TSN15_HUMAN
ID TSN15_HUMAN Reviewed; 294 AA.
AC O95858; Q6UW79;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Tetraspanin-15;
DE Short=Tspan-15;
DE AltName: Full=Tetraspan NET-7;
DE AltName: Full=Transmembrane 4 superfamily member 15;
GN Name=TSPAN15; Synonyms=NET7, TM4SF15; ORFNames=UNQ677/PRO1311;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rubinstein E., Serru V., Dessen P., Boucheix C.;
RT "New tetraspans identified in the EST database.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [4]
RP FUNCTION, INTERACTION WITH ADAM10, AND SUBCELLULAR LOCATION.
RX PubMed=26686862; DOI=10.1007/s00018-015-2111-z;
RA Jouannet S., Saint-Pol J., Fernandez L., Nguyen V., Charrin S.,
RA Boucheix C., Brou C., Milhiet P.E., Rubinstein E.;
RT "TspanC8 tetraspanins differentially regulate the cleavage of ADAM10
RT substrates, Notch activation and ADAM10 membrane compartmentalization.";
RL Cell. Mol. Life Sci. 73:1895-1915(2016).
RN [5]
RP FUNCTION, AND 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:26686862, PubMed:30463011). Promotes
CC ADAM10-mediated cleavage of CDH2 (By similarity). Negatively regulates
CC ligand-induced Notch activity probably by regulating ADAM10 activity
CC (PubMed:26686862). {ECO:0000250|UniProtKB:F7BWT7,
CC ECO:0000269|PubMed:26686862, ECO:0000269|PubMed:30463011}.
CC -!- SUBUNIT: Interacts with ADAM10; the interaction influences ADAM10
CC substrate specificity. {ECO:0000269|PubMed:26686862}.
CC -!- INTERACTION:
CC O95858; O14672: ADAM10; NbExp=9; IntAct=EBI-7361096, EBI-1536151;
CC O95858; P04921: GYPC; NbExp=3; IntAct=EBI-7361096, EBI-7797098;
CC O95858; P0DN84: STRIT1; NbExp=3; IntAct=EBI-7361096, EBI-12200293;
CC O95858; Q8N205: SYNE4; NbExp=3; IntAct=EBI-7361096, EBI-7131783;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26686862,
CC ECO:0000269|PubMed:30463011}; Multi-pass membrane protein
CC {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:26686862}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; AF120266; AAD17295.1; -; mRNA.
DR EMBL; AY358934; AAQ89293.1; -; mRNA.
DR EMBL; BC003157; AAH03157.1; -; mRNA.
DR EMBL; BC004161; AAH04161.1; -; mRNA.
DR CCDS; CCDS7294.1; -.
DR RefSeq; NP_036471.1; NM_012339.3.
DR PDB; 7RD5; X-ray; 3.60 A; E/F=115-230.
DR PDB; 7RDB; X-ray; 2.52 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=115-230.
DR PDBsum; 7RD5; -.
DR PDBsum; 7RDB; -.
DR AlphaFoldDB; O95858; -.
DR SMR; O95858; -.
DR BioGRID; 117099; 296.
DR IntAct; O95858; 62.
DR MINT; O95858; -.
DR STRING; 9606.ENSP00000362387; -.
DR TCDB; 8.A.40.1.17; the tetraspanin (tetraspanin) family.
DR GlyGen; O95858; 3 sites.
DR iPTMnet; O95858; -.
DR PhosphoSitePlus; O95858; -.
DR SwissPalm; O95858; -.
DR BioMuta; TSPAN15; -.
DR EPD; O95858; -.
DR jPOST; O95858; -.
DR MassIVE; O95858; -.
DR MaxQB; O95858; -.
DR PaxDb; O95858; -.
DR PeptideAtlas; O95858; -.
DR PRIDE; O95858; -.
DR ProteomicsDB; 51091; -.
DR Antibodypedia; 28879; 112 antibodies from 21 providers.
DR DNASU; 23555; -.
DR Ensembl; ENST00000373290.7; ENSP00000362387.2; ENSG00000099282.10.
DR GeneID; 23555; -.
DR KEGG; hsa:23555; -.
DR MANE-Select; ENST00000373290.7; ENSP00000362387.2; NM_012339.5; NP_036471.1.
DR UCSC; uc001jpo.2; human.
DR CTD; 23555; -.
DR DisGeNET; 23555; -.
DR GeneCards; TSPAN15; -.
DR HGNC; HGNC:23298; TSPAN15.
DR HPA; ENSG00000099282; Low tissue specificity.
DR MIM; 613140; gene.
DR neXtProt; NX_O95858; -.
DR OpenTargets; ENSG00000099282; -.
DR PharmGKB; PA128394634; -.
DR VEuPathDB; HostDB:ENSG00000099282; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157973; -.
DR HOGENOM; CLU_055524_0_1_1; -.
DR InParanoid; O95858; -.
DR OMA; CVRNKTD; -.
DR OrthoDB; 1416189at2759; -.
DR PhylomeDB; O95858; -.
DR TreeFam; TF313002; -.
DR PathwayCommons; O95858; -.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; O95858; -.
DR SIGNOR; O95858; -.
DR BioGRID-ORCS; 23555; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; TSPAN15; human.
DR GenomeRNAi; 23555; -.
DR Pharos; O95858; Tbio.
DR PRO; PR:O95858; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O95858; protein.
DR Bgee; ENSG00000099282; Expressed in tibial nerve and 171 other tissues.
DR ExpressionAtlas; O95858; baseline and differential.
DR Genevisible; O95858; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
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 3D-structure; Cell membrane; Endosome; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..294
FT /note="Tetraspanin-15"
FT /id="PRO_0000219263"
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..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..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 CONFLICT 236
FT /note="G -> C (in Ref. 2; AAQ89293)"
FT /evidence="ECO:0000305"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:7RDB"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:7RDB"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:7RDB"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:7RDB"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:7RDB"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:7RDB"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:7RDB"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:7RDB"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:7RDB"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:7RDB"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:7RDB"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:7RDB"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:7RDB"
SQ SEQUENCE 294 AA; 33165 MW; 71A6DC64D6CA6BAE CRC64;
MPRGDSEQVR YCARFSYLWL KFSLIIYSTV FWLIGALVLS VGIYAEVERQ KYKTLESAFL
APAIILILLG VVMFMVSFIG VLASLRDNLY LLQAFMYILG ICLIMELIGG VVALTFRNQT
IDFLNDNIRR GIENYYDDLD FKNIMDFVQK KFKCCGGEDY RDWSKNQYHD CSAPGPLACG
VPYTCCIRNT TEVVNTMCGY KTIDKERFSV QDVIYVRGCT NAVIIWFMDN YTIMAGILLG
ILLPQFLGVL LTLLYITRVE DIIMEHSVTD GLLGPGAKPS VEAAGTGCCL CYPN