ID   TSN10_HUMAN             Reviewed;         355 AA.
AC   Q9H1Z9; Q8N548;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Tetraspanin-10;
DE            Short=Tspan-10;
DE   AltName: Full=Oculospanin;
GN   Name=TSPAN10 {ECO:0000312|HGNC:HGNC:29942}; Synonyms=OCSP;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Eye;
RX   PubMed=12107410;
RA   Wistow G., Bernstein S.L., Wyatt M.K., Fariss R.N., Behal A.,
RA   Touchman J.W., Bouffard G., Smith D., Peterson K.;
RT   "Expressed sequence tag analysis of human RPE/choroid for the NEIBank
RT   project: over 6000 non-redundant transcripts, novel genes and splice
RT   variants.";
RL   Mol. Vis. 8:205-220(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   FUNCTION.
RX   PubMed=37516108; DOI=10.1016/j.cell.2023.06.026;
RA   Lipper C.H., Egan E.D., Gabriel K.H., Blacklow S.C.;
RT   "Structural basis for membrane-proximal proteolysis of substrates by
RT   ADAM10.";
RL   Cell 186:3632-3641.e10(2023).
CC   -!- FUNCTION: Part of TspanC8 subgroup, composed of 6 members that interact
CC       with the transmembrane metalloprotease ADAM10. This interaction is
CC       required for ADAM10 exit from the endoplasmic reticulum and for
CC       enzymatic maturation and trafficking to the cell surface as well as
CC       substrate specificity. Different TspanC8/ADAM10 complexes have distinct
CC       substrates. {ECO:0000269|PubMed:37516108}.
CC   -!- SUBUNIT: Interacts with ADAM10. {ECO:0000250|UniProtKB:Q8VCF5}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VCF5};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8VCF5}.
CC   -!- TISSUE SPECIFICITY: Expressed in the eye, including iris, ciliary body,
CC       retinal pigment epithelium, but not lens (protein level).
CC       {ECO:0000269|PubMed:12107410}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR   EMBL; AF325213; AAG42857.1; -; mRNA.
DR   EMBL; BC032802; AAH32802.1; -; mRNA.
DR   CCDS; CCDS58608.1; -.
DR   RefSeq; NP_001277141.1; NM_001290212.1.
DR   RefSeq; NP_114151.3; NM_031945.4.
DR   AlphaFoldDB; Q9H1Z9; -.
DR   SMR; Q9H1Z9; -.
DR   BioGRID; 123795; 132.
DR   IntAct; Q9H1Z9; 5.
DR   MINT; Q9H1Z9; -.
DR   STRING; 9606.ENSP00000480492; -.
DR   TCDB; 8.A.40.1.10; the tetraspanin (tetraspanin) family.
DR   GlyCosmos; Q9H1Z9; 1 site, No reported glycans.
DR   GlyGen; Q9H1Z9; 1 site.
DR   iPTMnet; Q9H1Z9; -.
DR   PhosphoSitePlus; Q9H1Z9; -.
DR   SwissPalm; Q9H1Z9; -.
DR   BioMuta; TSPAN10; -.
DR   DMDM; 34222702; -.
DR   jPOST; Q9H1Z9; -.
DR   MassIVE; Q9H1Z9; -.
DR   MaxQB; Q9H1Z9; -.
DR   PaxDb; 9606-ENSP00000480492; -.
DR   PeptideAtlas; Q9H1Z9; -.
DR   ProteomicsDB; 80462; -.
DR   DNASU; 83882; -.
DR   GeneID; 83882; -.
DR   KEGG; hsa:83882; -.
DR   AGR; HGNC:29942; -.
DR   CTD; 83882; -.
DR   DisGeNET; 83882; -.
DR   GeneCards; TSPAN10; -.
DR   HGNC; HGNC:29942; TSPAN10.
DR   neXtProt; NX_Q9H1Z9; -.
DR   PharmGKB; PA142670686; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   InParanoid; Q9H1Z9; -.
DR   OrthoDB; 4633400at2759; -.
DR   PhylomeDB; Q9H1Z9; -.
DR   PathwayCommons; Q9H1Z9; -.
DR   SignaLink; Q9H1Z9; -.
DR   BioGRID-ORCS; 83882; 10 hits in 246 CRISPR screens.
DR   GenomeRNAi; 83882; -.
DR   Pharos; Q9H1Z9; Tdark.
DR   PRO; PR:Q9H1Z9; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q9H1Z9; Protein.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0072594; P:establishment of protein localization to organelle; IDA:UniProtKB.
DR   CDD; cd03167; oculospanin_like_LEL; 1.
DR   Gene3D; 1.10.1450.10; Tetraspanin; 1.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR018503; Tetraspanin_CS.
DR   InterPro; IPR008952; Tetraspanin_EC2_sf.
DR   PANTHER; PTHR19282; TETRASPANIN; 1.
DR   PANTHER; PTHR19282:SF563; TETRASPANIN-10; 1.
DR   Pfam; PF00335; Tetraspanin; 1.
DR   PRINTS; PR00259; TMFOUR.
DR   SUPFAM; SSF48652; Tetraspanin; 1.
DR   PROSITE; PS00421; TM4_1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..355
FT                   /note="Tetraspanin-10"
FT                   /id="PRO_0000219255"
FT   TOPO_DOM        1..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..120
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..355
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..355
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        212..279
FT                   /evidence="ECO:0000250|UniProtKB:O95858"
FT   DISULFID        213..243
FT                   /evidence="ECO:0000250|UniProtKB:O95858"
FT   DISULFID        229..237
FT                   /evidence="ECO:0000250|UniProtKB:O95858"
FT   DISULFID        244..258
FT                   /evidence="ECO:0000250|UniProtKB:O95858"
FT   VARIANT         187
FT                   /note="R -> H (in dbSNP:rs34896443)"
FT                   /id="VAR_057277"
FT   VARIANT         218
FT                   /note="Y -> H (in dbSNP:rs34379910)"
FT                   /id="VAR_061849"
FT   CONFLICT        332
FT                   /note="H -> R (in Ref. 2; AAH32802)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   355 AA;  36498 MW;  1F9AEE3FAE7ABE7A CRC64;
     MEEGERSPLL SQETAGQKPL SVHRPPTSGC LGPVPREDQA EAWGCSCCPP ETKHQALSGT
     PKKGPAPSLS PGSSCVKYLI FLSNFPFSLL GLLALAIGLW GLAVKGSLGS DLGGPLPTDP
     MLGLALGGLV VSAASLAGCL GALCENTCLL RGFSGGILAF LVLEAVAGAL VVALWGPLQD
     SLEHTLRVAI AHYQDDPDLR FLLDQVQLGL RCCGAASYQD WQQNLYFNCS SPGVQACSLP
     ASCCIDPRED GASVNDQCGF GVLRLDADAA QRVVYLEGCG PPLRRWLRAN LAASGGYAIA
     VVLLQGAELL LAARLLGALA ARSGAAYGPG AHGEDRAGPQ SPSPGAPPAA KPARG
//