SRB5_CAEEL
ID SRB5_CAEEL Reviewed; 345 AA.
AC Q95ZY4;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Serpentine receptor class beta-5;
DE Short=Protein srb-5;
GN Name=srb-5 {ECO:0000312|WormBase:C27D6.6};
GN ORFNames=C27D6.6 {ECO:0000312|WormBase:C27D6.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28662030; DOI=10.1371/journal.pbio.2002047;
RA Hoang H.D., Miller M.A.;
RT "Chemosensory and hyperoxia circuits in C. elegans males influence sperm
RT navigational capacity.";
RL PLoS Biol. 15:E2002047-E2002047(2017).
CC -!- FUNCTION: G-protein coupled receptor (Probable). Plays a role in the
CC navigational capacity of sperm and promotes the targeting of sperm
CC derived from males to the fertilization site in the uterus of
CC hermaphrodites (PubMed:28662030). {ECO:0000269|PubMed:28662030,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:28662030}. Cell
CC projection, dendrite {ECO:0000269|PubMed:28662030}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the head.
CC {ECO:0000269|PubMed:28662030}.
CC -!- SIMILARITY: Belongs to the nematode receptor-like protein srb family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284602; CCD65814.1; -; Genomic_DNA.
DR RefSeq; NP_494961.1; NM_062560.1.
DR AlphaFoldDB; Q95ZY4; -.
DR STRING; 6239.C27D6.6; -.
DR PaxDb; Q95ZY4; -.
DR EnsemblMetazoa; C27D6.6.1; C27D6.6.1; WBGene00005070.
DR GeneID; 191787; -.
DR KEGG; cel:CELE_C27D6.6; -.
DR UCSC; C27D6.6; c. elegans.
DR CTD; 191787; -.
DR WormBase; C27D6.6; CE06886; WBGene00005070; srb-5.
DR eggNOG; ENOG502SXP2; Eukaryota.
DR GeneTree; ENSGT00970000195867; -.
DR HOGENOM; CLU_045882_1_0_1; -.
DR InParanoid; Q95ZY4; -.
DR OMA; LILTFTH; -.
DR OrthoDB; 1136874at2759; -.
DR PhylomeDB; Q95ZY4; -.
DR PRO; PR:Q95ZY4; -.
DR Proteomes; UP000001940; Chromosome II.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IEA:InterPro.
DR InterPro; IPR002184; 7TM_GPCR_serpentine_rcpt_Srb.
DR PANTHER; PTHR31216; PTHR31216; 1.
DR Pfam; PF02175; 7TM_GPCR_Srb; 1.
DR PRINTS; PR00699; TMPROTEINSRB.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..345
FT /note="Serpentine receptor class beta-5"
FT /id="PRO_0000104499"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..103
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 143..163
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..189
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 242..262
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..280
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 281..301
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 345 AA; 39932 MW; 281CCAB91DD7D14F CRC64;
MAEINQTKCD LAFQISYHPI YRLAQFWTLS VSLLAVPSLL YFLLKRVLLL PFHGNLKCLL
ITYFSSIFLY ALVLCFDFSY QCLIPFIVTT KCSLIIDQTL YKCGHMTSLF FLTTPMLLPF
GFSIERFVAV GMAYKYEKMR TLLGPILCFI LVAPNFVVFY FLFRDEQFTD SFISFLVLPN
TPAVQFNNYL WFLLYAKIGN FCCNCVLLIF HKRFKNTYLK KKTSLSVRYA LEEISNSSKF
TLILTFTHLV FFGAYTIGSI LVRTLGESFF GNFLNFYVAR GVNCAVPTYN LLIAFVGLIS
LRQLNSRRHA KILTKVLIRV TGQEGARNYD DIIMQQWNTV SNRTR
