TSN2_HUMAN
ID TSN2_HUMAN Reviewed; 221 AA.
AC O60636; D6PTH4; Q5TET2; Q8WU05;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Tetraspanin-2;
DE Short=Tspan-2;
DE AltName: Full=Tetraspan NET-3;
GN Name=TSPAN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9714763; DOI=10.1016/s0167-4781(98)00087-6;
RA Todd S.C., Doctor V.S., Levy S.;
RT "Sequences and expression of six new members of the tetraspanin/TM4SF
RT family.";
RL Biochim. Biophys. Acta 1399:101-104(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RA Ryu H.-W., Park J.;
RT "Cloning of a TSPAN2 splice isoform.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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: 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. {ECO:0000250}.
CC -!- INTERACTION:
CC O60636; O95870: ABHD16A; NbExp=3; IntAct=EBI-3914288, EBI-348517;
CC O60636; Q86V38: ATN1; NbExp=3; IntAct=EBI-3914288, EBI-11954292;
CC O60636; Q9UN42: ATP1B4; NbExp=3; IntAct=EBI-3914288, EBI-12894731;
CC O60636; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-3914288, EBI-11532900;
CC O60636; P11912: CD79A; NbExp=3; IntAct=EBI-3914288, EBI-7797864;
CC O60636; O00501: CLDN5; NbExp=3; IntAct=EBI-3914288, EBI-18400628;
CC O60636; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-3914288, EBI-17710733;
CC O60636; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-3914288, EBI-6942903;
CC O60636; P02489: CRYAA; NbExp=3; IntAct=EBI-3914288, EBI-6875961;
CC O60636; Q96PD2-2: DCBLD2; NbExp=3; IntAct=EBI-3914288, EBI-12135455;
CC O60636; P00488: F13A1; NbExp=3; IntAct=EBI-3914288, EBI-2565863;
CC O60636; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-3914288, EBI-18304435;
CC O60636; P22607: FGFR3; NbExp=3; IntAct=EBI-3914288, EBI-348399;
CC O60636; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-3914288, EBI-10226858;
CC O60636; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-3914288, EBI-3918971;
CC O60636; P62993: GRB2; NbExp=6; IntAct=EBI-3914288, EBI-401755;
CC O60636; P06396: GSN; NbExp=3; IntAct=EBI-3914288, EBI-351506;
CC O60636; P54652: HSPA2; NbExp=3; IntAct=EBI-3914288, EBI-356991;
CC O60636; P38484: IFNGR2; NbExp=3; IntAct=EBI-3914288, EBI-3905457;
CC O60636; O43731-2: KDELR3; NbExp=3; IntAct=EBI-3914288, EBI-18157502;
CC O60636; O14901: KLF11; NbExp=3; IntAct=EBI-3914288, EBI-948266;
CC O60636; Q92876: KLK6; NbExp=3; IntAct=EBI-3914288, EBI-2432309;
CC O60636; O95214: LEPROTL1; NbExp=3; IntAct=EBI-3914288, EBI-750776;
CC O60636; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-3914288, EBI-11956541;
CC O60636; O14880: MGST3; NbExp=3; IntAct=EBI-3914288, EBI-724754;
CC O60636; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-3914288, EBI-2811583;
CC O60636; O15173: PGRMC2; NbExp=3; IntAct=EBI-3914288, EBI-1050125;
CC O60636; Q92569: PIK3R3; NbExp=3; IntAct=EBI-3914288, EBI-79893;
CC O60636; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-3914288, EBI-7545592;
CC O60636; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-3914288, EBI-2466594;
CC O60636; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-3914288, EBI-17247926;
CC O60636; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-3914288, EBI-18159983;
CC O60636; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-3914288, EBI-10262251;
CC O60636; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-3914288, EBI-17295964;
CC O60636; Q8N3G9: TMEM130; NbExp=3; IntAct=EBI-3914288, EBI-19763514;
CC O60636; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-3914288, EBI-8638294;
CC O60636; Q9Y320: TMX2; NbExp=3; IntAct=EBI-3914288, EBI-6447886;
CC O60636; Q12999: TSPAN31; NbExp=3; IntAct=EBI-3914288, EBI-17678331;
CC O60636; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-3914288, EBI-741480;
CC O60636; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-3914288, EBI-744988;
CC O60636; Q5T4F4: ZFYVE27; NbExp=3; IntAct=EBI-3914288, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60636-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60636-2; Sequence=VSP_047734;
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; AF054839; AAC69715.1; -; mRNA.
DR EMBL; GU971730; ADF80915.1; -; mRNA.
DR EMBL; AL109660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021675; AAH21675.1; -; mRNA.
DR CCDS; CCDS881.1; -. [O60636-1]
DR PIR; A59263; A59263.
DR RefSeq; NP_001295245.1; NM_001308316.1. [O60636-2]
DR RefSeq; NP_005716.2; NM_005725.5. [O60636-1]
DR AlphaFoldDB; O60636; -.
DR SMR; O60636; -.
DR BioGRID; 115407; 68.
DR IntAct; O60636; 61.
DR STRING; 9606.ENSP00000358529; -.
DR GlyGen; O60636; 1 site.
DR iPTMnet; O60636; -.
DR PhosphoSitePlus; O60636; -.
DR BioMuta; TSPAN2; -.
DR jPOST; O60636; -.
DR MassIVE; O60636; -.
DR MaxQB; O60636; -.
DR PaxDb; O60636; -.
DR PeptideAtlas; O60636; -.
DR PRIDE; O60636; -.
DR ProteomicsDB; 12837; -.
DR ProteomicsDB; 49489; -. [O60636-1]
DR Antibodypedia; 2866; 246 antibodies from 26 providers.
DR DNASU; 10100; -.
DR Ensembl; ENST00000369516.7; ENSP00000358529.2; ENSG00000134198.10. [O60636-1]
DR GeneID; 10100; -.
DR KEGG; hsa:10100; -.
DR MANE-Select; ENST00000369516.7; ENSP00000358529.2; NM_005725.6; NP_005716.2.
DR UCSC; uc001eft.5; human. [O60636-1]
DR CTD; 10100; -.
DR DisGeNET; 10100; -.
DR GeneCards; TSPAN2; -.
DR HGNC; HGNC:20659; TSPAN2.
DR HPA; ENSG00000134198; Tissue enhanced (endometrium).
DR MIM; 613133; gene.
DR neXtProt; NX_O60636; -.
DR OpenTargets; ENSG00000134198; -.
DR PharmGKB; PA134938787; -.
DR VEuPathDB; HostDB:ENSG00000134198; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157504; -.
DR InParanoid; O60636; -.
DR OMA; VNRTIYH; -.
DR PhylomeDB; O60636; -.
DR TreeFam; TF352895; -.
DR PathwayCommons; O60636; -.
DR SignaLink; O60636; -.
DR BioGRID-ORCS; 10100; 3 hits in 1065 CRISPR screens.
DR ChiTaRS; TSPAN2; human.
DR GeneWiki; TSPAN2; -.
DR GenomeRNAi; 10100; -.
DR Pharos; O60636; Tbio.
DR PRO; PR:O60636; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60636; protein.
DR Bgee; ENSG00000134198; Expressed in body of uterus and 152 other tissues.
DR ExpressionAtlas; O60636; baseline and differential.
DR Genevisible; O60636; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0061564; P:axon development; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0014005; P:microglia development; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
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 Alternative splicing; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..221
FT /note="Tetraspanin-2"
FT /id="PRO_0000219236"
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:0000255"
FT VAR_SEQ 173..200
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047734"
FT VARIANT 118
FT /note="R -> L (in dbSNP:rs9659602)"
FT /id="VAR_052328"
FT CONFLICT 80..82
FT /note="AMR -> PCW (in Ref. 1; AAC69715)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..148
FT /note="HST -> PLQH (in Ref. 1; AAC69715)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="G -> R (in Ref. 1; AAC69715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 24148 MW; 8973B46795901802 CRC64;
MGRFRGGLRC IKYLLLGFNL LFWLAGSAVI AFGLWFRFGG AIKELSSEDK SPEYFYVGLY
VLVGAGALMM AVGFFGCCGA MRESQCVLGS FFTCLLVIFA AEVTTGVFAF IGKGVAIRHV
QTMYEEAYND YLKDRGKGNG TLITFHSTFQ CCGKESSEQV QPTCPKELLG HKNCIDEIET
IISVKLQLIG IVGIGIAGLT IFGMIFSMVL CCAIRNSRDV I
