RELL2_MOUSE
ID RELL2_MOUSE Reviewed; 303 AA.
AC Q8BRJ3;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=RELT-like protein 2;
GN Name=Rell2;
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=Brain cortex;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Induces activation of MAPK14/p38 cascade, when overexpressed.
CC Induces apoptosis, when overexpressed. {ECO:0000250|UniProtKB:Q8NC24}.
CC -!- SUBUNIT: Interacts with RELT, RELL1, OXSR1, PLSCR1 AND TRAF2.
CC {ECO:0000250|UniProtKB:Q8NC24}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NC24};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q8NC24}.
CC -!- SIMILARITY: Belongs to the RELT family. {ECO:0000305}.
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DR EMBL; AK044097; BAC31774.1; -; mRNA.
DR CCDS; CCDS29195.2; -.
DR RefSeq; NP_722488.2; NM_153793.2.
DR RefSeq; XP_006525925.1; XM_006525862.1.
DR AlphaFoldDB; Q8BRJ3; -.
DR SMR; Q8BRJ3; -.
DR STRING; 10090.ENSMUSP00000070280; -.
DR iPTMnet; Q8BRJ3; -.
DR PhosphoSitePlus; Q8BRJ3; -.
DR MaxQB; Q8BRJ3; -.
DR PaxDb; Q8BRJ3; -.
DR PRIDE; Q8BRJ3; -.
DR ProteomicsDB; 253204; -.
DR Antibodypedia; 53224; 66 antibodies from 14 providers.
DR Ensembl; ENSMUST00000070709; ENSMUSP00000070280; ENSMUSG00000044024.
DR Ensembl; ENSMUST00000176104; ENSMUSP00000135556; ENSMUSG00000044024.
DR Ensembl; ENSMUST00000177058; ENSMUSP00000135615; ENSMUSG00000044024.
DR GeneID; 225392; -.
DR KEGG; mmu:225392; -.
DR UCSC; uc008ern.2; mouse.
DR CTD; 285613; -.
DR MGI; MGI:1918044; Rell2.
DR VEuPathDB; HostDB:ENSMUSG00000044024; -.
DR eggNOG; ENOG502RZW4; Eukaryota.
DR GeneTree; ENSGT00940000160541; -.
DR InParanoid; Q8BRJ3; -.
DR OMA; RIVQCII; -.
DR OrthoDB; 1464869at2759; -.
DR PhylomeDB; Q8BRJ3; -.
DR TreeFam; TF332339; -.
DR BioGRID-ORCS; 225392; 5 hits in 74 CRISPR screens.
DR PRO; PR:Q8BRJ3; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BRJ3; protein.
DR Bgee; ENSMUSG00000044024; Expressed in primary visual cortex and 110 other tissues.
DR ExpressionAtlas; Q8BRJ3; baseline and differential.
DR Genevisible; Q8BRJ3; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005518; F:collagen binding; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:UniProtKB.
DR InterPro; IPR042313; RELL2.
DR InterPro; IPR022248; TNF_rcpt_RELT.
DR PANTHER; PTHR31481; PTHR31481; 1.
DR Pfam; PF12606; RELT; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..303
FT /note="RELT-like protein 2"
FT /id="PRO_0000249846"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 303 AA; 32326 MW; 06287A05AA64793B CRC64;
MSEPQPDLEP PQHGLYMLFL LVLVFFLMGL VGFMICHVLK KKGYRCRTSR GSEPDDAQLQ
PPEDDDVNED TVERIVRCII QNEANAEALK EMLGDSEGEG TVQLSSVDAT SSLQDGAPSH
HHTVHLGSAA PCIHCSRSKR PPLVRQGRSK EGKSRPRPGE TTVFSVGRFR VTHIEKRYGL
HEHRDGSPTD RSWGSGGGQE PGGSQAAGGG QPRTGTAAIE RLLPEPPPSQ AAATHSVQNG
RLQDASLVPC TLEGTPGTSA ELNLGPRGRD PSPGLSSQEA NGQPTKLDTS GQQESLPPEA
GGM
