL NIPRKIEENM TFCIKMNNVV
YYLIFMYILF VLLSIIIKAI FYRKGKLLEN SNDTFFTVLE DFIGLYILVL PVMLYSEKSL
IYIIQSLKIE RDTRMNKDEN SNNTKVFNKN KNDALGTVDI IATARNGVLV NKKEILVSCT
INNVLYSKKK FIISDEFLKL PSLNILDAER TNVSELLNLD ERIFKDPENI FFPSRDFNNF
LKILGNNTNP IYDPINGDFS KILKEIYRNY LNEEFLYKKI KLSSSVKSLL DNGYNQFLED
CESSYDCKEI IEDGLKNNEQ SEKIEEFILG ICACNRIIIY NEKFGDIEMK DNINEKSTSE
HMNYDKDREV ENIESENKYA VDSDGEENMN TIEHEDICLF NTSKNIGFHI YCYKKCLFFY
NLKNICKEYY IICFHDFLRS NNYTMCILKN KKELDKGILY IRGYDFNILP YLCKNKNDIN
KIKKTIKIHT ANYLKVILIC KKNITNEDIA KYIYLKSVRS KFSFKFFDII KTFFLYDLEC
IGIIGLKNDL NDGVVETFND INNFDIRSWI FTNDSSKNTY LTALQCNLIT PNSNLFIINF
LNPDHSDEET VANYLFNNFL FSMENMKSRS YAIAINEMSL KNIMRSRYAL KVFLCIIMRA
TVVLFCKLNN ETKGKIISKF LSYTTPKLTV LGVGSTLNDA YLLKNTTISV CLTLNKQVNA
LYSISDYAME EFKYVGELLI LGRLNRFSLC RAFLWIIYLK VMIGSFYFFH NFDNFFSGSS
ISSILYSQTA FAIFHYSLIV AFASYEIDIP YKFIRNFPYI YQLARRKYFL NNTIIFLNIV
ESIFSSFISY YILRGNLFNL ITHRKFTFHI FVLNFFLISE KILLFSKTWH IFFFIMTIII
VSILFIYINI YTLVDCLITG KCEFSLFDPE DSYFWISLLP ILYINFIIDK FMKFVKNKIY
PDITYHLSNT LKIETQEKFA TNNKREEVIT DKNIEKLAPV PKSYIIKEDN AYYGKSKKNK
YIFDTLRKII DIKIKYRNQQ LNLEYKTYEK RNKLKLRIII LLLFIIFLIT FTIQIIISKF
IEKKLHSLSY LTVIYYIVAV LYLIKILIRN KTNYTYFYII GKLLLVIGYL LEISENSVNN
IINMLVTYSF TVCYIFFISF KILEGLVMCI IILSIAIWVY YHKNNNLNAM CTDFCDNPYT
SLDNLEYINI SCICKQQIFT FLICTLSFTL ICLFMKYYEI YYLKKKFLTR YKQKVNLGKQ
IEILHTMLPS FLVEYLLVSD PKADGIMVGK NISGEDRGII SVIFCDIDDF QTMVSTLEPH
TLVQTLDNLY LYFDKCIKYF NCIKIETVFE SYLAASGLSE KKNNCVHKIK YDTKCAIKMA
IAQLSAKYYI SYKVLDTLSN NKDSNSIFPI ESKYIYKNIS LRIGIHTGKA ISGVIGSVKP
QYSLFGDTVN TASRMKSTSL KDHIHVSYDT YKYLKDDKTL VWKERSIFIK GKGEMKTYLL
VDILDNSKKD HTKALEESTS SIFRSNDEIV NKSELITKEK EFDKIEMPDK SEIIDETKKI
FKKSEKPSTK KKKIKKENAK EKNINIKMKE MGEILNNYDK EKVYNCNKSD DGSNSIGQND
FLYSTKNYNY KKSKYLDLER LSTNKSFRRN VLAYNFESPI NLPPKIGDNT KRNYDSDNFF
TSPYIIDKNE KDEIRDTTNK ALYIKKSKNI INRMREDSID FKDEFSKEND KIKEYIKERI
TYRQKVTPNY FNFNNMSKYS NAFKKKKKKK KDIQKKYTYR QKTSFYNFLN KNDIINYNYS
SEFEYFIDPK MKNKKPINFN NLFAKIYKKK LSLLNIKNEP INIKKKNIKN KSRDRIIFSS
RRDEEHDDNQ KMNKKLFSRT YAQKAEQTSH ENIFTEMIND NFLKKEDKEQ CEIRNENRCP
TVFLIKRNKT TININKNRVL KRIFKDIITR KKIKRNRILK NKKLNYVNKN DNLGKKYEIL
NNICLVHKRA MTFVQYNTED EEKKRTKRFH KNDEIFGSDM NISRNLNGSN SNIQNINRRS
KNKAEDDLFI RNKVNLNNIK NNINLRKNIY KTDERGMQYN DLKGYDKKKN TEENNEDKEK
KIEYDSNENI KNGFPKNEDK MIMKKRMISK RISFYSLKEY EKGDSFKSYD NSSCGIKSKK
TNSIISDEEM NEYFNYNTEF NSNRNKNKQN KEFSLASKVN NIFKNIFKKN YISDKLKSGK
YNTMSNSKSG QTNITTDNKK SQIKKNGDVN KANTNVSNKN SDFVTNFDNY NKNILKKLTS
TLQINRKTSY FNRFYYKFKD EELEEEYTRE YYQEIINIDL TKKLIIIFVI SELILSLCNV
IELSYYENKE TPNDFIVIIW LIRSIYLFTI TFIWLLLKTK LKEYKDNSSK MMWTTFILNI
FLSSWGIIMI DLACIHYSNL VGNSRERSIF FMKDATELII SMQLIFVKNM LFKHKFFFFV
FFFVFLMYSF FKLFVIHVCE LRICCSILLI LSINILYFWY SEYLDRTQYI IKRKRNRMER
TSHDFLTRIL PRQVLEEYQN DNLQLTYKHE KIAFLFADIV GFTKWSKTAA PKNVLKLLQK
LISKIDKDTI KLGLYKLFTI GDAYVATSQP NASITDQTEA ADGIISIFKL AKLILHNINT
IKIQFNKHDF NMRIGLHYGS CVGGIIGSVR IRYDMWGLDV LIANHIESNG IPGEIVCSEQ
FKNFFLENEP HAKLNFWHYK TISINDKDIK IYVVEDKNYE EDYDPKIINY ETLLKLREQN
KVKG
