TSN10_HUMAN
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 25-MAY-2022, entry version 143.
DE RecName: Full=Tetraspanin-10;
DE Short=Tspan-10;
DE AltName: Full=Oculospanin;
GN Name=TSPAN10; 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).
CC -!- FUNCTION: Regulates maturation of the transmembrane metalloprotease
CC ADAM10. {ECO:0000250|UniProtKB:Q8VCF5}.
CC -!- SUBUNIT: Interacts with ADAM10. {ECO:0000250|UniProtKB:Q8VCF5}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; CCDS77130.1; -.
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; 131.
DR IntAct; Q9H1Z9; 5.
DR MINT; Q9H1Z9; -.
DR STRING; 9606.ENSP00000480492; -.
DR TCDB; 8.A.40.1.10; the tetraspanin (tetraspanin) family.
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 PeptideAtlas; Q9H1Z9; -.
DR PRIDE; Q9H1Z9; -.
DR ProteomicsDB; 80462; -.
DR DNASU; 83882; -.
DR GeneID; 83882; -.
DR KEGG; hsa:83882; -.
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; 1416189at2759; -.
DR PhylomeDB; Q9H1Z9; -.
DR PathwayCommons; Q9H1Z9; -.
DR SignaLink; Q9H1Z9; -.
DR BioGRID-ORCS; 83882; 10 hits in 202 CRISPR screens.
DR GenomeRNAi; 83882; -.
DR Pharos; Q9H1Z9; Tdark.
DR PRO; PR:Q9H1Z9; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9H1Z9; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IDA:UniProtKB.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR018503; Tetraspanin_CS.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR SUPFAM; SSF48652; SSF48652; 1.
DR PROSITE; PS00421; TM4_1; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW 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 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
