TMM79_MOUSE
ID TMM79_MOUSE Reviewed; 391 AA.
AC Q9D709;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Transmembrane protein 79;
DE AltName: Full=Mattrin;
GN Name=Tmem79; Synonyms=Matt;
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=Tongue;
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=129; 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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24060273; DOI=10.1016/j.jaci.2013.08.027;
RA Sasaki T., Shiohama A., Kubo A., Kawasaki H., Ishida-Yamamoto A.,
RA Yamada T., Hachiya T., Shimizu A., Okano H., Kudoh J., Amagai M.;
RT "A homozygous nonsense mutation in the gene for Tmem79, a component for the
RT lamellar granule secretory system, produces spontaneous eczema in an
RT experimental model of atopic dermatitis.";
RL J. Allergy Clin. Immunol. 132:1111-1120(2013).
RN [4]
RP INVOLVEMENT IN ATOPIC DERMATITIS, AND TISSUE SPECIFICITY.
RX PubMed=24084074; DOI=10.1016/j.jaci.2013.08.046;
RA Saunders S.P., Goh C.S., Brown S.J., Palmer C.N., Porter R.M., Cole C.,
RA Campbell L.E., Gierlinski M., Barton G.J., Schneider G., Balmain A.,
RA Prescott A.R., Weidinger S., Baurecht H., Kabesch M., Gieger C., Lee Y.A.,
RA Tavendale R., Mukhopadhyay S., Turner S.W., Madhok V.B., Sullivan F.M.,
RA Relton C., Burn J., Meggitt S., Smith C.H., Allen M.A., Barker J.N.,
RA Reynolds N.J., Cordell H.J., Irvine A.D., McLean W.H., Sandilands A.,
RA Fallon P.G.;
RT "Tmem79/Matt is the matted mouse gene and is a predisposing gene for atopic
RT dermatitis in human subjects.";
RL J. Allergy Clin. Immunol. 132:1121-1129(2013).
CC -!- FUNCTION: Contributes to the epidermal integrity and skin barrier
CC function. Plays a role in the lamellar granule (LG) secretory system
CC and in the stratum corneum (SC) epithelial cell formation.
CC {ECO:0000269|PubMed:24060273}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:24060273}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:24060273}. Membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC Note=Colocalized with TGOLN2 in the trans-Golgi network. Colocalized
CC with LAMP1 in the lysosome.
CC -!- TISSUE SPECIFICITY: Expressed in the epidermis of the skin. Expressed
CC in epithelial cells of the outermost layer of the stratum granulosum
CC (SG) and in hair follicles (at protein level).
CC {ECO:0000269|PubMed:24060273, ECO:0000269|PubMed:24084074}.
CC -!- DISEASE: Note=Defects in Tmem79 are the cause of the spontaneous matted
CC (matt) mutant phenotype, a model for human atopic dermatitis. Atopic
CC dermatitis (ma/ma) mice have a matted hair phenotype with progressive
CC dermatitis-like skin inflammation and a scratching behavior. Mice
CC display an altered skin barrier that facilitates allergic
CC sensitization. {ECO:0000269|PubMed:24084074}.
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DR EMBL; AK009760; BAB26484.1; -; mRNA.
DR EMBL; BC003309; AAH03309.1; -; mRNA.
DR CCDS; CCDS17470.1; -.
DR RefSeq; NP_077208.1; NM_024246.5.
DR RefSeq; XP_006502187.1; XM_006502124.2.
DR RefSeq; XP_006502188.1; XM_006502125.2.
DR AlphaFoldDB; Q9D709; -.
DR STRING; 10090.ENSMUSP00000001456; -.
DR iPTMnet; Q9D709; -.
DR PhosphoSitePlus; Q9D709; -.
DR PaxDb; Q9D709; -.
DR PRIDE; Q9D709; -.
DR ProteomicsDB; 259590; -.
DR Antibodypedia; 34211; 86 antibodies from 19 providers.
DR Ensembl; ENSMUST00000001456; ENSMUSP00000001456; ENSMUSG00000001420.
DR Ensembl; ENSMUST00000107552; ENSMUSP00000103176; ENSMUSG00000001420.
DR Ensembl; ENSMUST00000107553; ENSMUSP00000103177; ENSMUSG00000001420.
DR GeneID; 71913; -.
DR KEGG; mmu:71913; -.
DR UCSC; uc008puq.1; mouse.
DR CTD; 84283; -.
DR MGI; MGI:1919163; Tmem79.
DR VEuPathDB; HostDB:ENSMUSG00000001420; -.
DR eggNOG; ENOG502QVUB; Eukaryota.
DR GeneTree; ENSGT00390000002390; -.
DR HOGENOM; CLU_062246_1_0_1; -.
DR InParanoid; Q9D709; -.
DR OMA; YYMFLVE; -.
DR OrthoDB; 963760at2759; -.
DR PhylomeDB; Q9D709; -.
DR TreeFam; TF333310; -.
DR BioGRID-ORCS; 71913; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Tmem79; mouse.
DR PRO; PR:Q9D709; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D709; protein.
DR Bgee; ENSMUSG00000001420; Expressed in lumbar dorsal root ganglion and 118 other tissues.
DR ExpressionAtlas; Q9D709; baseline and differential.
DR Genevisible; Q9D709; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070268; P:cornification; IMP:MGI.
DR GO; GO:0042335; P:cuticle development; IMP:MGI.
DR GO; GO:0002070; P:epithelial cell maturation; IMP:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0045684; P:positive regulation of epidermis development; IMP:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Golgi apparatus; Lysosome; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..391
FT /note="Transmembrane protein 79"
FT /id="PRO_0000254119"
FT TOPO_DOM 1..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..391
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 43464 MW; 2B2E83DA66BAB27F CRC64;
MTEPETLALL DMKEPETPEK SPPQALVLQS EEEGGTESPG TESLRVGSSV GSPIVREGPE
DGPDSTISEA ATLPWGTDPH PSAPLPDPPG WRDIEPEPLE SEAPTKSEEP FKEDANLLPE
KTVRAFVPID LQCIERKPQE ERILHRDAGP GELRNFLPAR LSHPEPPERK WAEAVVRPPG
RSCGGCGSCG GREALRAVAS VVAALIFFPC LLYGAYAFLP FDAPRLPTMS SRLVYTLRCG
VFATFPIVLG LLVYGLSLLC FSALRPFGEP RREVEIHRQY VAQSVQLFIL YFFNLAVLST
YLPQDTLKLL PLLTGLFAIS RLIYWLTFAV GRSFRGFGYG LTFLPLLAML VWNLYYMFVV
EPERMLTASE SRLDYPDHAR SVSDYRPRSW G
