LYRIC_MOUSE
ID LYRIC_MOUSE Reviewed; 579 AA.
AC Q80WJ7; B2RSG8; Q05CM0; Q3U9F8; Q3UAQ8; Q8BN67; Q8CBT9; Q8CDL0; Q8CGI7;
AC Q9D052;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein LYRIC;
DE AltName: Full=3D3/LYRIC;
DE AltName: Full=Lysine-rich CEACAM1 co-isolated protein;
DE AltName: Full=Metadherin;
DE AltName: Full=Metastasis adhesion protein;
GN Name=Mtdh; Synonyms=Lyric;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Mammary tumor;
RX PubMed=15093543; DOI=10.1016/s1535-6108(04)00079-0;
RA Brown D.M., Ruoslahti E.;
RT "Metadherin, a cell surface protein in breast tumors that mediates lung
RT metastasis.";
RL Cancer Cell 5:365-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=129; TISSUE=Teratocarcinoma;
RX PubMed=14980505; DOI=10.1016/j.yexcr.2003.11.020;
RA Sutherland H.G.E., Lam Y.W., Briers S., Lamond A.I., Bickmore W.A.;
RT "3D3/lyric: a novel transmembrane protein of the endoplasmic reticulum and
RT nuclear envelope, which is also present in the nucleolus.";
RL Exp. Cell Res. 294:94-105(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow macrophage, Embryo, Testis, and Urinary bladder;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, Embryo, and 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-565, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Down-regulates SLC1A2/EAAT2 promoter activity when expressed
CC ectopically. Activates the nuclear factor kappa-B (NF-kappa-B)
CC transcription factor. Promotes anchorage-independent growth of
CC immortalized melanocytes and astrocytes which is a key component in
CC tumor cell expansion. Promotes lung metastasis and also has an effect
CC on bone and brain metastasis, possibly by enhancing the seeding of
CC tumor cells to the target organ endothelium. Induces chemoresistance
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BCCIP, CREBBP/CBP and RELA/p65. {ECO:0000250}.
CC -!- INTERACTION:
CC Q80WJ7; Q78PY7: Snd1; NbExp=4; IntAct=EBI-774530, EBI-529864;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Nucleus membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cell
CC junction, tight junction {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=In
CC epithelial cells, recruited to tight junctions (TJ) during the
CC maturation of the TJ complexes. A nucleolar staining may be due to
CC nuclear targeting of an isoform lacking the transmembrane domain. TNF-
CC alpha causes translocation from the cytoplasm to the nucleus (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In the mammary gland, expressed at the apical
CC surface of epithelial cells lining ducts, as well as in the mammary fat
CC pad. Not detected in the spleen, kidney, lung, or skin; minute amounts
CC seen in the liver. Expressed in Purkinje neurons in the early postnatal
CC and adult cerebellum. Overexpressed in mammary tumors (at protein
CC level). {ECO:0000269|PubMed:15093543}.
CC -!- CAUTION: Was originally thought to be a type II membrane protein but
CC this is inconsistent with the results of multiple phosphorylation
CC studies because this topology would locate the phosphorylation sites in
CC the lumen or extracellularly rather than in the cytoplasm.
CC {ECO:0000305|PubMed:15093543}.
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DR EMBL; AY553638; AAS68097.1; -; mRNA.
DR EMBL; AF501309; AAP30790.1; -; mRNA.
DR EMBL; AK011808; BAB27854.1; -; mRNA.
DR EMBL; AK029915; BAC26673.1; -; mRNA.
DR EMBL; AK035302; BAC29022.1; -; mRNA.
DR EMBL; AK151269; BAE30256.1; -; mRNA.
DR EMBL; AK151810; BAE30709.1; -; mRNA.
DR EMBL; BC023115; AAH23115.1; -; mRNA.
DR EMBL; BC036994; AAH36994.1; -; mRNA.
DR EMBL; BC138858; AAI38859.1; -; mRNA.
DR EMBL; BC138859; AAI38860.1; -; mRNA.
DR CCDS; CCDS27415.1; -.
DR RefSeq; NP_080278.3; NM_026002.4.
DR AlphaFoldDB; Q80WJ7; -.
DR SMR; Q80WJ7; -.
DR BioGRID; 211981; 5.
DR IntAct; Q80WJ7; 4.
DR MINT; Q80WJ7; -.
DR STRING; 10090.ENSMUSP00000022865; -.
DR iPTMnet; Q80WJ7; -.
DR PhosphoSitePlus; Q80WJ7; -.
DR SwissPalm; Q80WJ7; -.
DR EPD; Q80WJ7; -.
DR jPOST; Q80WJ7; -.
DR MaxQB; Q80WJ7; -.
DR PaxDb; Q80WJ7; -.
DR PeptideAtlas; Q80WJ7; -.
DR PRIDE; Q80WJ7; -.
DR ProteomicsDB; 252693; -.
DR TopDownProteomics; Q80WJ7; -.
DR Antibodypedia; 2507; 416 antibodies from 38 providers.
DR DNASU; 67154; -.
DR Ensembl; ENSMUST00000022865; ENSMUSP00000022865; ENSMUSG00000022255.
DR GeneID; 67154; -.
DR KEGG; mmu:67154; -.
DR UCSC; uc007vlh.1; mouse.
DR CTD; 92140; -.
DR MGI; MGI:1914404; Mtdh.
DR VEuPathDB; HostDB:ENSMUSG00000022255; -.
DR eggNOG; ENOG502QU7P; Eukaryota.
DR GeneTree; ENSGT00940000154181; -.
DR HOGENOM; CLU_034908_0_0_1; -.
DR InParanoid; Q80WJ7; -.
DR OMA; KNRGSHE; -.
DR OrthoDB; 1432988at2759; -.
DR PhylomeDB; Q80WJ7; -.
DR TreeFam; TF331350; -.
DR BioGRID-ORCS; 67154; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Mtdh; mouse.
DR PRO; PR:Q80WJ7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80WJ7; protein.
DR Bgee; ENSMUSG00000022255; Expressed in otic placode and 253 other tissues.
DR ExpressionAtlas; Q80WJ7; baseline and differential.
DR Genevisible; Q80WJ7; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046581; C:intercellular canaliculus; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR031402; LYRIC.
DR Pfam; PF15686; LYRIC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..579
FT /note="Protein LYRIC"
FT /id="PRO_0000084534"
FT TOPO_DOM 1..48
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..71
FT /note="Activation of NF-kappa-B"
FT /evidence="ECO:0000250"
FT REGION 72..168
FT /note="Interaction with BCCIP"
FT /evidence="ECO:0000250"
FT REGION 78..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..204
FT /note="Interaction with RELA"
FT /evidence="ECO:0000250"
FT REGION 277..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..440
FT /note="Lung-homing for mammary tumors"
FT COMPBIAS 105..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W6"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 190
FT /note="A -> I (in Ref. 3; BAB27854)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="G -> R (in Ref. 3; BAE30709)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="S -> T (in Ref. 3; BAC26673)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="L -> F (in Ref. 3; BAE30709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 63846 MW; E47E98303F588126 CRC64;
MAARSWQDEL AQQAEEGSAR LRELLSVGLG FLRTELGLDL GLEPKRYPGW VILVGTGALG
LLLLFLLGYG WAAACAGARK KRRSPPRKRE EAAPPTPAPD DLAQLKNLRS EEQKKKNRKK
LPEKPKPNGR TVEVPEDEVV RNPRSITAKQ APETDKKNEK SKKNKKKSKS DAKAVQNSSR
HDGKEVDEGA WETKISHREK RQQRKRDKVL TDSGSLDSTI PGIENIITVT TEQLTTASFP
VGSKKNKGDS HLNVQVSNFK SGKGDSTLQV SSRLNENLTV NGGGWSEKSV KLSSQLSEEK
WNSVPPASAG KRKTEPSAWT QDTGDTNANG KDWGRNWSDR SIFSGIGSTA EPVSQSTTSD
YQWDVSRNQP YIDDEWSGLN GLSSADPSSD WNAPAEEWGN WVDEDRASLL KSQEPISNDQ
KVSDDDKEKG EGALPTGKSK KKKKKKKKQG EDNSHTQDTE DLEKDTREEL PVNTSKARPK
QEKACSLKTM STSDPAEVLI KNSQPVKTLP PAISAEPSIT LSKGDSDNSS SQVPPMLQDT
DKPKSNAKQN SVPPSQTKSE TNWESPKQIK KKKKARRET
