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TSN15_HUMAN
ID   TSN15_HUMAN             Reviewed;         294 AA.
AC   O95858; Q6UW79;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Tetraspanin-15;
DE            Short=Tspan-15;
DE   AltName: Full=Tetraspan NET-7;
DE   AltName: Full=Transmembrane 4 superfamily member 15;
GN   Name=TSPAN15; Synonyms=NET7, TM4SF15; ORFNames=UNQ677/PRO1311;
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].
RA   Rubinstein E., Serru V., Dessen P., Boucheix C.;
RT   "New tetraspans identified in the EST database.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN   [4]
RP   FUNCTION, INTERACTION WITH ADAM10, AND SUBCELLULAR LOCATION.
RX   PubMed=26686862; DOI=10.1007/s00018-015-2111-z;
RA   Jouannet S., Saint-Pol J., Fernandez L., Nguyen V., Charrin S.,
RA   Boucheix C., Brou C., Milhiet P.E., Rubinstein E.;
RT   "TspanC8 tetraspanins differentially regulate the cleavage of ADAM10
RT   substrates, Notch activation and ADAM10 membrane compartmentalization.";
RL   Cell. Mol. Life Sci. 73:1895-1915(2016).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=30463011; DOI=10.1016/j.celrep.2018.10.088;
RA   Shah J., Rouaud F., Guerrera D., Vasileva E., Popov L.M., Kelley W.L.,
RA   Rubinstein E., Carette J.E., Amieva M.R., Citi S.;
RT   "A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
RT   Promote alpha-Toxin Cytotoxicity.";
RL   Cell Rep. 25:2132-2147(2018).
CC   -!- FUNCTION: Regulates maturation and trafficking of the transmembrane
CC       metalloprotease ADAM10 (PubMed:26686862, PubMed:30463011). Promotes
CC       ADAM10-mediated cleavage of CDH2 (By similarity). Negatively regulates
CC       ligand-induced Notch activity probably by regulating ADAM10 activity
CC       (PubMed:26686862). {ECO:0000250|UniProtKB:F7BWT7,
CC       ECO:0000269|PubMed:26686862, ECO:0000269|PubMed:30463011}.
CC   -!- SUBUNIT: Interacts with ADAM10; the interaction influences ADAM10
CC       substrate specificity. {ECO:0000269|PubMed:26686862}.
CC   -!- INTERACTION:
CC       O95858; O14672: ADAM10; NbExp=9; IntAct=EBI-7361096, EBI-1536151;
CC       O95858; P04921: GYPC; NbExp=3; IntAct=EBI-7361096, EBI-7797098;
CC       O95858; P0DN84: STRIT1; NbExp=3; IntAct=EBI-7361096, EBI-12200293;
CC       O95858; Q8N205: SYNE4; NbExp=3; IntAct=EBI-7361096, EBI-7131783;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26686862,
CC       ECO:0000269|PubMed:30463011}; Multi-pass membrane protein
CC       {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:26686862}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR   EMBL; AF120266; AAD17295.1; -; mRNA.
DR   EMBL; AY358934; AAQ89293.1; -; mRNA.
DR   EMBL; BC003157; AAH03157.1; -; mRNA.
DR   EMBL; BC004161; AAH04161.1; -; mRNA.
DR   CCDS; CCDS7294.1; -.
DR   RefSeq; NP_036471.1; NM_012339.3.
DR   PDB; 7RD5; X-ray; 3.60 A; E/F=115-230.
DR   PDB; 7RDB; X-ray; 2.52 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=115-230.
DR   PDBsum; 7RD5; -.
DR   PDBsum; 7RDB; -.
DR   AlphaFoldDB; O95858; -.
DR   SMR; O95858; -.
DR   BioGRID; 117099; 296.
DR   IntAct; O95858; 62.
DR   MINT; O95858; -.
DR   STRING; 9606.ENSP00000362387; -.
DR   TCDB; 8.A.40.1.17; the tetraspanin (tetraspanin) family.
DR   GlyGen; O95858; 3 sites.
DR   iPTMnet; O95858; -.
DR   PhosphoSitePlus; O95858; -.
DR   SwissPalm; O95858; -.
DR   BioMuta; TSPAN15; -.
DR   EPD; O95858; -.
DR   jPOST; O95858; -.
DR   MassIVE; O95858; -.
DR   MaxQB; O95858; -.
DR   PaxDb; O95858; -.
DR   PeptideAtlas; O95858; -.
DR   PRIDE; O95858; -.
DR   ProteomicsDB; 51091; -.
DR   Antibodypedia; 28879; 112 antibodies from 21 providers.
DR   DNASU; 23555; -.
DR   Ensembl; ENST00000373290.7; ENSP00000362387.2; ENSG00000099282.10.
DR   GeneID; 23555; -.
DR   KEGG; hsa:23555; -.
DR   MANE-Select; ENST00000373290.7; ENSP00000362387.2; NM_012339.5; NP_036471.1.
DR   UCSC; uc001jpo.2; human.
DR   CTD; 23555; -.
DR   DisGeNET; 23555; -.
DR   GeneCards; TSPAN15; -.
DR   HGNC; HGNC:23298; TSPAN15.
DR   HPA; ENSG00000099282; Low tissue specificity.
DR   MIM; 613140; gene.
DR   neXtProt; NX_O95858; -.
DR   OpenTargets; ENSG00000099282; -.
DR   PharmGKB; PA128394634; -.
DR   VEuPathDB; HostDB:ENSG00000099282; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   GeneTree; ENSGT00940000157973; -.
DR   HOGENOM; CLU_055524_0_1_1; -.
DR   InParanoid; O95858; -.
DR   OMA; CVRNKTD; -.
DR   OrthoDB; 1416189at2759; -.
DR   PhylomeDB; O95858; -.
DR   TreeFam; TF313002; -.
DR   PathwayCommons; O95858; -.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   SignaLink; O95858; -.
DR   SIGNOR; O95858; -.
DR   BioGRID-ORCS; 23555; 11 hits in 1076 CRISPR screens.
DR   ChiTaRS; TSPAN15; human.
DR   GenomeRNAi; 23555; -.
DR   Pharos; O95858; Tbio.
DR   PRO; PR:O95858; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; O95858; protein.
DR   Bgee; ENSG00000099282; Expressed in tibial nerve and 171 other tissues.
DR   ExpressionAtlas; O95858; baseline and differential.
DR   Genevisible; O95858; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0097197; C:tetraspanin-enriched microdomain; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR   GO; GO:0051604; P:protein maturation; IMP:UniProtKB.
DR   Gene3D; 1.10.1450.10; -; 1.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR000301; Tetraspanin_animals.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Endosome; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..294
FT                   /note="Tetraspanin-15"
FT                   /id="PRO_0000219263"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..62
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..294
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        236
FT                   /note="G -> C (in Ref. 2; AAQ89293)"
FT                   /evidence="ECO:0000305"
FT   HELIX           117..133
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   TURN            134..137
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   HELIX           139..151
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   STRAND          156..159
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   HELIX           160..165
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   TURN            167..169
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   TURN            196..199
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   HELIX           207..210
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   TURN            211..213
FT                   /evidence="ECO:0007829|PDB:7RDB"
FT   HELIX           219..229
FT                   /evidence="ECO:0007829|PDB:7RDB"
SQ   SEQUENCE   294 AA;  33165 MW;  71A6DC64D6CA6BAE CRC64;
     MPRGDSEQVR YCARFSYLWL KFSLIIYSTV FWLIGALVLS VGIYAEVERQ KYKTLESAFL
     APAIILILLG VVMFMVSFIG VLASLRDNLY LLQAFMYILG ICLIMELIGG VVALTFRNQT
     IDFLNDNIRR GIENYYDDLD FKNIMDFVQK KFKCCGGEDY RDWSKNQYHD CSAPGPLACG
     VPYTCCIRNT TEVVNTMCGY KTIDKERFSV QDVIYVRGCT NAVIIWFMDN YTIMAGILLG
     ILLPQFLGVL LTLLYITRVE DIIMEHSVTD GLLGPGAKPS VEAAGTGCCL CYPN
 
 
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