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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
 
 
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