RELL2_HUMAN
ID RELL2_HUMAN Reviewed; 303 AA.
AC Q8NC24; D3DQE2; Q6P4E7; Q6UXY2;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=RELT-like protein 2;
GN Name=RELL2; Synonyms=C5orf16; ORFNames=UNQ9423/PRO34565;
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 MRNA], AND VARIANTS ILE-133; ARG-196 AND
RP GLU-283.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-128; ILE-133;
RP ARG-196 AND GLU-283.
RC TISSUE=Blood;
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RELT; RELL1 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 [6]
RP FUNCTION, AND INTERACTION WITH TRAF2.
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 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 [8]
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, RELL1 and OXSR1 (PubMed:16389068).
CC Interacts with PLSCR1 (PubMed:22052202). Interacts with TRAF2
CC (PubMed:19969290). {ECO:0000269|PubMed:16389068,
CC ECO:0000269|PubMed:19969290, ECO:0000269|PubMed:22052202}.
CC -!- INTERACTION:
CC Q8NC24; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-10269209, EBI-12109402;
CC Q8NC24; Q12797-6: ASPH; NbExp=3; IntAct=EBI-10269209, EBI-12092171;
CC Q8NC24; O14735: CDIPT; NbExp=3; IntAct=EBI-10269209, EBI-358858;
CC Q8NC24; Q8NHS1: CLDND2; NbExp=3; IntAct=EBI-10269209, EBI-11959453;
CC Q8NC24; P29400-2: COL4A5; NbExp=3; IntAct=EBI-10269209, EBI-12211159;
CC Q8NC24; Q92520: FAM3C; NbExp=3; IntAct=EBI-10269209, EBI-2876774;
CC Q8NC24; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-10269209, EBI-12033434;
CC Q8NC24; P30301: MIP; NbExp=3; IntAct=EBI-10269209, EBI-8449636;
CC Q8NC24; P42857: NSG1; NbExp=3; IntAct=EBI-10269209, EBI-6380741;
CC Q8NC24; O95747: OXSR1; NbExp=7; IntAct=EBI-10269209, EBI-620853;
CC Q8NC24; P60201-2: PLP1; NbExp=3; IntAct=EBI-10269209, EBI-12188331;
CC Q8NC24; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-10269209, EBI-10244780;
CC Q8NC24; O75396: SEC22B; NbExp=3; IntAct=EBI-10269209, EBI-1058865;
CC Q8NC24; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-10269209, EBI-10262251;
CC Q8NC24; P78382: SLC35A1; NbExp=3; IntAct=EBI-10269209, EBI-12870360;
CC Q8NC24; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-10269209, EBI-12188413;
CC Q8NC24; P02786: TFRC; NbExp=3; IntAct=EBI-10269209, EBI-355727;
CC Q8NC24; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-10269209, EBI-12045841;
CC Q8NC24; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-10269209, EBI-12195249;
CC Q8NC24; O95159: ZFPL1; NbExp=3; IntAct=EBI-10269209, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16389068};
CC Single-pass membrane protein {ECO:0000269|PubMed:16389068}.
CC -!- TISSUE SPECIFICITY: Primarily expressed in spleen, thymus, testis,
CC peripheral blood leukocytes, brain and placenta. Not detected in
CC prostate, ovary, small intestine, colon, heart, lung, liver, skeletal
CC muscle, kidney and pancreas. {ECO:0000269|PubMed:16389068}.
CC -!- PTM: Phosphorylated in vitro by OXSR1. {ECO:0000269|PubMed:16389068}.
CC -!- SIMILARITY: Belongs to the RELT family. {ECO:0000305}.
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DR EMBL; AK075064; BAC11380.1; -; mRNA.
DR EMBL; AY358163; AAQ88530.1; -; mRNA.
DR EMBL; CH471062; EAW61911.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61913.1; -; Genomic_DNA.
DR EMBL; BC063469; AAH63469.1; -; mRNA.
DR CCDS; CCDS4265.1; -.
DR RefSeq; NP_001123501.1; NM_001130029.1.
DR RefSeq; NP_776189.3; NM_173828.4.
DR AlphaFoldDB; Q8NC24; -.
DR SMR; Q8NC24; -.
DR BioGRID; 130157; 50.
DR IntAct; Q8NC24; 37.
DR STRING; 9606.ENSP00000297164; -.
DR iPTMnet; Q8NC24; -.
DR PhosphoSitePlus; Q8NC24; -.
DR BioMuta; RELL2; -.
DR DMDM; 74715151; -.
DR MassIVE; Q8NC24; -.
DR PaxDb; Q8NC24; -.
DR PeptideAtlas; Q8NC24; -.
DR PRIDE; Q8NC24; -.
DR ProteomicsDB; 72844; -.
DR Antibodypedia; 53224; 66 antibodies from 14 providers.
DR DNASU; 285613; -.
DR Ensembl; ENST00000297164.8; ENSP00000297164.3; ENSG00000164620.9.
DR Ensembl; ENST00000444782.5; ENSP00000409443.1; ENSG00000164620.9.
DR GeneID; 285613; -.
DR KEGG; hsa:285613; -.
DR MANE-Select; ENST00000297164.8; ENSP00000297164.3; NM_173828.5; NP_776189.3.
DR UCSC; uc003llh.4; human.
DR CTD; 285613; -.
DR GeneCards; RELL2; -.
DR HGNC; HGNC:26902; RELL2.
DR HPA; ENSG00000164620; Tissue enhanced (brain, parathyroid gland).
DR MIM; 611213; gene.
DR neXtProt; NX_Q8NC24; -.
DR OpenTargets; ENSG00000164620; -.
DR PharmGKB; PA162401073; -.
DR VEuPathDB; HostDB:ENSG00000164620; -.
DR eggNOG; ENOG502RZW4; Eukaryota.
DR GeneTree; ENSGT00940000160541; -.
DR HOGENOM; CLU_074130_0_0_1; -.
DR InParanoid; Q8NC24; -.
DR OMA; RIVQCII; -.
DR OrthoDB; 1464869at2759; -.
DR PhylomeDB; Q8NC24; -.
DR TreeFam; TF332339; -.
DR PathwayCommons; Q8NC24; -.
DR SignaLink; Q8NC24; -.
DR BioGRID-ORCS; 285613; 6 hits in 1075 CRISPR screens.
DR ChiTaRS; RELL2; human.
DR GenomeRNAi; 285613; -.
DR Pharos; Q8NC24; Tbio.
DR PRO; PR:Q8NC24; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8NC24; protein.
DR Bgee; ENSG00000164620; Expressed in right frontal lobe and 114 other tissues.
DR ExpressionAtlas; Q8NC24; baseline and differential.
DR Genevisible; Q8NC24; HS.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IBA:GO_Central.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA: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_0000249845"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 46..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..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 276..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BRJ3"
FT VARIANT 128
FT /note="S -> P (in dbSNP:rs17855845)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027496"
FT VARIANT 133
FT /note="L -> I (in dbSNP:rs14251)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_027497"
FT VARIANT 196
FT /note="G -> R (in dbSNP:rs17855844)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_027498"
FT VARIANT 283
FT /note="Q -> E (in dbSNP:rs11742646)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_027499"
SQ SEQUENCE 303 AA; 32405 MW; D43F2C733D91620C CRC64;
MSEPQPDLEP PQHGLYMLFL LVLVFFLMGL VGFMICHVLK KKGYRCRTSR GSEPDDAQLQ
PPEDDDMNED TVERIVRCII QNEANAEALK EMLGDSEGEG TVQLSSVDAT SSLQDGAPSH
HHTVHLGSAA PCLHCSRSKR PPLVRQGRSK EGKSRPRTGE TTVFSVGRFR VTHIEKRYGL
HEHRDGSPTD RSWGSGGGQD PGGGQGSGGG QPKAGMPAME RLPPERPQPQ VLASPPVQNG
GLRDSSLTPR ALEGNPRASA EPTLRAGGRG PSPGLPTQEA NGQPSKPDTS DHQVSLPQGA
GSM
