GPCRDB: Swiss-Prot entry

ID   GPA4_CAEEL     STANDARD;      PRT;   358 AA.
AC   Q9BIG5; O44409;
DT   28-FEB-2003 (Rel. 41, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Guanine nucleotide-binding protein alpha-4 subunit.
GN   Name=gpa-4; ORFNames=T07A9.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; 
OC   Rhabditidae; Peloderinae; Caenorhabditis. 
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol N2;
RA   Cuppen E., Jansen G., Plasterk R.H.A.;
RT   "Interaction analysis of the complete G-alpha subfamily of
RT   heterotrimeric G proteins from Caenorhabditis elegans.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan];
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   SEQUENCE REVISION.
RG   WormBase consortium;
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AY008127; AAG32080.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; AF036706; AAK39279.2; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; T32578; T32578.
DR   HSSP; P04896; 1AZT. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   Ensembl; T07A9.7; Caenorhabditis_elegans
DR   WormBase; WBGene00001666; gpa-4.
DR   WormPep; T07A9.7; CE31599. [WormPep / WormBase / WorfDB]
DR   InterPro; IPR001019; Gprotein_alpha.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00503; G-alpha; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   ProDom; PD000281; Gprotein_alpha; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   SMART; SM00275; G_alpha; 1.
DR   CMR; Q9BIG5.
DR   BLOCKS; Q9BIG5.
DR   ProtoNet; Q9BIG5.
DR   ProtoMap; Q9BIG5.
DR   PRESAGE; Q9BIG5.
DR   DIP; Q9BIG5.
DR   ModBase; Q9BIG5.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   GTP-binding; Lipoprotein; Multigene family; Myristate; Palmitate;
KW   Transducer.
FT   INIT_MET      0      0       By similarity.
FT   LIPID         1      1       N-myristoyl glycine (By similarity).
FT   LIPID         2      2       S-palmitoyl cysteine (By similarity).
SQ   SEQUENCE   358 AA;  41540 MW;  9390547E29E2D3DE CRC64;
     GCFHSTGSEA KKRSKLIDEQ LRHDHERCVG EIKLLLLGAG ESGKSTIVRQ MRILHETGFN
     KQEQMAYRPV VFSNMVQSML AILKAMQPLN ISFTDAAREE DARMFISHFL HVNNAELSEA
     FSLELSDLMK QLWMDEGVKK CVKRAHEYQL NDSAEYYFNA LDRISSSSYL PTQDDILRAR
     VKSTGIVETT FMYKDLCFKM FDVGGQRSER KKWIHCFDSV TAVIFCVALS EYDLRLAEDQ
     TMNRMHESMQ LFDSIVNNCW FTETSIILFL NKMDIFEERI RYTPLTVCFP EYQGGMTITE
     TSTFIQSRFE ILNKRQTPAQ KEIYSHFTCA TDTNNIRFVF DAVTDIIIRN NLYLCGLY
//