TSN15_MOUSE
ID TSN15_MOUSE Reviewed; 294 AA.
AC F7BWT7; C0H5X1; Q3TA07;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Tetraspanin-15;
DE Short=Tspan-15;
DE AltName: Full=Transmembrane 4 superfamily member 15;
GN Name=Tspan15;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND INTERACTION WITH ADAM10.
RX PubMed=23035126; DOI=10.1074/jbc.m112.416503;
RA Haining E.J., Yang J., Bailey R.L., Khan K., Collier R., Tsai S.,
RA Watson S.P., Frampton J., Garcia P., Tomlinson M.G.;
RT "The TspanC8 subgroup of tetraspanins interacts with A disintegrin and
RT metalloprotease 10 (ADAM10) and regulates its maturation and cell surface
RT expression.";
RL J. Biol. Chem. 287:39753-39765(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH ADAM10.
RX PubMed=26668317; DOI=10.1074/jbc.m115.703058;
RA Noy P.J., Yang J., Reyat J.S., Matthews A.L., Charlton A.E., Furmston J.,
RA Rogers D.A., Rainger G.E., Tomlinson M.G.;
RT "TspanC8 tetraspanins and A disintegrin and metalloprotease 10 (ADAM10)
RT interact via their extracellular regions: evidence for distinct binding
RT mechanisms for different TspanC8 proteins.";
RL J. Biol. Chem. 291:3145-3157(2016).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=30463011; DOI=10.1016/j.celrep.2018.10.088;
RA Shah J., Rouaud F., Guerrera D., Vasileva E., Popov L.M., Kelley W.L.,
RA Rubinstein E., Carette J.E., Amieva M.R., Citi S.;
RT "A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
RT Promote alpha-Toxin Cytotoxicity.";
RL Cell Rep. 25:2132-2147(2018).
CC -!- FUNCTION: Regulates maturation and trafficking of the transmembrane
CC metalloprotease ADAM10 (PubMed:23035126, PubMed:26668317). Promotes
CC ADAM10-mediated cleavage of (CDH2) (PubMed:26668317). Negatively
CC regulates ligand-induced Notch activity probably by regulating ADAM10
CC activity (By similarity). {ECO:0000250|UniProtKB:O95858,
CC ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}.
CC -!- SUBUNIT: Interacts with ADAM10; the interaction influences ADAM10
CC substrate specificity. {ECO:0000269|PubMed:23035126,
CC ECO:0000269|PubMed:26668317}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30463011};
CC Multi-pass membrane protein {ECO:0000305}. Late endosome membrane
CC {ECO:0000250|UniProtKB:O95858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F7BWT7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F7BWT7-2; Sequence=VSP_042389;
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE42863.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK172169; BAE42863.1; ALT_INIT; mRNA.
DR EMBL; AC127417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466553; EDL32110.1; -; Genomic_DNA.
DR EMBL; BC003872; AAH03872.1; -; mRNA.
DR CCDS; CCDS56705.1; -. [F7BWT7-1]
DR RefSeq; NP_932113.2; NM_197996.2. [F7BWT7-1]
DR AlphaFoldDB; F7BWT7; -.
DR SMR; F7BWT7; -.
DR STRING; 10090.ENSMUSP00000047029; -.
DR GlyGen; F7BWT7; 3 sites.
DR iPTMnet; F7BWT7; -.
DR PhosphoSitePlus; F7BWT7; -.
DR SwissPalm; F7BWT7; -.
DR MaxQB; F7BWT7; -.
DR PaxDb; F7BWT7; -.
DR PeptideAtlas; F7BWT7; -.
DR PRIDE; F7BWT7; -.
DR ProteomicsDB; 297721; -. [F7BWT7-1]
DR ProteomicsDB; 297722; -. [F7BWT7-2]
DR Antibodypedia; 28879; 112 antibodies from 21 providers.
DR DNASU; 70423; -.
DR Ensembl; ENSMUST00000047883; ENSMUSP00000047029; ENSMUSG00000037031. [F7BWT7-1]
DR GeneID; 70423; -.
DR KEGG; mmu:70423; -.
DR UCSC; uc007fgv.1; mouse. [F7BWT7-1]
DR CTD; 23555; -.
DR MGI; MGI:1917673; Tspan15.
DR VEuPathDB; HostDB:ENSMUSG00000037031; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157973; -.
DR HOGENOM; CLU_055524_0_1_1; -.
DR InParanoid; F7BWT7; -.
DR OMA; CVRNKTD; -.
DR OrthoDB; 1416189at2759; -.
DR PhylomeDB; F7BWT7; -.
DR TreeFam; TF313002; -.
DR BioGRID-ORCS; 70423; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Tspan15; mouse.
DR PRO; PR:F7BWT7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; F7BWT7; protein.
DR Bgee; ENSMUSG00000037031; Expressed in small intestine Peyer's patch and 185 other tissues.
DR Genevisible; F7BWT7; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0051604; P:protein maturation; IMP: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 Alternative splicing; Cell membrane; Endosome; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..294
FT /note="Tetraspanin-15"
FT /id="PRO_0000415812"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..62
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 191..294
FT /note="TDVVNTMCGYKTIDKERLNAQNIIHVRGCTNAVLIWFMDNYTIMAGLLLGIL
FT LPQFLGVLLTLLYITRVEDIILEHSVTDGLLGPGAKSRTDTAGTGCCLCYPD -> MLS
FT TPCVATKQSTRSA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042389"
FT CONFLICT 199
FT /note="G -> D (in Ref. 1; BAE42863)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="R -> S (in Ref. 1; BAE42863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 33071 MW; BE1BFE47F255B6C8 CRC64;
MPRGDSEQVR YCARFSYLWL KFSLIIYSTV FWLIGGLVLS VGIYAEAERQ KYKTLESAFL
APAIILILLG VVMFIVSFIG VLASLRDNLC LLQSFMYILG ICLVMELIGG IVALIFRNQT
IDFLNDNIRR GIENYYDDLD FKNIMDFVQK KFKCCGGEDY RDWSKNQYHD CSAPGPLACG
VPYTCCIRNT TDVVNTMCGY KTIDKERLNA QNIIHVRGCT NAVLIWFMDN YTIMAGLLLG
ILLPQFLGVL LTLLYITRVE DIILEHSVTD GLLGPGAKSR TDTAGTGCCL CYPD
