LYRIC_RAT
ID LYRIC_RAT Reviewed; 581 AA.
AC Q9Z1W6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein 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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Fischer; TISSUE=Bile duct;
RX PubMed=15383321; DOI=10.1016/j.yexcr.2004.06.026;
RA Britt D.E., Yang D.-F., Yang D.-Q., Flanagan D.L., Callanan H., Lim Y.-P.,
RA Lin S.-H., Hixson D.C.;
RT "Identification of a novel protein, LYRIC, localized to tight junctions of
RT polarized epithelial cells.";
RL Exp. Cell Res. 300:134-148(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-425; SER-456 AND
RP SER-567, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Z1W6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z1W6-2; Sequence=VSP_012227;
CC Name=3;
CC IsoId=Q9Z1W6-3; Sequence=VSP_012228;
CC Name=4;
CC IsoId=Q9Z1W6-4; Sequence=VSP_012227, VSP_012228;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in liver,
CC kidney, prostate and small intestine. Not detected in endothelial
CC cells. {ECO:0000269|PubMed:15383321}.
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DR EMBL; AF100421; AAC72405.2; -; mRNA.
DR RefSeq; NP_596889.1; NM_133398.1. [Q9Z1W6-1]
DR AlphaFoldDB; Q9Z1W6; -.
DR IntAct; Q9Z1W6; 5.
DR STRING; 10116.ENSRNOP00000009989; -.
DR iPTMnet; Q9Z1W6; -.
DR PhosphoSitePlus; Q9Z1W6; -.
DR SwissPalm; Q9Z1W6; -.
DR jPOST; Q9Z1W6; -.
DR PaxDb; Q9Z1W6; -.
DR PeptideAtlas; Q9Z1W6; -.
DR PRIDE; Q9Z1W6; -.
DR GeneID; 170910; -.
DR KEGG; rno:170910; -.
DR UCSC; RGD:620992; rat. [Q9Z1W6-1]
DR CTD; 92140; -.
DR RGD; 620992; Mtdh.
DR VEuPathDB; HostDB:ENSRNOG00000006870; -.
DR eggNOG; ENOG502QU7P; Eukaryota.
DR HOGENOM; CLU_034908_0_0_1; -.
DR InParanoid; Q9Z1W6; -.
DR OMA; KNRGSHE; -.
DR OrthoDB; 1432988at2759; -.
DR PhylomeDB; Q9Z1W6; -.
DR TreeFam; TF331350; -.
DR PRO; PR:Q9Z1W6; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000006870; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; Q9Z1W6; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046581; C:intercellular canaliculus; IDA:RGD.
DR GO; GO:0016604; C:nuclear body; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
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:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0070830; P:bicellular tight junction assembly; IEP:RGD.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
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:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
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:RGD.
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; Alternative splicing; Cell junction; Cytoplasm;
KW Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..581
FT /note="Protein LYRIC"
FT /id="PRO_0000084535"
FT TOPO_DOM 1..49
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..581
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 77..221
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 280..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..442
FT /note="Lung-homing for mammary tumors"
FT /evidence="ECO:0000250"
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 280..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
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:0000250|UniProtKB:Q80WJ7"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 477
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 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UE4"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 248..269
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_012227"
FT VAR_SEQ 349..382
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_012228"
SQ SEQUENCE 581 AA; 63969 MW; 9F86534238C3513C CRC64;
MAARSWQDEL AQQAEEGSAR LRELLSVGLG FLRTELGLDL GLEPKRYPSW VILVGTGALG
LLLLFLLGYG WAAACAGARK KRRSPPRKRE EVTPPTPAPE DPAQLKNLRS EEQKKKNRKK
LPEKPKPNGR TVEIPEDEVV RTPRSITAKQ PPETDKKNEK SKKNKKKSKS DAKAVQNSSR
HDGKEVDEGA WETKISHREK RQQRKRDKVL TDSGSLDSTI PGIENTITVT TEQLTTASFP
VGSKKNKGDS HLNVQVSNFK SGKGDSTLQV SSGLNENITV NGGGWSEKSV KLSSQLSAGE
EKWNSVPPAS AGKRKTEQSA WTQDPGDTNA NGKDWGRNWS DRSIFSGIGS TAEPVSQSTT
SDYQWDGSRN QPHIDDEWSG LNGLSSADPS SDWNAPAEEW GNWVDEDRAS LLKSQEPISN
DQKDSDDDKE KGEGALPTGK SKKKKKKKKK QGEDNSITQD TEDLEKDTRE ELPVNTSKAR
PKQEKACSLK TMSTSDPVEV LIKNSQPIKT LPPAISAEPS VTLSKGDSDK SSSQVPPMLQ
DTDKPKSNAK QNSVPPSQTK SETNWESPKQ IKKKKKARRE T
