TSN2_RAT
ID TSN2_RAT Reviewed; 221 AA.
AC Q9JJW1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Tetraspanin-2;
DE Short=Tspan-2;
GN Name=Tspan2;
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].
RX PubMed=10582623; DOI=10.1046/j.1471-4159.1999.0732600.x;
RA Birling M.C., Tait S., Hardy R.J., Brophy P.J.;
RT "A novel rat tetraspan protein in cells of the oligodendrocyte lineage.";
RL J. Neurochem. 73:2600-2608(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
RN [3]
RP PROTEIN SEQUENCE OF 119-133; 155-166 AND 178-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: May play a role in signalling in oligodendrocytes in the
CC early stages of their terminal differentiation into myelin-forming glia
CC and may also function in stabilizing the mature sheath.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to the nervous system.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; AJ271442; CAB69827.1; -; mRNA.
DR EMBL; BC085733; AAH85733.1; -; mRNA.
DR RefSeq; NP_072111.1; NM_022589.1.
DR AlphaFoldDB; Q9JJW1; -.
DR SMR; Q9JJW1; -.
DR STRING; 10116.ENSRNOP00000033076; -.
DR GlyGen; Q9JJW1; 1 site, 33 N-linked glycans (1 site).
DR iPTMnet; Q9JJW1; -.
DR PaxDb; Q9JJW1; -.
DR PRIDE; Q9JJW1; -.
DR Ensembl; ENSRNOT00000035605; ENSRNOP00000033076; ENSRNOG00000023338.
DR GeneID; 64521; -.
DR KEGG; rno:64521; -.
DR UCSC; RGD:620982; rat.
DR CTD; 10100; -.
DR RGD; 620982; Tspan2.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157504; -.
DR HOGENOM; CLU_055524_10_1_1; -.
DR InParanoid; Q9JJW1; -.
DR OMA; VNRTIYH; -.
DR OrthoDB; 1205716at2759; -.
DR PhylomeDB; Q9JJW1; -.
DR TreeFam; TF352895; -.
DR PRO; PR:Q9JJW1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000023338; Expressed in lung and 20 other tissues.
DR Genevisible; Q9JJW1; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014002; P:astrocyte development; ISO:RGD.
DR GO; GO:0061564; P:axon development; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0014005; P:microglia development; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; 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 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..221
FT /note="Tetraspanin-2"
FT /id="PRO_0000219238"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..54
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
SQ SEQUENCE 221 AA; 24190 MW; E369888361AF4824 CRC64;
MGRFRGGLRC IKYLLLGFNL LFWLAGSAVI AFGLWFRFGG TIKDLSSEEK SPEYFYVGLY
VLVGAGALMM AVGFFGCCGA MRESQCVLGS FFTCLLVIFA AEVTTGVFAF IGKDVAIRHV
QSMYEEAYSD YVRDRGRGNG TLITFHSAFQ CCGKESSEQV QPTCPKELPG HKNCIDKIET
IISVKLQLIG IVGIGIAGLT IFGMIFSMVL CCAIRNSRDV I
