TR19L_MOUSE
ID TR19L_MOUSE Reviewed; 436 AA.
AC Q8BX43; Q497Z8; Q8BTV0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 19L;
DE Flags: Precursor;
GN Name=Relt; Synonyms=Tnfrsf19l;
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, and NOD; TISSUE=Cerebellum, and Thymus;
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 TISSUE=Brain, and Thyroid;
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 TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION, AND MUTAGENESIS OF
RP 396-PRO--ILE-436.
RX PubMed=30506946; DOI=10.1111/cge.13487;
RA Kim J.W., Zhang H., Seymen F., Koruyucu M., Hu Y., Kang J., Kim Y.J.,
RA Ikeda A., Kasimoglu Y., Bayram M., Zhang C., Kawasaki K., Bartlett J.D.,
RA Saunders T.L., Simmer J.P., Hu J.C.;
RT "Mutations in RELT cause autosomal recessive amelogenesis imperfecta.";
RL Clin. Genet. 95:375-383(2019).
CC -!- FUNCTION: May play a role in apoptosis. Induces activation of
CC MAPK14/p38 and MAPK8/JNK MAPK cascades, when overexpressed. Involved in
CC dental enamel formation (PubMed:30506946).
CC {ECO:0000250|UniProtKB:Q969Z4, ECO:0000269|PubMed:30506946}.
CC -!- SUBUNIT: Interacts with RELL1, RELL2, OXSR1, PLSCR1 and STK39.
CC {ECO:0000250|UniProtKB:Q969Z4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q969Z4};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q969Z4}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q969Z4}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q969Z4}.
CC -!- TISSUE SPECIFICITY: Expressed in the teeth.
CC {ECO:0000269|PubMed:30506946}.
CC -!- DEVELOPMENTAL STAGE: Expressed by secretory stage ameloblasts and by
CC odontoblasts at postnatal day 5. It is not detected in maturation stage
CC ameloblasts and only residual expression is observed in odontoblasts by
CC postnatal day 12. {ECO:0000269|PubMed:30506946}.
CC -!- PTM: Phosphorylated in vitro by OXSR1. Phosphorylated by STK39.
CC {ECO:0000250|UniProtKB:Q969Z4}.
CC -!- SIMILARITY: Belongs to the RELT family. {ECO:0000305}.
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DR EMBL; AK049073; BAC33534.1; -; mRNA.
DR EMBL; AK088621; BAC40459.1; -; mRNA.
DR EMBL; BC100310; AAI00311.1; -; mRNA.
DR EMBL; BC131929; AAI31930.1; -; mRNA.
DR EMBL; BC131931; AAI31932.1; -; mRNA.
DR EMBL; BC145200; AAI45201.1; -; mRNA.
DR CCDS; CCDS21506.1; -.
DR RefSeq; NP_796047.2; NM_177073.6.
DR RefSeq; XP_006507994.1; XM_006507931.3.
DR RefSeq; XP_006507995.1; XM_006507932.3.
DR RefSeq; XP_006507996.1; XM_006507933.2.
DR RefSeq; XP_006507997.1; XM_006507934.3.
DR RefSeq; XP_006507998.1; XM_006507935.3.
DR RefSeq; XP_006507999.1; XM_006507936.3.
DR AlphaFoldDB; Q8BX43; -.
DR STRING; 10090.ENSMUSP00000008462; -.
DR GlyGen; Q8BX43; 1 site.
DR iPTMnet; Q8BX43; -.
DR PhosphoSitePlus; Q8BX43; -.
DR EPD; Q8BX43; -.
DR MaxQB; Q8BX43; -.
DR PaxDb; Q8BX43; -.
DR PRIDE; Q8BX43; -.
DR ProteomicsDB; 297516; -.
DR Antibodypedia; 30960; 378 antibodies from 32 providers.
DR DNASU; 320100; -.
DR Ensembl; ENSMUST00000008462; ENSMUSP00000008462; ENSMUSG00000008318.
DR GeneID; 320100; -.
DR KEGG; mmu:320100; -.
DR UCSC; uc009int.2; mouse.
DR CTD; 84957; -.
DR MGI; MGI:2443373; Relt.
DR VEuPathDB; HostDB:ENSMUSG00000008318; -.
DR eggNOG; ENOG502QVCC; Eukaryota.
DR GeneTree; ENSGT00940000160350; -.
DR HOGENOM; CLU_058936_0_0_1; -.
DR InParanoid; Q8BX43; -.
DR OMA; AEEVQCQ; -.
DR OrthoDB; 672843at2759; -.
DR PhylomeDB; Q8BX43; -.
DR TreeFam; TF332339; -.
DR BioGRID-ORCS; 320100; 7 hits in 76 CRISPR screens.
DR PRO; PR:Q8BX43; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BX43; protein.
DR Bgee; ENSMUSG00000008318; Expressed in granulocyte and 70 other tissues.
DR ExpressionAtlas; Q8BX43; baseline and differential.
DR Genevisible; Q8BX43; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097186; P:amelogenesis; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR CDD; cd13419; TNFRSF19L; 1.
DR InterPro; IPR022248; TNF_rcpt_RELT.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR022333; TNFR_19-like.
DR InterPro; IPR034048; TNFRSF19L_N.
DR PANTHER; PTHR47397; PTHR47397; 1.
DR Pfam; PF12606; RELT; 1.
DR PRINTS; PR01970; TNFACTORR19L.
DR SMART; SM00208; TNFR; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..436
FT /note="Tumor necrosis factor receptor superfamily member
FT 19L"
FT /id="PRO_0000034601"
FT TOPO_DOM 32..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 57..97
FT /note="TNFR-Cys"
FT REGION 123..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 355..358
FT /note="RFRV motif; mediates interaction with STK39"
FT /evidence="ECO:0000250|UniProtKB:Q969Z4"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q969Z4"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..72
FT /evidence="ECO:0000250"
FT DISULFID 78..97
FT /evidence="ECO:0000250"
FT MUTAGEN 396..436
FT /note="Missing: Enamel of mutant mice has a rough surface
FT and is hypomineralized."
FT /evidence="ECO:0000269|PubMed:30506946"
FT CONFLICT 39
FT /note="C -> G (in Ref. 1; BAC33534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 46518 MW; E61304480DBA0815 CRC64;
MSLQGLMMKR TLLCWPLSCL FVLLPWPLAT PTPITPWLCP PGKEPDPDPG QGTLCRTCPP
GTFSASWNSY PCQPHYRCSL QKRLEAQAGT ATHDTMCGDC QHGWFGPQGV PHVPCQPCSK
APPSTGGCDE SGRRGRRGVE VAAGTSSNGE PRQPGNGTRA GGPEETAAQY AVIAIVPVFC
LMGLLGILVC NLLKRKGYHC TAQKEVGPSP GGGGSGINPA YRTEDANEDT IGVLVRLITE
KKENAAALEE LLKEYHSKQL VQTSHRPVPR LLPASPSIPH ICPHHHHLHT VQGLASLSGP
CCSRCSQKWP EVLLSPEAAA ATTPAPTLLP TASRAPKASA KPGRQGEITI LSVGRFRVAR
IPEQRTSSLL SEVKTITEAG PSEGDLPDSP QPGLPPEQRA LLGSGGSHTK WLKPPAENKA
EENRYVVRLS ESNLVI
