ID TSN3_MOUSE Reviewed; 253 AA. AC Q9QY33; Q9EQG4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 153. DE RecName: Full=Tetraspanin-3; DE Short=Tspan-3; DE AltName: Full=OSP-associated protein 1; DE Short=OAP-1; DE AltName: Full=Tetraspanin TM4-A; DE AltName: Full=Transmembrane 4 superfamily member 8; GN Name=Tspan3; Synonyms=Tm4sf8; 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 [MRNA]. RC TISSUE=Spleen; RX PubMed=11092739; DOI=10.3109/10425170009033242; RA Puls K.L., Wright M.D.; RT "The molecular characterisation of mouse tspan-3."; RL DNA Seq. 11:271-275(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CLDN11. RC STRAIN=C57BL/6J; RX PubMed=11309411; DOI=10.1083/jcb.153.2.295; RA Tiwari-Woodruff S.K., Buznikov A.G., Vu T.Q., Micevych P.E., Chen K., RA Kornblum H.I., Bronstein J.M.; RT "OSP/claudin-11 forms a complex with a novel member of the tetraspanin RT super family and beta1 integrin and regulates proliferation and migration RT of oligodendrocytes."; RL J. Cell Biol. 153:295-306(2001). CC -!- FUNCTION: Regulates the proliferation and migration of CC oligodendrocytes, a process essential for normal myelination and CC repair. CC -!- SUBUNIT: Interacts with claudin-11/CLDN11 and integrins. CC {ECO:0000269|PubMed:11309411}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF133427; AAF15362.1; -; mRNA. DR EMBL; AF242591; AAG49145.1; -; mRNA. DR CCDS; CCDS23207.1; -. DR RefSeq; NP_062767.3; NM_019793.3. DR AlphaFoldDB; Q9QY33; -. DR SMR; Q9QY33; -. DR CORUM; Q9QY33; -. DR STRING; 10090.ENSMUSP00000034876; -. DR GlyConnect; 2761; 13 N-Linked glycans (1 site). DR GlyCosmos; Q9QY33; 4 sites, 13 glycans. DR GlyGen; Q9QY33; 4 sites, 13 N-linked glycans (1 site). DR iPTMnet; Q9QY33; -. DR PhosphoSitePlus; Q9QY33; -. DR SwissPalm; Q9QY33; -. DR PaxDb; 10090-ENSMUSP00000034876; -. DR ProteomicsDB; 297665; -. DR Pumba; Q9QY33; -. DR Antibodypedia; 3085; 186 antibodies from 20 providers. DR DNASU; 56434; -. DR Ensembl; ENSMUST00000034876.10; ENSMUSP00000034876.9; ENSMUSG00000032324.12. DR GeneID; 56434; -. DR KEGG; mmu:56434; -. DR UCSC; uc009psx.2; mouse. DR AGR; MGI:1928098; -. DR CTD; 10099; -. DR MGI; MGI:1928098; Tspan3. DR VEuPathDB; HostDB:ENSMUSG00000032324; -. DR eggNOG; KOG3882; Eukaryota. DR GeneTree; ENSGT00940000154954; -. DR HOGENOM; CLU_055524_5_2_1; -. DR InParanoid; Q9QY33; -. DR OMA; ISCCKIA; -. DR OrthoDB; 2913577at2759; -. DR PhylomeDB; Q9QY33; -. DR TreeFam; TF316345; -. DR BioGRID-ORCS; 56434; 1 hit in 78 CRISPR screens. DR ChiTaRS; Tspan3; mouse. DR PRO; PR:Q9QY33; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q9QY33; Protein. DR Bgee; ENSMUSG00000032324; Expressed in vestibular epithelium and 256 other cell types or tissues. DR ExpressionAtlas; Q9QY33; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR CDD; cd03163; TM4SF8_like_LEL; 1. DR Gene3D; 1.10.1450.10; Tetraspanin; 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; TETRASPANIN; 1. DR PANTHER; PTHR19282:SF48; TETRASPANIN-3; 1. DR Pfam; PF00335; Tetraspanin; 1. DR PIRSF; PIRSF002419; Tetraspanin; 1. DR PRINTS; PR00259; TMFOUR. DR SUPFAM; SSF48652; Tetraspanin; 1. DR PROSITE; PS00421; TM4_1; 1. DR Genevisible; Q9QY33; MM. PE 1: Evidence at protein level; KW Glycoprotein; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..253 FT /note="Tetraspanin-3" FT /id="PRO_0000219240" FT TOPO_DOM 1..11 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 33..50 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 51..71 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 72..85 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 86..106 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 107..212 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 213..233 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 234..253 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 152 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 167 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 183 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 220 FT /note="A -> R (in Ref. 2; AAG49145)" FT /evidence="ECO:0000305" FT CONFLICT 226 FT /note="G -> A (in Ref. 2; AAG49145)" FT /evidence="ECO:0000305" SQ SEQUENCE 253 AA; 28049 MW; 8A7378F76263019A CRC64; MGQCGITSSK TVLVFLNLIF WGAAGILCYV GAYVFITYDD YDHFFEDVYT LFPAVVIIAV GALLFIIGLI GCCATIRESR CGLATFVFIL LLVFVTEVVV VVLGYVYRAK VENEVDRSIQ KVYKTYNGTN SDAASRAIDY VQRQLHCCGI HNYSDWENTD WFKETKNQSV PLSCCRETAK SCNGSLANPS DLYAEGCEAL VVKKLQEILM HVIWAALAFA AIQLLGMLCA CIVLCRRSRD PAYELLITGG TYA //