ID   TSN7_MOUSE              Reviewed;         249 AA.
AC   Q62283; O88429; Q9DBS3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 2.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Tetraspanin-7;
DE            Short=Tspan-7;
DE   AltName: Full=Cell surface glycoprotein A15;
DE   AltName: Full=PE31;
DE   AltName: Full=TALLA homolog;
DE   AltName: Full=Transmembrane 4 superfamily member 2;
DE   AltName: CD_antigen=CD231;
GN   Name=Tspan7; Synonyms=Mxs1, Tm4sf2;
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] OF 5-249.
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RA   Nagira M., Ishikawa K., Fujikawa K., Takagi S., Yoshie O.;
RT   "Molecular cloning and expression of mouse PE31 (TALLA).";
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-249.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=10617319; DOI=10.1016/s0168-0102(99)00093-0;
RA   Hosokawa Y., Ueyama E., Morikawa Y., Maeda Y., Seto M., Senba E.;
RT   "Molecular cloning of a cDNA encoding mouse A15, a member of the
RT   transmembrane 4 superfamily, and its preferential expression in brain
RT   neurons.";
RL   Neurosci. Res. 35:281-290(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May be involved in cell proliferation and cell motility.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC34579.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA05493.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D26483; BAA05493.1; ALT_INIT; mRNA.
DR   EMBL; AF052492; AAC34579.1; ALT_INIT; mRNA.
DR   EMBL; AK004776; BAB23554.1; -; mRNA.
DR   CCDS; CCDS30016.1; -.
DR   RefSeq; NP_062608.2; NM_019634.2.
DR   AlphaFoldDB; Q62283; -.
DR   SMR; Q62283; -.
DR   BioGRID; 204231; 2.
DR   STRING; 10090.ENSMUSP00000075692; -.
DR   GlyCosmos; Q62283; 5 sites, No reported glycans.
DR   GlyGen; Q62283; 5 sites.
DR   PhosphoSitePlus; Q62283; -.
DR   SwissPalm; Q62283; -.
DR   jPOST; Q62283; -.
DR   MaxQB; Q62283; -.
DR   PaxDb; 10090-ENSMUSP00000075692; -.
DR   PeptideAtlas; Q62283; -.
DR   ProteomicsDB; 297995; -.
DR   DNASU; 21912; -.
DR   Ensembl; ENSMUST00000076354.13; ENSMUSP00000075692.7; ENSMUSG00000058254.13.
DR   GeneID; 21912; -.
DR   KEGG; mmu:21912; -.
DR   UCSC; uc009sqm.1; mouse.
DR   AGR; MGI:1298407; -.
DR   CTD; 7102; -.
DR   MGI; MGI:1298407; Tspan7.
DR   VEuPathDB; HostDB:ENSMUSG00000058254; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   GeneTree; ENSGT00940000156153; -.
DR   HOGENOM; CLU_055524_3_0_1; -.
DR   InParanoid; Q62283; -.
DR   OMA; MTIAPTK; -.
DR   OrthoDB; 2913577at2759; -.
DR   PhylomeDB; Q62283; -.
DR   TreeFam; TF352891; -.
DR   Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
DR   BioGRID-ORCS; 21912; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Tspan7; mouse.
DR   PRO; PR:Q62283; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q62283; Protein.
DR   Bgee; ENSMUSG00000058254; Expressed in dentate gyrus of hippocampal formation granule cell and 263 other cell types or tissues.
DR   ExpressionAtlas; Q62283; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
DR   CDD; cd03161; TM4SF2_6_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   InterPro; IPR048232; TSN6/7_LEL.
DR   PANTHER; PTHR19282; TETRASPANIN; 1.
DR   PANTHER; PTHR19282:SF257; TETRASPANIN-7; 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; Q62283; MM.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..249
FT                   /note="Tetraspanin-7"
FT                   /id="PRO_0000219249"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..56
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        146
FT                   /note="R -> P (in Ref. 2; AAC34579)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  27544 MW;  04B3A24D16B5DCD3 CRC64;
     MASRRMETKP VITCLKTLLI IYSFVFWITG VILLAVGVWG KLTLGTYISL IAENSTNAPY
     VLIGTGTTIV VFGLFGCFAT CRGSPWMLKL YAMFLSLVFL AELVAGISGF VFRHEIKDTF
     LRTYTDAMQN YNGNDERSRA VDHVQRSLSC CGVQNYTNWS SSPYFLDHGI PPSCCMNETD
     CNPLDLHNLT VAATKVNQKG CYDLVTSFME TNMGIIAGVA FGIAFSQLIG MLLACCLSRF
     ITANQYEMV
//