TSP21_CAEEL
ID TSP21_CAEEL Reviewed; 301 AA.
AC Q5WRN1;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tetraspanin-21 {ECO:0000305};
GN Name=tsp-21 {ECO:0000312|WormBase:C17G1.8};
GN ORFNames=C17G1.8 {ECO:0000312|WormBase:C17G1.8};
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, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-109.
RX PubMed=25978409; DOI=10.1371/journal.pgen.1005221;
RA Liu Z., Shi H., Szymczak L.C., Aydin T., Yun S., Constas K., Schaeffer A.,
RA Ranjan S., Kubba S., Alam E., McMahon D.E., He J., Shwartz N., Tian C.,
RA Plavskin Y., Lindy A., Dad N.A., Sheth S., Amin N.M., Zimmerman S., Liu D.,
RA Schwarz E.M., Smith H., Krause M.W., Liu J.;
RT "Promotion of bone morphogenetic protein signaling by tetraspanins and
RT glycosphingolipids.";
RL PLoS Genet. 11:E1005221-E1005221(2015).
CC -!- FUNCTION: Regulates cell fate specification in the postembryonic
CC mesodermal M lineage and body size, probably by positively modulating
CC BMP-like Sma/Mab signaling at the ligand-receptor level. Promotes
CC ventral fate specification in the M lineage, probably by positively
CC modulating lin-12/Notch signaling. {ECO:0000269|PubMed:25978409}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|RuleBase:RU361218,
CC ECO:0000269|PubMed:25978409}; Multi-pass membrane protein
CC {ECO:0000255|RuleBase:RU361218}. Basolateral cell membrane
CC {ECO:0000269|PubMed:25978409}; Multi-pass membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:25978409}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Specifically localizes to the basolateral side of
CC intestinal cells. Localizes to cytoplasmic vesicles in the M mesoblast.
CC {ECO:0000269|PubMed:25978409}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 100-cell embryonic stage, in the
CC pharynx, intestine, hypodermis and M lineage (M-1 to M-16 stages) at
CC the L1 larval stage and in somatic gonad, vulva and rectal epithelium
CC at the L4 larval stage. {ECO:0000269|PubMed:25978409}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a sma-9 (cc604) mutant
CC background restores the production of the 2 M lineage-derived
CC coelomocytes. {ECO:0000269|PubMed:25978409}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU361218}.
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DR EMBL; BX284606; CAH60758.2; -; Genomic_DNA.
DR RefSeq; NP_001024415.2; NM_001029244.4.
DR AlphaFoldDB; Q5WRN1; -.
DR SMR; Q5WRN1; -.
DR STRING; 6239.C17G1.8; -.
DR EPD; Q5WRN1; -.
DR PaxDb; Q5WRN1; -.
DR PeptideAtlas; Q5WRN1; -.
DR EnsemblMetazoa; C17G1.8.1; C17G1.8.1; WBGene00023491.
DR EnsemblMetazoa; C17G1.8.2; C17G1.8.2; WBGene00023491.
DR GeneID; 259720; -.
DR UCSC; C17G1.8; c. elegans.
DR CTD; 259720; -.
DR WormBase; C17G1.8; CE42559; WBGene00023491; tsp-21.
DR eggNOG; KOG3882; Eukaryota.
DR HOGENOM; CLU_055524_4_3_1; -.
DR InParanoid; Q5WRN1; -.
DR OMA; ADWLYHH; -.
DR OrthoDB; 1224210at2759; -.
DR PhylomeDB; Q5WRN1; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q5WRN1; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00023491; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0042661; P:regulation of mesodermal cell fate specification; IGI:UniProtKB.
DR GO; GO:1901048; P:transforming growth factor beta receptor signaling pathway involved in regulation of multicellular organism growth; IGI:UniProtKB.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR000301; Tetraspanin_animals.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PIRSF; PIRSF002419; Tetraspanin; 1.
DR SUPFAM; SSF48652; SSF48652; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..301
FT /note="Tetraspanin-21"
FT /id="PRO_0000441402"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..59
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..222
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 109
FT /note="G->E: In jj60; in a sma-9 (cc604) mutant background,
FT restores the production of the 2 M lineage-derived
FT coelomocytes."
FT /evidence="ECO:0000269|PubMed:25978409"
SQ SEQUENCE 301 AA; 34408 MW; 3A725BA37C22AFAE CRC64;
MIDLKSIWND KRKITYFFLA NVCFLISGLS SLIVGVWLYS SKNNFIELTP TSYSALSAAG
LCVFTGVTIF IIVAVGYLGV SWSNKSLLYS YIGFVILLIL VHGIARITGS LHKEEAKENL
RKSMLHNINT TAVVTKIGRE IKLSLTWDHL QRELQCCGVD NYTDWHYSVH WPNNLYTPDS
CCDPQHFDAE NGTENCGKLP DEQSLLYQKG CFPKFSDWLY HHIILVNWVT SILFVVEILL
LILSLVVLRV LKNSRHKTRR SHRERDPETT SENMRLNSMD RIADARLETD TVEDGMSINS
R
