TSN14_HUMAN
ID TSN14_HUMAN Reviewed; 270 AA.
AC Q8NG11; A6NHE1; B4DHY6; D3DWD7; D3DWD8; Q567U7; Q9BU34; Q9H0U1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Tetraspanin-14;
DE Short=Tspan-14;
DE AltName: Full=DC-TM4F2;
DE AltName: Full=Transmembrane 4 superfamily member 14;
GN Name=TSPAN14; Synonyms=TM4SF14;
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).
RA Zhang W., Li N., Wan T., Cao X.;
RT "Identification of novel membrane proteins.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Skin;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, AND INTERACTION WITH ADAM10.
RX PubMed=23035126; DOI=10.1074/jbc.m112.416503;
RA Haining E.J., Yang J., Bailey R.L., Khan K., Collier R., Tsai S.,
RA Watson S.P., Frampton J., Garcia P., Tomlinson M.G.;
RT "The TspanC8 subgroup of tetraspanins interacts with A disintegrin and
RT metalloprotease 10 (ADAM10) and regulates its maturation and cell surface
RT expression.";
RL J. Biol. Chem. 287:39753-39765(2012).
RN [9]
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 [10]
RP FUNCTION, AND INTERACTION WITH ADAM10.
RX PubMed=26668317; DOI=10.1074/jbc.m115.703058;
RA Noy P.J., Yang J., Reyat J.S., Matthews A.L., Charlton A.E., Furmston J.,
RA Rogers D.A., Rainger G.E., Tomlinson M.G.;
RT "TspanC8 tetraspanins and A disintegrin and metalloprotease 10 (ADAM10)
RT interact via their extracellular regions: evidence for distinct binding
RT mechanisms for different TspanC8 proteins.";
RL J. Biol. Chem. 291:3145-3157(2016).
CC -!- FUNCTION: Regulates maturation and trafficking of the transmembrane
CC metalloprotease ADAM10 (PubMed:26668317, PubMed:23035126,
CC PubMed:26686862). Negatively regulates ADAM10-mediated cleavage of GP6
CC (By similarity). Promotes ADAM10-mediated cleavage of CDH5 (By
CC similarity). {ECO:0000250|UniProtKB:Q8QZY6,
CC ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317,
CC ECO:0000269|PubMed:26686862}.
CC -!- SUBUNIT: Interacts with ADAM10; the interaction promotes ADAM10
CC maturation and cell surface expression. {ECO:0000269|PubMed:23035126,
CC ECO:0000269|PubMed:26668317, ECO:0000269|PubMed:26686862}.
CC -!- INTERACTION:
CC Q8NG11; O14672: ADAM10; NbExp=9; IntAct=EBI-6308913, EBI-1536151;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26686862};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NG11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NG11-2; Sequence=VSP_011878;
CC Name=3;
CC IsoId=Q8NG11-3; Sequence=VSP_043194;
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; AF311903; AAM94899.1; -; mRNA.
DR EMBL; AL136638; CAB66573.1; -; mRNA.
DR EMBL; AK295321; BAG58298.1; -; mRNA.
DR EMBL; AC021028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471142; EAW80384.1; -; Genomic_DNA.
DR EMBL; CH471142; EAW80385.1; -; Genomic_DNA.
DR EMBL; CH471142; EAW80386.1; -; Genomic_DNA.
DR EMBL; CH471142; EAW80388.1; -; Genomic_DNA.
DR EMBL; CH471142; EAW80389.1; -; Genomic_DNA.
DR EMBL; BC002920; AAH02920.1; -; mRNA.
DR EMBL; BC093016; AAH93016.1; -; mRNA.
DR CCDS; CCDS44448.1; -. [Q8NG11-3]
DR CCDS; CCDS7369.1; -. [Q8NG11-1]
DR RefSeq; NP_001121781.1; NM_001128309.1. [Q8NG11-3]
DR RefSeq; NP_112189.2; NM_030927.2. [Q8NG11-1]
DR RefSeq; XP_006718055.1; XM_006717992.3.
DR RefSeq; XP_011538524.1; XM_011540222.2.
DR RefSeq; XP_016872196.1; XM_017016707.1.
DR RefSeq; XP_016872197.1; XM_017016708.1.
DR RefSeq; XP_016872198.1; XM_017016709.1.
DR RefSeq; XP_016872199.1; XM_017016710.1.
DR RefSeq; XP_016872200.1; XM_017016711.1.
DR AlphaFoldDB; Q8NG11; -.
DR SMR; Q8NG11; -.
DR BioGRID; 123554; 11.
DR IntAct; Q8NG11; 15.
DR MINT; Q8NG11; -.
DR STRING; 9606.ENSP00000396270; -.
DR TCDB; 8.A.40.1.21; the tetraspanin (tetraspanin) family.
DR GlyGen; Q8NG11; 1 site.
DR iPTMnet; Q8NG11; -.
DR PhosphoSitePlus; Q8NG11; -.
DR SwissPalm; Q8NG11; -.
DR BioMuta; TSPAN14; -.
DR DMDM; 55976537; -.
DR CPTAC; CPTAC-1188; -.
DR EPD; Q8NG11; -.
DR jPOST; Q8NG11; -.
DR MassIVE; Q8NG11; -.
DR MaxQB; Q8NG11; -.
DR PaxDb; Q8NG11; -.
DR PeptideAtlas; Q8NG11; -.
DR PRIDE; Q8NG11; -.
DR ProteomicsDB; 73407; -. [Q8NG11-1]
DR ProteomicsDB; 73408; -. [Q8NG11-2]
DR ProteomicsDB; 73409; -. [Q8NG11-3]
DR Antibodypedia; 3113; 64 antibodies from 21 providers.
DR DNASU; 81619; -.
DR Ensembl; ENST00000372156.5; ENSP00000361229.1; ENSG00000108219.15. [Q8NG11-1]
DR Ensembl; ENST00000372158.6; ENSP00000361231.1; ENSG00000108219.15. [Q8NG11-1]
DR Ensembl; ENST00000372164.7; ENSP00000361237.3; ENSG00000108219.15. [Q8NG11-2]
DR Ensembl; ENST00000429989.7; ENSP00000396270.2; ENSG00000108219.15. [Q8NG11-1]
DR Ensembl; ENST00000481124.5; ENSP00000418195.1; ENSG00000108219.15. [Q8NG11-3]
DR Ensembl; ENST00000616406.1; ENSP00000480263.1; ENSG00000108219.15. [Q8NG11-2]
DR GeneID; 81619; -.
DR KEGG; hsa:81619; -.
DR MANE-Select; ENST00000429989.8; ENSP00000396270.2; NM_030927.4; NP_112189.2.
DR UCSC; uc001kci.5; human. [Q8NG11-1]
DR CTD; 81619; -.
DR DisGeNET; 81619; -.
DR GeneCards; TSPAN14; -.
DR HGNC; HGNC:23303; TSPAN14.
DR HPA; ENSG00000108219; Low tissue specificity.
DR neXtProt; NX_Q8NG11; -.
DR OpenTargets; ENSG00000108219; -.
DR PharmGKB; PA128394731; -.
DR VEuPathDB; HostDB:ENSG00000108219; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000159235; -.
DR InParanoid; Q8NG11; -.
DR OMA; YRYSSAE; -.
DR OrthoDB; 1180379at2759; -.
DR PhylomeDB; Q8NG11; -.
DR TreeFam; TF313002; -.
DR PathwayCommons; Q8NG11; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; Q8NG11; -.
DR BioGRID-ORCS; 81619; 12 hits in 1083 CRISPR screens.
DR ChiTaRS; TSPAN14; human.
DR GenomeRNAi; 81619; -.
DR Pharos; Q8NG11; Tdark.
DR PRO; PR:Q8NG11; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8NG11; protein.
DR Bgee; ENSG00000108219; Expressed in cortical plate and 186 other tissues.
DR ExpressionAtlas; Q8NG11; baseline and differential.
DR Genevisible; Q8NG11; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
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:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP: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; 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; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..270
FT /note="Tetraspanin-14"
FT /id="PRO_0000219261"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..61
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..232
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 114..232
FT /note="Necessary and sufficient for interaction with
FT ADAM10"
FT /evidence="ECO:0000269|PubMed:26668317"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 28..150
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043194"
FT VAR_SEQ 28..44
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011878"
FT CONFLICT 143
FT /note="L -> V (in Ref. 2; CAB66573)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="H -> R (in Ref. 2; CAB66573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 30691 MW; C74D64CDC52DF107 CRC64;
MHYYRYSNAK VSCWYKYLLF SYNIIFWLAG VVFLGVGLWA WSEKGVLSDL TKVTRMHGID
PVVLVLMVGV VMFTLGFAGC VGALRENICL LNFFCGTIVL IFFLELAVAV LAFLFQDWVR
DRFREFFESN IKSYRDDIDL QNLIDSLQKA NQCCGAYGPE DWDLNVYFNC SGASYSREKC
GVPFSCCVPD PAQKVVNTQC GYDVRIQLKS KWDESIFTKG CIQALESWLP RNIYIVAGVF
IAISLLQIFG IFLARTLISD IEAVKAGHHF
