ID   TSN17_BOVIN             Reviewed;         270 AA.
AC   Q58DN3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Tetraspanin-17;
DE            Short=Tspan-17;
GN   Name=TSPAN17;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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 ADAM10 maturation. {ECO:0000250|UniProtKB:Q9D7W4}.
CC   -!- SUBUNIT: Interacts with ADAM10. {ECO:0000269|PubMed:23035126}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR   EMBL; BT021564; AAX46411.1; -; mRNA.
DR   EMBL; BC111310; AAI11311.1; -; mRNA.
DR   RefSeq; NP_001014880.1; NM_001014880.3.
DR   AlphaFoldDB; Q58DN3; -.
DR   SMR; Q58DN3; -.
DR   STRING; 9913.ENSBTAP00000023198; -.
DR   PaxDb; Q58DN3; -.
DR   GeneID; 509386; -.
DR   KEGG; bta:509386; -.
DR   CTD; 26262; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   HOGENOM; CLU_055524_0_2_1; -.
DR   InParanoid; Q58DN3; -.
DR   OrthoDB; 1180379at2759; -.
DR   TreeFam; TF313002; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; IPR018503; Tetraspanin_CS.
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.
DR   PROSITE; PS00421; TM4_1; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..270
FT                   /note="Tetraspanin-17"
FT                   /id="PRO_0000287714"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..63
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..234
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   270 AA;  30262 MW;  DC98EFD0256F87C8 CRC64;
     MPGKHQHFQE PEVGCCGKYF LFGFNIVFWV LGALFLAIGL WAWSEKGVLS NISALTDLGG
     LDPVWLFVVV GGVMSVLGFA GCIGALRENT FLLKFFSVFL GLIFFLELAT GILAFVFKDW
     IRDQLNLFIN NNVKAYRDDI DLQNLIDFAQ EYWSCCGARG PNDWNLNIYF NCTDLNPSRE
     RCGVPFSCCV RDPAEDVLNT QCGYDVRLKL ELEQQGFIHT KGCVGQFEKW LQDNLIVVAG
     VFVGIALLQI FGICLAQNLV SDIKAVKANW