RELL1_HUMAN
ID RELL1_HUMAN Reviewed; 271 AA.
AC Q8IUW5; Q8NBK1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=RELT-like protein 1;
DE Flags: Precursor;
GN Name=RELL1; ORFNames=PSEC0162;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RELT; RELL2 AND
RP OXSR1, AND PHOSPHORYLATION.
RX PubMed=16389068; DOI=10.1016/j.bbrc.2005.12.033;
RA Cusick J.K., Xu L.-G., Bin L.-H., Han K.-J., Shu H.-B.;
RT "Identification of RELT homologues that associate with RELT and are
RT phosphorylated by OSR1.";
RL Biochem. Biophys. Res. Commun. 340:535-543(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP FUNCTION.
RX PubMed=19969290; DOI=10.1016/j.cellimm.2009.10.013;
RA Cusick J.K., Mustian A., Goldberg K., Reyland M.E.;
RT "RELT induces cellular death in HEK 293 epithelial cells.";
RL Cell. Immunol. 261:1-8(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-114, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP INTERACTION WITH PLSCR1.
RX PubMed=22052202; DOI=10.1007/s11010-011-1127-4;
RA Cusick J.K., Mustian A., Jacobs A.T., Reyland M.E.;
RT "Identification of PLSCR1 as a protein that interacts with RELT family
RT members.";
RL Mol. Cell. Biochem. 362:55-63(2012).
RN [9]
RP FUNCTION.
RX PubMed=28688764; DOI=10.1016/j.bbrc.2017.07.022;
RA Moua P., Checketts M., Xu L.G., Shu H.B., Reyland M.E., Cusick J.K.;
RT "RELT family members activate p38 and induce apoptosis by a mechanism
RT distinct from TNFR1.";
RL Biochem. Biophys. Res. Commun. 491:25-32(2017).
CC -!- FUNCTION: Induces activation of MAPK14/p38 cascade, when overexpressed
CC (PubMed:28688764). Induces apoptosis, when overexpressed
CC (PubMed:19969290). {ECO:0000269|PubMed:19969290,
CC ECO:0000269|PubMed:28688764}.
CC -!- SUBUNIT: Interacts with RELT, RELL2 and OXSR1 (PubMed:16389068).
CC Interacts with PLSCR1 (PubMed:22052202). {ECO:0000269|PubMed:16389068,
CC ECO:0000269|PubMed:22052202}.
CC -!- INTERACTION:
CC Q8IUW5; Q9NSU2-1: TREX1; NbExp=3; IntAct=EBI-11343385, EBI-16746122;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16389068};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16389068}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at highest levels in
CC the placenta, skeletal muscle, spleen and testis.
CC {ECO:0000269|PubMed:16389068}.
CC -!- PTM: Phosphorylated in vitro by OXSR1. {ECO:0000269|PubMed:16389068}.
CC -!- SIMILARITY: Belongs to the RELT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK075468; BAC11638.1; -; mRNA.
DR EMBL; CH471069; EAW92885.1; -; Genomic_DNA.
DR EMBL; BC039540; AAH39540.1; -; mRNA.
DR CCDS; CCDS43221.1; -.
DR RefSeq; NP_001078868.1; NM_001085399.1.
DR RefSeq; NP_001078869.1; NM_001085400.1.
DR AlphaFoldDB; Q8IUW5; -.
DR BioGRID; 612841; 70.
DR IntAct; Q8IUW5; 26.
DR MINT; Q8IUW5; -.
DR STRING; 9606.ENSP00000398778; -.
DR GlyGen; Q8IUW5; 2 sites.
DR iPTMnet; Q8IUW5; -.
DR PhosphoSitePlus; Q8IUW5; -.
DR SwissPalm; Q8IUW5; -.
DR BioMuta; RELL1; -.
DR DMDM; 74727997; -.
DR EPD; Q8IUW5; -.
DR jPOST; Q8IUW5; -.
DR MassIVE; Q8IUW5; -.
DR MaxQB; Q8IUW5; -.
DR PaxDb; Q8IUW5; -.
DR PeptideAtlas; Q8IUW5; -.
DR PRIDE; Q8IUW5; -.
DR ProteomicsDB; 70617; -.
DR Antibodypedia; 2874; 10 antibodies from 7 providers.
DR DNASU; 768211; -.
DR Ensembl; ENST00000314117.8; ENSP00000313385.4; ENSG00000181826.10.
DR Ensembl; ENST00000454158.7; ENSP00000398778.2; ENSG00000181826.10.
DR GeneID; 768211; -.
DR KEGG; hsa:768211; -.
DR MANE-Select; ENST00000454158.7; ENSP00000398778.2; NM_001085400.2; NP_001078869.1.
DR UCSC; uc003gsz.3; human.
DR CTD; 768211; -.
DR DisGeNET; 768211; -.
DR GeneCards; RELL1; -.
DR HGNC; HGNC:27379; RELL1.
DR HPA; ENSG00000181826; Tissue enhanced (brain).
DR MIM; 611212; gene.
DR neXtProt; NX_Q8IUW5; -.
DR OpenTargets; ENSG00000181826; -.
DR PharmGKB; PA162401054; -.
DR VEuPathDB; HostDB:ENSG00000181826; -.
DR eggNOG; ENOG502R0TD; Eukaryota.
DR GeneTree; ENSGT00940000159709; -.
DR HOGENOM; CLU_084225_0_0_1; -.
DR InParanoid; Q8IUW5; -.
DR OMA; KNICTRC; -.
DR OrthoDB; 1464869at2759; -.
DR PhylomeDB; Q8IUW5; -.
DR TreeFam; TF332339; -.
DR PathwayCommons; Q8IUW5; -.
DR SignaLink; Q8IUW5; -.
DR BioGRID-ORCS; 768211; 7 hits in 1075 CRISPR screens.
DR ChiTaRS; RELL1; human.
DR GenomeRNAi; 768211; -.
DR Pharos; Q8IUW5; Tbio.
DR PRO; PR:Q8IUW5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8IUW5; protein.
DR Bgee; ENSG00000181826; Expressed in germinal epithelium of ovary and 194 other tissues.
DR ExpressionAtlas; Q8IUW5; baseline and differential.
DR Genevisible; Q8IUW5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:UniProtKB.
DR InterPro; IPR042315; RELL1.
DR InterPro; IPR022248; TNF_rcpt_RELT.
DR PANTHER; PTHR31037; PTHR31037; 1.
DR Pfam; PF12606; RELT; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..271
FT /note="RELT-like protein 1"
FT /id="PRO_0000323590"
FT TOPO_DOM 24..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 28..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..113
FT /evidence="ECO:0000255"
FT COMPBIAS 151..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 36
FT /note="T -> A (in Ref. 1; BAC11638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 29340 MW; D85AAA0E86349EA7 CRC64;
MAPRALPGSA VLAAAVFVGG AVSSPLVAPD NGSSRTLHSR TETTPSPSND TGNGHPEYIA
YALVPVFFIM GLFGVLICHL LKKKGYRCTT EAEQDIEEEK VEKIELNDSV NENSDTVGQI
VHYIMKNEAN ADVLKAMVAD NSLYDPESPV TPSTPGSPPV SPGPLSPGGT PGKHVCGHHL
HTVGGVVERD VCHRCRHKRW HFIKPTNKSR ESRPRRQGEV TVLSVGRFRV TKVEHKSNQK
ERRSLMSVSG AETVNGEVPA TPVKRERSGT E
