TSN14_MOUSE
ID TSN14_MOUSE Reviewed; 270 AA.
AC Q8QZY6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Tetraspanin-14;
DE Short=Tspan-14;
DE AltName: Full=Transmembrane 4 superfamily member 14;
GN Name=Tspan14; Synonyms=D14Ertd226e, Tm4sf14;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PROTEIN SEQUENCE OF 6-16, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, 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).
RN [5]
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 [6]
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). Negatively
CC regulates ADAM10-mediated cleavage of GP6 (PubMed:26668317). Promotes
CC ADAM10-mediated cleavage of CDH5 (PubMed:23035126).
CC {ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}.
CC -!- SUBUNIT: Interacts with ADAM10; the interaction promotes ADAM10
CC maturation and cell surface expression. {ECO:0000269|PubMed:23035126,
CC ECO:0000269|PubMed:26668317}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NG11};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; AK030593; BAC27035.1; -; mRNA.
DR EMBL; BC024611; AAH24611.1; -; mRNA.
DR EMBL; BC025568; AAH25568.1; -; mRNA.
DR EMBL; BC026574; AAH26574.1; -; mRNA.
DR CCDS; CCDS26956.1; -.
DR RefSeq; NP_001303677.1; NM_001316748.1.
DR RefSeq; NP_666040.1; NM_145928.2.
DR RefSeq; XP_006519324.1; XM_006519261.1.
DR AlphaFoldDB; Q8QZY6; -.
DR SMR; Q8QZY6; -.
DR IntAct; Q8QZY6; 1.
DR MINT; Q8QZY6; -.
DR STRING; 10090.ENSMUSP00000035263; -.
DR GlyGen; Q8QZY6; 1 site.
DR iPTMnet; Q8QZY6; -.
DR PhosphoSitePlus; Q8QZY6; -.
DR SwissPalm; Q8QZY6; -.
DR EPD; Q8QZY6; -.
DR jPOST; Q8QZY6; -.
DR MaxQB; Q8QZY6; -.
DR PaxDb; Q8QZY6; -.
DR PeptideAtlas; Q8QZY6; -.
DR PRIDE; Q8QZY6; -.
DR ProteomicsDB; 298147; -.
DR Antibodypedia; 3113; 64 antibodies from 21 providers.
DR DNASU; 52588; -.
DR Ensembl; ENSMUST00000047652; ENSMUSP00000035263; ENSMUSG00000037824.
DR Ensembl; ENSMUST00000224209; ENSMUSP00000153208; ENSMUSG00000037824.
DR GeneID; 52588; -.
DR KEGG; mmu:52588; -.
DR UCSC; uc007tcg.1; mouse.
DR CTD; 81619; -.
DR MGI; MGI:1196325; Tspan14.
DR VEuPathDB; HostDB:ENSMUSG00000037824; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000159235; -.
DR HOGENOM; CLU_055524_0_2_1; -.
DR InParanoid; Q8QZY6; -.
DR OMA; YRYSSAE; -.
DR OrthoDB; 1180379at2759; -.
DR PhylomeDB; Q8QZY6; -.
DR TreeFam; TF313002; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 52588; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tspan14; mouse.
DR PRO; PR:Q8QZY6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8QZY6; protein.
DR Bgee; ENSMUSG00000037824; Expressed in placenta labyrinth and 243 other tissues.
DR Genevisible; Q8QZY6; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
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 Cell membrane; Direct protein sequencing; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..270
FT /note="Tetraspanin-14"
FT /id="PRO_0000219262"
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:0000250|UniProtKB:Q8NG11"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 270 AA; 30674 MW; 814DF8AF38E360CB CRC64;
MHYYRYSNAE VSCWYKYLLF SYNIVFWLAG VVFLGVGLWA WSEKGVLSDL TKVTRLHGID
PVVLVLMVGV VMFTLGFAGC VGALRENICL LKFFCGAIVL IFFLELAVAV LAFLFQDWVR
DRFREFFESN IKSYRDDIDL QNLIDSLQKA NQCCGAYGPE DWDLNVYFNC SGASYSREKC
GVPFSCCVPD PAQKVVNTQC GYDVRIQLKS KWDEFIFTKG CIQALEGWLP RNIYIVAGVF
IAISLLQIFG IFLARTLISD IEAVKAGHHF
