SRB13_CAEEL
ID SRB13_CAEEL Reviewed; 345 AA.
AC Q20963;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serpentine receptor class beta-13 {ECO:0000312|WormBase:F58A6.11};
DE Short=Protein srb-13 {ECO:0000305};
GN Name=srb-13 {ECO:0000312|WormBase:F58A6.11};
GN ORFNames=F58A6.11 {ECO:0000312|WormBase:F58A6.11};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
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 that antagonizes the negative
CC effects of the gcy-35 oxygen sensor on spermatogenesis
CC (PubMed:28662030). This leads to the maintenance of mitochondrial
CC function in developing spermatocytes and/or spermatids prior to testis
CC maturation during the early larval stages (PubMed:28662030). Regulates
CC the navigational capacity of sperm during hyperoxic conditions ensuring
CC the proper targeting of sperm derived from males to the fertilization
CC site in the uterus of hermaphrodites (PubMed:28662030). May act in the
CC same signaling pathway as the neuropeptide flp-21 (PubMed:28662030).
CC {ECO:0000269|PubMed:28662030}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:28662030}. Cell
CC projection, dendrite {ECO:0000269|PubMed:28662030}. Note=Detected in
CC ciliated sensory neurons. {ECO:0000269|PubMed:28662030}.
CC -!- TISSUE SPECIFICITY: Expressed in the head sensory neurons ASI, ASK and
CC AWB (PubMed:28662030). Not expressed in male somatic gonads or sperm
CC (PubMed:28662030). {ECO:0000269|PubMed:28662030}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout larval development and
CC adulthood. {ECO:0000269|PubMed:28662030}.
CC -!- DISRUPTION PHENOTYPE: Reduced brood size, which is in part due to an
CC abnormal distribution of male-derived sperm in the hermaphrodite uterus
CC following mating, with sperm reversing course frequently and
CC accumulating at the spermathecal-uterine valve 1 hour following mating
CC (PubMed:28662030). No visible defects in oogenesis (PubMed:28662030).
CC Double knockout with the mcu-1 ju1154 mutant suppresses the sperm
CC navigation defect in the srb-13 single mutant (PubMed:28662030).
CC {ECO:0000269|PubMed:28662030}.
CC -!- SIMILARITY: Belongs to the nematode receptor-like protein srb family.
CC {ECO:0000305}.
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DR EMBL; BX284602; CCD65841.1; -; Genomic_DNA.
DR PIR; T16498; T16498.
DR RefSeq; NP_494958.1; NM_062557.1.
DR AlphaFoldDB; Q20963; -.
DR STRING; 6239.F58A6.11; -.
DR PaxDb; Q20963; -.
DR EnsemblMetazoa; F58A6.11.1; F58A6.11.1; WBGene00019028.
DR GeneID; 3565668; -.
DR KEGG; cel:CELE_F58A6.11; -.
DR UCSC; F58A6.11; c. elegans.
DR CTD; 3565668; -.
DR WormBase; F58A6.11; CE07297; WBGene00019028; srb-13.
DR eggNOG; ENOG502SXP2; Eukaryota.
DR GeneTree; ENSGT00970000195867; -.
DR HOGENOM; CLU_045882_1_0_1; -.
DR InParanoid; Q20963; -.
DR OMA; GVNCAIP; -.
DR OrthoDB; 1145011at2759; -.
DR PhylomeDB; Q20963; -.
DR PRO; PR:Q20963; -.
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-13"
FT /id="PRO_0000447259"
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..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..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"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 345 AA; 39809 MW; 5AF6D824127A299C CRC64;
MAGINQTKCD LGFQITFNTV YRFSQFYTFS VSSFAVPGLI YFMFKRLFQL YFHGNLKTLL
IAYFISILLY AVMLCFAFGY QFFVPFFIKS NCDLIINKTL FKYIHTSVIF LLTTPMMFPL
GFSIERFTAM AMASRYENIR TLIGPVLVIF LIIPNCIIFY FLFQHETYDD TFISFLMLPN
TTAVNFNTYL WFLLYLNIGN LALNVLLLLV HRKFKRRLLL HKTSLSTRYA IEEISQSSKF
TLIITFTHLL FFGCNTICSI LVRVLGEPFF GSFINHSVAR GVNCAVPTYN LVIVVVGFVS
LSKLNSRRQQ EVQTTVQLKT TGKEGARNYD NITANQWATI TQIGF
