ID   GBB_PINFU               Reviewed;         341 AA.
AC   Q5GIS3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Guanine nucleotide-binding protein subunit beta {ECO:0000250|UniProtKB:P23232};
DE            Short=pfGbeta1 {ECO:0000303|PubMed:16054410};
DE   AltName: Full=G protein subunit beta-1;
OS   Pinctada fucata (Akoya pearl oyster) (Pinctada imbricata fucata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=50426;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAS90835.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF 49-ARG-ARG-50 AND 49-ARG--LEU-52.
RC   TISSUE=Mantle {ECO:0000269|PubMed:16054410};
RX   PubMed=16054410; DOI=10.1016/j.cbpc.2005.02.013;
RA   Chen L., Xie L., Xiong X., Dai Y., Fan W., Zhang R.;
RT   "Cloning and characterization of a novel G protein beta-subunit of pearl
RT   oyster (Pinctada fucata), and its interaction sites with calmodulin.";
RL   Comp. Biochem. Physiol. 142:142-152(2005).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as a modulator or transducer in various transmembrane signaling
CC       systems. The beta and gamma chains are required for the GTPase
CC       activity, for replacement of GDP by GTP, and for G protein-effector
CC       interaction. {ECO:0000305}.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. The
CC       G protein beta1-gamma2 dimer interacts with calmodulin.
CC       {ECO:0000269|PubMed:16054410, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16054410}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in gills, gonad and mantle and
CC       at lower levels in digestion gland. Not detected in muscle.
CC       {ECO:0000269|PubMed:16054410}.
CC   -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC       {ECO:0000255}.
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DR   EMBL; AY524667; AAS90835.1; -; mRNA.
DR   AlphaFoldDB; Q5GIS3; -.
DR   SMR; Q5GIS3; -.
DR   PRIDE; Q5GIS3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR001632; Gprotein_B.
DR   InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR19850; PTHR19850; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00319; GPROTEINB.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Cytoplasm; Repeat; Transducer; WD repeat.
FT   CHAIN           1..341
FT                   /note="Guanine nucleotide-binding protein subunit beta"
FT                   /id="PRO_0000407915"
FT   REPEAT          54..93
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          96..135
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          142..180
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          183..222
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          225..264
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          269..308
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          311..341
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         49..52
FT                   /note="Missing: Greatly reduces beta1-gamma2 binding
FT                   affinity for calmodulin."
FT                   /evidence="ECO:0000269|PubMed:16054410"
FT   MUTAGEN         49..50
FT                   /note="RR->AA: Greatly reduces beta1-gamma2 binding
FT                   affinity for calmodulin."
FT                   /evidence="ECO:0000269|PubMed:16054410"
SQ   SEQUENCE   341 AA;  37499 MW;  A0829427C5602F6F CRC64;
     MSSELEALRQ ETEQLKNQIR EARKAAADTT LNQAAVNVEQ VGRIQMRTRR TLRGHLAKIY
     AMHWASDSRN LVSASQDGKL IVWDGYTTNK VHAIPLRSSW VMTCAYAPSG SYVACGGLDN
     ICSIYSLKTR EGNVRVSREL PGHTGYLSCC RFLDDNQIVT SSGDMSCALW DIETGQQTTA
     FTGHTGDVMS LSLSPDMRTF VSGACDASAK LWDIRDGMCK QTFSGHESDI NAITYFPNGY
     AFATGSDDAT CRLFDIRADQ EIGMYSHDNI ICGITSVAFS KSGRLLLGGY DDFNCNVWDV
     LRQERAGVLA GHDNRVSCLG VTEDGMAVAT GSWDSFLRIW N