TSP12_CAEEL
ID TSP12_CAEEL Reviewed; 308 AA.
AC Q22495;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Tetraspanin-12 {ECO:0000305};
GN Name=tsp-12 {ECO:0000312|WormBase:T14G10.6};
GN ORFNames=T14G10.6 {ECO:0000312|WormBase:T14G10.6};
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, INTERACTION WITH SUP-17, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, 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-14, 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). May regulate BMP-like Sma/Mab
CC signaling by mediating protease sup-17 trafficking to the cell surface
CC (PubMed:28068334). Together with tsp-14, probably acts by modulating
CC the activation of glp-1, a Notch-like receptor, to regulate germline
CC maturation (PubMed:20220101). Probably acts by modulating the
CC activation of lin-12, a Notch-like receptor, to regulate cell fate
CC specification such as the anchor cell/ventral uterine precursor cell
CC decision (PubMed:20220101). {ECO:0000269|PubMed:20220101,
CC ECO:0000269|PubMed:25978409, ECO:0000269|PubMed:28068334}.
CC -!- SUBUNIT: May interact with protease sup-17; the interaction promotes
CC sup-17 cell membrane localization. {ECO:0000269|PubMed:28068334}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28068334};
CC Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}.
CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:28068334}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline.
CC {ECO:0000269|PubMed:28068334}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and in adults.
CC Expressed in the developing vulva at the L4 larval stage and in the
CC hypodermis at the L3 larval stage. {ECO:0000269|PubMed:28068334}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:28068334). In embryos,
CC loss of protease sup-17 cell membrane localization (PubMed:28068334).
CC In a tsp-14 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-14 mutant background, restores the production of the 2 M lineage-
CC derived coelomocytes (PubMed:28068334). In a glp-1 (ar202) mutant
CC background, partially restores normal fertility (PubMed:20220101). In a
CC glp-1 (e2142) mutant background, enhances embryonic lethality
CC (PubMed:20220101). In a sup-17 (n1258) or adm-4 (ok265) mutant
CC background, causes lethality at various developmental stages
CC (PubMed:20220101). In a lin-12 (n302) mutant background, restores egg-
CC laying function (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; BX284604; CAA93092.1; -; Genomic_DNA.
DR PIR; T24912; T24912.
DR RefSeq; NP_501853.1; NM_069452.4.
DR AlphaFoldDB; Q22495; -.
DR SMR; Q22495; -.
DR IntAct; Q22495; 1.
DR STRING; 6239.T14G10.6; -.
DR PaxDb; Q22495; -.
DR EnsemblMetazoa; T14G10.6.1; T14G10.6.1; WBGene00006638.
DR GeneID; 177890; -.
DR KEGG; cel:CELE_T14G10.6; -.
DR UCSC; T14G10.6; c. elegans.
DR CTD; 177890; -.
DR WormBase; T14G10.6; CE06452; WBGene00006638; tsp-12.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000168794; -.
DR HOGENOM; CLU_055524_0_0_1; -.
DR InParanoid; Q22495; -.
DR OMA; SRKHHHF; -.
DR OrthoDB; 1180379at2759; -.
DR PhylomeDB; Q22495; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q22495; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006638; Expressed in embryo and 4 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
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: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:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
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..308
FT /note="Tetraspanin-12"
FT /id="PRO_0000441400"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..86
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..268
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 308 AA; 34658 MW; E37221DDD2ADE78E CRC64;
MANRRQPVQH RAQQRVYRQS QIRYAPGAGG ESEISCCVKY SVFSFNVIFF LLGFGLLLFG
VWAQIEKNTF VNMLSKASKL YLDPTWPLLI VGFLTFIIGF SGCVGSLREN TSFLTFYSTL
LGLLLIAEFS AGVFAYACRD QLDNYIRNLL NDVVVGYRDD PDLQLLIDSM QETWMCCGIN
GADDWDRNTY FSIEAREVAS PEAGGVPFSC CINSSKLEFK NYFCGHGVRL KPESHMAAHL
AAQRVMAHTA SIYTEGCLPK LQLWLNNNML LVAVSMVIIA IIQVLGICFA QNLKSDILAQ
RAKWYYTH