TSN15_CAEEL
ID TSN15_CAEEL Reviewed; 258 AA.
AC Q9XVM9;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Tetraspanin-15 {ECO:0000312|WormBase:F53B6.1};
GN Name=tsp-15 {ECO:0000312|WormBase:F53B6.1};
GN ORFNames=F53B6.1 {ECO:0000312|WormBase:F53B6.1};
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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15454573; DOI=10.1242/jcs.01403;
RA Moribe H., Yochem J., Yamada H., Tabuse Y., Fujimoto T., Mekada E.;
RT "Tetraspanin protein (TSP-15) is required for epidermal integrity in
RT Caenorhabditis elegans.";
RL J. Cell Sci. 117:5209-5220(2004).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DOXA-1 AND BLI-3, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23028364; DOI=10.1371/journal.pgen.1002957;
RA Moribe H., Konakawa R., Koga D., Ushiki T., Nakamura K., Mekada E.;
RT "Tetraspanin is required for generation of reactive oxygen species by the
RT dual oxidase system in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002957-E1002957(2012).
RN [4] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-249.
RX PubMed=25480962; DOI=10.1534/g3.114.015982;
RA Xu Z., Luo J., Li Y., Ma L.;
RT "The BLI-3/TSP-15/DOXA-1 dual oxidase complex is required for iodide
RT toxicity in Caenorhabditis elegans.";
RL G3 (Bethesda) 5:195-203(2015).
CC -!- FUNCTION: Plays a role in cuticle biogenesis (PubMed:15454573,
CC PubMed:23028364, PubMed:25480962). In complex with doxa-1 and the dual
CC oxidase bli-3, promotes the generation of reactive oxygen species (ROS)
CC and tyrosine cross-linking of collagen, thus stabilizing cuticular
CC extracellular matrix (PubMed:23028364). {ECO:0000269|PubMed:15454573,
CC ECO:0000269|PubMed:23028364, ECO:0000269|PubMed:25480962}.
CC -!- SUBUNIT: Interacts with doxa-1 and bli-3.
CC {ECO:0000269|PubMed:23028364}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the body wall (hyp7 hypodermal
CC syncitium), pharynx and vulva. Expressed in a punctate pattern along
CC the thick region of the hypodermis. {ECO:0000269|PubMed:15454573}.
CC -!- DEVELOPMENTAL STAGE: Expressed in cells along the anteroposterior axis
CC from the 1.5-fold stage of embryogenesis until the 3-fold stage when
CC expression decreases but increases in the body surface with prominent
CC expression in the lateral hypodermal cells (PubMed:23028364,
CC PubMed:15454573). Expressed in the pharynx and body wall from the
CC larval stage to adulthood. {ECO:0000269|PubMed:15454573,
CC ECO:0000269|PubMed:23028364}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal (PubMed:23028364). Mutants
CC display dumpy and blistered cuticle phenotypes (PubMed:23028364).
CC Blisters contain unidentified cellular material (PubMed:23028364,
CC PubMed:25480962). Resistant to iodide toxicity (PubMed:25480962). RNAi-
CC mediated knockdown results in the lethality of more than 95% of progeny
CC at the larval stage (PubMed:15454573). Most larval arrest occurs at the
CC L4 larval stage and is characterized by body swelling and abnormal
CC epidermal morphology, which includes blistering of the cuticle
CC (PubMed:15454573, PubMed:25480962). The few animals that develop into
CC adults have a distended body shape and/or epidermal blistering
CC (PubMed:15454573). Abnormal cuticular and hypodermal morphology
CC including splits in the cortical layer of the cuticle, abnormal gaps
CC between the hypodermis and musculature and inconsistent thickness of
CC the hypodermis (PubMed:15454573, PubMed:25480962). Impaired hypodermal
CC membrane integrity and reduced fibrous organelles (PubMed:15454573).
CC {ECO:0000269|PubMed:15454573, ECO:0000269|PubMed:23028364,
CC ECO:0000269|PubMed:25480962}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; BX284601; CAB03120.2; -; Genomic_DNA.
DR PIR; T22544; T22544.
DR RefSeq; NP_492404.1; NM_060003.5.
DR AlphaFoldDB; Q9XVM9; -.
DR ComplexPortal; CPX-1020; BLI-3/DOXA-1/TSP-15 dual oxidase complex.
DR STRING; 6239.F53B6.1; -.
DR EPD; Q9XVM9; -.
DR PaxDb; Q9XVM9; -.
DR PeptideAtlas; Q9XVM9; -.
DR EnsemblMetazoa; F53B6.1.1; F53B6.1.1; WBGene00006641.
DR GeneID; 192065; -.
DR KEGG; cel:CELE_F53B6.1; -.
DR UCSC; F53B6.1; c. elegans.
DR CTD; 192065; -.
DR WormBase; F53B6.1; CE26464; WBGene00006641; tsp-15.
DR eggNOG; KOG3882; Eukaryota.
DR HOGENOM; CLU_105183_0_0_1; -.
DR InParanoid; Q9XVM9; -.
DR OMA; IWKTSKW; -.
DR OrthoDB; 1051357at2759; -.
DR PhylomeDB; Q9XVM9; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q9XVM9; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006641; Expressed in larva and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:1990204; C:oxidoreductase complex; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IDA:ComplexPortal.
DR GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
DR GO; GO:0098773; P:skin epidermis development; IMP:WormBase.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR SUPFAM; SSF48652; SSF48652; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..258
FT /note="Tetraspanin-15"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433623"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..62
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..223
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MUTAGEN 249
FT /note="G->R: In mac33; blistered cuticle phenotype with
FT blisters containing cellular material. Resistant to iodide
FT toxicity."
FT /evidence="ECO:0000269|PubMed:25480962"
SQ SEQUENCE 258 AA; 29028 MW; 863F01C3C928916D CRC64;
MGALGDSAYG ARGRLIKFSY IVTALISILF SISCICYGIW LLARRSQYAE LVSPSLYVDV
GRILVIISIL SILNYLICFY AIFKEMRCFV TSCAVASIVI AVMLIIGGCI GLNFRDQLTH
YTPLNLKMLT SLRELYGTHD MKGITESWDA LQSNFKCCGV NGTDNAQIWK TSKWYMHQRA
PKLLIPESCC IPSEIERCRS NPFDQDAPPP YYTSTCYEPL QNDLLHVMNV ASWLCITNAI
VQIIPSVAGC WYSKLIRK
