TSP14_CAEEL
ID TSP14_CAEEL Reviewed; 451 AA.
AC H2L006; O44582;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Tetraspanin-14 {ECO:0000305};
GN Name=tsp-14 {ECO:0000312|WormBase:F39C12.3b};
GN ORFNames=F39C12.3 {ECO:0000312|WormBase:F39C12.3b};
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, AND DISRUPTION PHENOTYPE.
RX PubMed=20220101; DOI=10.1073/pnas.1001647107;
RA Dunn C.D., Sulis M.L., Ferrando A.A., Greenwald I.;
RT "A conserved tetraspanin subfamily promotes Notch signaling in
RT Caenorhabditis elegans and in human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5907-5912(2010).
RN [3] {ECO:0000305}
RP FUNCTION.
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).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28068334; DOI=10.1371/journal.pgen.1006568;
RA Wang L., Liu Z., Shi H., Liu J.;
RT "Two paralogous tetraspanins TSP-12 and TSP-14 function with the ADAM10
RT metalloprotease SUP-17 to promote BMP signaling in caenorhabditis
RT elegans.";
RL PLoS Genet. 13:E1006568-E1006568(2017).
CC -!- FUNCTION: Together with tsp-12, regulates cell fate specification in
CC the postembryonic mesodermal M lineage, body size and male development,
CC probably by positively modulating BMP-like Sma/Mab signaling
CC (PubMed:25978409, PubMed:28068334). Together with tsp-12, probably acts
CC by modulating the activation of glp-1, Notch-like receptor, to regulate
CC germline maturation (PubMed:20220101). {ECO:0000269|PubMed:20220101,
CC ECO:0000269|PubMed:25978409, ECO:0000269|PubMed:28068334}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|RuleBase:RU361218}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:F39C12.3b};
CC IsoId=H2L006-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F39C12.3a};
CC IsoId=H2L006-2; Sequence=VSP_059065;
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:28068334). No effect
CC on sup-17 localization in embryos (PubMed:28068334). In a tsp-12
CC (ok236) mutant background, exhibits vulva morphogenesis defects,
CC impaired egg-laying, smaller body size and reduced RAD-SMAD reporter
CC expression, a reporter system for the sma-6/daf-4 BMP-like pathway
CC (PubMed:28068334). Males have severe tail defects including crumpled
CC spicules, fused and shortened sensory rays and smaller fans
CC (PubMed:28068334). F1 progeny die at the late embryonic stage with
CC defects in ventral enclosure (PubMed:28068334). In a sma-9 (cc604) and
CC tsp-12 (ok236) mutant background, restores the production of the 2 M
CC lineage-derived coelomocytes (PubMed:28068334). In a glp-1 (ar202)
CC mutant background, partially restores normal fertility
CC (PubMed:20220101). {ECO:0000269|PubMed:20220101,
CC ECO:0000269|PubMed:28068334}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU361218}.
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DR EMBL; BX284606; CCD70847.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD70848.1; -; Genomic_DNA.
DR PIR; T32652; T32652.
DR RefSeq; NP_508828.1; NM_076427.5.
DR RefSeq; NP_508829.1; NM_076428.3.
DR AlphaFoldDB; H2L006; -.
DR SMR; H2L006; -.
DR STRING; 6239.F39C12.3b; -.
DR PaxDb; H2L006; -.
DR EnsemblMetazoa; F39C12.3a.1; F39C12.3a.1; WBGene00006640. [H2L006-2]
DR EnsemblMetazoa; F39C12.3a.2; F39C12.3a.2; WBGene00006640. [H2L006-2]
DR EnsemblMetazoa; F39C12.3a.3; F39C12.3a.3; WBGene00006640. [H2L006-2]
DR EnsemblMetazoa; F39C12.3b.1; F39C12.3b.1; WBGene00006640. [H2L006-1]
DR UCSC; F39C12.3b; c. elegans.
DR WormBase; F39C12.3a; CE10096; WBGene00006640; tsp-14. [H2L006-2]
DR WormBase; F39C12.3b; CE29315; WBGene00006640; tsp-14. [H2L006-1]
DR eggNOG; KOG3882; Eukaryota.
DR InParanoid; H2L006; -.
DR OMA; KNYHTNR; -.
DR OrthoDB; 804962at2759; -.
DR PhylomeDB; H2L006; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:H2L006; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006640; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IGI:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; IGI:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IGI:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IGI:UniProtKB.
DR GO; GO:0040026; P:positive regulation of vulval development; IGI: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; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR SUPFAM; SSF48652; SSF48652; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..451
FT /note="Tetraspanin-14"
FT /id="PRO_0000441401"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..96
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..285
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 328..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_059065"
SQ SEQUENCE 451 AA; 50451 MW; 3219A4019193CD87 CRC64;
MPHRAPRRFM KTAPGACDWE QCLLMGSGEP TRARAVVSSS HKQRKPRQEI SACLKWLVFL
LNSIVFLVGV GILALGVYLF IKDFREVKLV DIILNPAILI SIFGFSICVV SFFGFMGALR
DNIFLLKCFA ACVFLSYILV VAVTLVFFTL FYTDTTEGLS ANWLLLYAVK NYHTNRNLAE
IMDALQENLE CCGVSSIAQG YRDWNMSYQF NCTNSNPQPE KCGVPFSCCR KSVISEAAGS
SNPLLPAMRS LECWQNALTK RPGDLEHDIY TRGCLQPLRT LFESHAVHVG AFVALLIVPV
CISVCLTNIL AKQVDHQRYL LEREARRNDR RRKRDHNRRD QLNSLDLLEE GKFNNASANA
TRPRPPDIPP PLPPIEHVPR KKSRNASSSP TRKPKSAGVE NAAARRKRTA TTTRTPPAAA
GPAPTPQATT TNRTHQWVLQ QTDLVPQKSK S
