ID   TSN5_RAT                Reviewed;         268 AA.
AC   Q68VK5; Q498N9;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Tetraspanin-5;
DE            Short=Tspan-5;
DE   AltName: Full=Transmembrane 4 superfamily member 9;
GN   Name=Tspan5; Synonyms=Tm4sf9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Brain;
RA   Braeuer A.U., Savaskan N.E., Ninnemann O., Nitsch R.;
RT   "Tetraspanin-5 is upregulated after lesion in the hippocampus.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: Regulates ADAM10 maturation and trafficking to the cell
CC       surface. Promotes ADAM10-mediated cleavage of CD44.
CC       {ECO:0000250|UniProtKB:P62079, ECO:0000250|UniProtKB:P62080}.
CC   -!- SUBUNIT: Interacts with ADAM10. {ECO:0000250|UniProtKB:P62080}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P62079};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR   EMBL; AF540877; AAQ11226.1; -; mRNA.
DR   EMBL; BC100135; AAI00136.1; -; mRNA.
DR   RefSeq; NP_001004090.2; NM_001004090.2.
DR   AlphaFoldDB; Q68VK5; -.
DR   SMR; Q68VK5; -.
DR   STRING; 10116.ENSRNOP00000021381; -.
DR   GlyGen; Q68VK5; 4 sites.
DR   PhosphoSitePlus; Q68VK5; -.
DR   PaxDb; Q68VK5; -.
DR   Ensembl; ENSRNOT00000021381; ENSRNOP00000021381; ENSRNOG00000015913.
DR   GeneID; 362048; -.
DR   KEGG; rno:362048; -.
DR   CTD; 10098; -.
DR   RGD; 1303176; Tspan5.
DR   eggNOG; KOG3882; Eukaryota.
DR   GeneTree; ENSGT00940000161376; -.
DR   HOGENOM; CLU_055524_0_2_1; -.
DR   InParanoid; Q68VK5; -.
DR   OMA; RECAWDE; -.
DR   OrthoDB; 1180379at2759; -.
DR   PhylomeDB; Q68VK5; -.
DR   TreeFam; TF313002; -.
DR   PRO; PR:Q68VK5; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000015913; Expressed in frontal cortex and 19 other tissues.
DR   Genevisible; Q68VK5; RN.
DR   GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR   GO; GO:0008283; P:cell population proliferation; TAS:RGD.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR   GO; GO:0051604; P:protein maturation; ISO:RGD.
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   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..268
FT                   /note="Tetraspanin-5"
FT                   /id="PRO_0000219245"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..61
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        142
FT                   /note="N -> S (in Ref. 1; AAQ11226)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   268 AA;  30337 MW;  7F4480BD0FA6192D CRC64;
     MSGKHYKGPE VSCCIKYFIF GFNVIFWFLG ITFLGIGLWA WNEKGVLSNI SSITDLGGFD
     PVWLFLVVGG VMFILGFAGC IGALRENTFL LKFFSVFLGI IFFLELTAGV LAFVFKDWIK
     DQLYFFINNN IRAYRDDIDL QNLIDFTQEY WQCCGAFGAD DWNLNIYFNC TDSNASRERC
     GVPFSCCTKD PAEDVINTQC GYDARQKPEV DQQIVIYTKG CVPQFEKWLQ DNLTIVAGIF
     IGIALLQIFG ICLAQNLVSD IEAVRASW