ID   TSN15_BOVIN             Reviewed;         294 AA.
AC   Q1JQA4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Tetraspanin-15;
DE            Short=Tspan-15;
GN   Name=TSPAN15;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   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).
CC   -!- FUNCTION: Regulates maturation and trafficking of the transmembrane
CC       metalloprotease ADAM10 (By similarity). Promotes ADAM10-mediated
CC       cleavage of CDH2 (By similarity). Negatively regulates ligand-induced
CC       Notch activity probably by regulating ADAM10 activity (By similarity).
CC       {ECO:0000250|UniProtKB:F7BWT7, ECO:0000250|UniProtKB:O95858}.
CC   -!- SUBUNIT: Interacts with ADAM10; the interaction influences ADAM10
CC       substrate specificity. {ECO:0000269|PubMed:23035126}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95858};
CC       Multi-pass membrane protein {ECO:0000305}. Late endosome membrane
CC       {ECO:0000250|UniProtKB:O95858}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR   EMBL; BC116110; AAI16111.1; -; mRNA.
DR   RefSeq; NP_001069297.1; NM_001075829.1.
DR   AlphaFoldDB; Q1JQA4; -.
DR   SMR; Q1JQA4; -.
DR   STRING; 9913.ENSBTAP00000031290; -.
DR   PaxDb; Q1JQA4; -.
DR   Ensembl; ENSBTAT00000031335; ENSBTAP00000031290; ENSBTAG00000000224.
DR   GeneID; 522371; -.
DR   KEGG; bta:522371; -.
DR   CTD; 23555; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000224; -.
DR   VGNC; VGNC:36430; TSPAN15.
DR   eggNOG; KOG3882; Eukaryota.
DR   GeneTree; ENSGT00940000157973; -.
DR   HOGENOM; CLU_055524_0_1_1; -.
DR   InParanoid; Q1JQA4; -.
DR   OMA; CVRNKTD; -.
DR   OrthoDB; 1416189at2759; -.
DR   TreeFam; TF313002; -.
DR   Proteomes; UP000009136; Chromosome 28.
DR   Bgee; ENSBTAG00000000224; Expressed in abomasum and 106 other tissues.
DR   ExpressionAtlas; Q1JQA4; baseline and differential.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR   GO; GO:0051604; P:protein maturation; IBA:GO_Central.
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; Endosome; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..294
FT                   /note="Tetraspanin-15"
FT                   /id="PRO_0000284966"
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"
SQ   SEQUENCE   294 AA;  33091 MW;  864E06351832534D CRC64;
     MPRGDSEQVR YCARFSYLWL KFSLVIYSTV FWLIGGLVLS VGIYAEVERQ KYKTLESAFL
     APAIILILLG VVMFIVSFIG VLASLRDNLC LLQAFMYILG ICLIIELIGG VVALIFRNQT
     IDFLNDNIRR GIENYYDDLD FKNIMDFVQK EFKCCGGEDY RDWSKNQYHD CRAPGPLACG
     VPYTCCFRNT TEVVNTMCGY KTIDKERLSV QNVIYVRGCT NAVLMWFTDN YTIMAGVLLG
     ILLPQFLGVL LTFLYITRVE DIITEHSVTD GLLGPGTKAG VEAAGTGCCM CYPI