TSN3_MOUSE
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 03-AUG-2022, entry version 145.
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}.
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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 GlyGen; Q9QY33; 4 sites, 13 N-linked glycans (1 site).
DR iPTMnet; Q9QY33; -.
DR PhosphoSitePlus; Q9QY33; -.
DR SwissPalm; Q9QY33; -.
DR PaxDb; Q9QY33; -.
DR PRIDE; Q9QY33; -.
DR ProteomicsDB; 297665; -.
DR Antibodypedia; 3085; 163 antibodies from 20 providers.
DR DNASU; 56434; -.
DR Ensembl; ENSMUST00000034876; ENSMUSP00000034876; ENSMUSG00000032324.
DR GeneID; 56434; -.
DR KEGG; mmu:56434; -.
DR UCSC; uc009psx.2; mouse.
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; CRETARS; -.
DR OrthoDB; 1406905at2759; -.
DR PhylomeDB; Q9QY33; -.
DR TreeFam; TF316345; -.
DR BioGRID-ORCS; 56434; 1 hit in 73 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 253 other tissues.
DR ExpressionAtlas; Q9QY33; baseline and differential.
DR Genevisible; Q9QY33; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; 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..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
