ERLEC_HUMAN
ID ERLEC_HUMAN Reviewed; 483 AA.
AC Q96DZ1; B2RDB4; B5MC72; O95901; Q6UWN7; Q9NUY7; Q9UQL4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Endoplasmic reticulum lectin 1;
DE AltName: Full=ER lectin;
DE Short=Erlectin;
DE AltName: Full=XTP3-transactivated gene B protein;
DE Flags: Precursor;
GN Name=ERLEC1; Synonyms=C2orf30, XTP3TPB; ORFNames=UNQ1878/PRO4321;
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 [MRNA] (ISOFORM 1).
RA Wang C., Cheng J., Lang Z., Wu Y., Yang Y., Zhang L., Ji D.;
RT "Screening and cloning of the target genes transactivated by XTP3 using a
RT suppression subtractive hybridization technique.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Placenta;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-483.
RC TISSUE=Brain;
RA Mei G., Yu W., Gibbs R.A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH KREMEN2,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-379.
RX PubMed=16531414; DOI=10.1074/jbc.m511872200;
RA Cruciat C.-M., Hassler C., Niehrs C.;
RT "The MRH protein Erlectin is a member of the endoplasmic reticulum
RT synexpression group and functions in N-glycan recognition.";
RL J. Biol. Chem. 281:12986-12993(2006).
RN [9]
RP FUNCTION IN ERAD, SUBCELLULAR LOCATION, GLYCOSYLATION, AND INTERACTION WITH
RP HSPA5; OS9; SEL1L AND SYVN1.
RX PubMed=18502753; DOI=10.1074/jbc.m709336200;
RA Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.;
RT "Human XTP3-B forms an endoplasmic reticulum quality control scaffold with
RT the HRD1-SEL1L ubiquitin ligase complex and BiP.";
RL J. Biol. Chem. 283:20914-20924(2008).
RN [10]
RP FUNCTION, INTERACTION WITH HSPA5; SEL1L AND SYVN1, AND MUTAGENESIS OF
RP ARG-207 AND ARG-428.
RX PubMed=18264092; DOI=10.1038/ncb1689;
RA Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.;
RT "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L
RT ubiquitin ligase complex for ERAD.";
RL Nat. Cell Biol. 10:272-282(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Probable lectin that binds selectively to improperly folded
CC lumenal proteins. May function in endoplasmic reticulum quality control
CC and endoplasmic reticulum-associated degradation (ERAD) of both non-
CC glycosylated proteins and glycoproteins. {ECO:0000269|PubMed:16531414,
CC ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18502753}.
CC -!- SUBUNIT: May form a complex with OS9, HSPA5, SYVN1, and SEL1L with
CC which it interacts directly. Interacts (via PRKCSH 2 domain) with
CC KREMEN2 (when glycosylated). Interacts with HSPA5.
CC {ECO:0000269|PubMed:16531414, ECO:0000269|PubMed:18264092,
CC ECO:0000269|PubMed:18502753}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:16531414, ECO:0000269|PubMed:18502753}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=hXTP3B-long;
CC IsoId=Q96DZ1-1; Sequence=Displayed;
CC Name=2; Synonyms=hXTP3B-short;
CC IsoId=Q96DZ1-2; Sequence=VSP_015790;
CC Name=3;
CC IsoId=Q96DZ1-3; Sequence=VSP_047155;
CC -!- PTM: Isoform 1 and isoform 2 are N-glycosylated.
CC {ECO:0000269|PubMed:18502753}.
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DR EMBL; AY453410; AAR26725.1; -; mRNA.
DR EMBL; AY358717; AAQ89079.1; -; mRNA.
DR EMBL; AK001913; BAA91974.1; -; mRNA.
DR EMBL; AK315477; BAG37861.1; -; mRNA.
DR EMBL; AC007883; AAY24352.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00164.1; -; Genomic_DNA.
DR EMBL; BC013129; AAH13129.1; -; mRNA.
DR EMBL; BC022228; AAH22228.1; -; mRNA.
DR EMBL; AF131743; AAD20029.1; -; mRNA.
DR EMBL; AF131849; AAD20060.1; -; mRNA.
DR CCDS; CCDS1848.1; -. [Q96DZ1-1]
DR CCDS; CCDS46283.1; -. [Q96DZ1-3]
DR CCDS; CCDS46284.1; -. [Q96DZ1-2]
DR RefSeq; NP_001120869.1; NM_001127397.2. [Q96DZ1-3]
DR RefSeq; NP_001120870.1; NM_001127398.2. [Q96DZ1-2]
DR RefSeq; NP_056516.2; NM_015701.4. [Q96DZ1-1]
DR AlphaFoldDB; Q96DZ1; -.
DR SMR; Q96DZ1; -.
DR BioGRID; 118096; 177.
DR CORUM; Q96DZ1; -.
DR IntAct; Q96DZ1; 31.
DR MINT; Q96DZ1; -.
DR STRING; 9606.ENSP00000185150; -.
DR GlyGen; Q96DZ1; 1 site.
DR iPTMnet; Q96DZ1; -.
DR PhosphoSitePlus; Q96DZ1; -.
DR BioMuta; ERLEC1; -.
DR DMDM; 74731510; -.
DR EPD; Q96DZ1; -.
DR jPOST; Q96DZ1; -.
DR MassIVE; Q96DZ1; -.
DR MaxQB; Q96DZ1; -.
DR PaxDb; Q96DZ1; -.
DR PeptideAtlas; Q96DZ1; -.
DR PRIDE; Q96DZ1; -.
DR ProteomicsDB; 6002; -.
DR ProteomicsDB; 76344; -. [Q96DZ1-1]
DR ProteomicsDB; 76345; -. [Q96DZ1-2]
DR Antibodypedia; 30214; 44 antibodies from 13 providers.
DR DNASU; 27248; -.
DR Ensembl; ENST00000185150.9; ENSP00000185150.4; ENSG00000068912.15. [Q96DZ1-1]
DR Ensembl; ENST00000378239.5; ENSP00000367485.5; ENSG00000068912.15. [Q96DZ1-2]
DR Ensembl; ENST00000405123.7; ENSP00000385629.3; ENSG00000068912.15. [Q96DZ1-3]
DR GeneID; 27248; -.
DR KEGG; hsa:27248; -.
DR MANE-Select; ENST00000185150.9; ENSP00000185150.4; NM_015701.5; NP_056516.2.
DR UCSC; uc002rxm.4; human. [Q96DZ1-1]
DR CTD; 27248; -.
DR DisGeNET; 27248; -.
DR GeneCards; ERLEC1; -.
DR HGNC; HGNC:25222; ERLEC1.
DR HPA; ENSG00000068912; Low tissue specificity.
DR MIM; 611229; gene.
DR neXtProt; NX_Q96DZ1; -.
DR OpenTargets; ENSG00000068912; -.
DR PharmGKB; PA165696636; -.
DR VEuPathDB; HostDB:ENSG00000068912; -.
DR eggNOG; KOG3394; Eukaryota.
DR GeneTree; ENSGT00530000063603; -.
DR HOGENOM; CLU_048035_1_0_1; -.
DR InParanoid; Q96DZ1; -.
DR OMA; QYHEERE; -.
DR OrthoDB; 1475416at2759; -.
DR PhylomeDB; Q96DZ1; -.
DR TreeFam; TF314309; -.
DR PathwayCommons; Q96DZ1; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR SignaLink; Q96DZ1; -.
DR BioGRID-ORCS; 27248; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; ERLEC1; human.
DR GeneWiki; C2orf30; -.
DR GenomeRNAi; 27248; -.
DR Pharos; Q96DZ1; Tbio.
DR PRO; PR:Q96DZ1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96DZ1; protein.
DR Bgee; ENSG00000068912; Expressed in epithelial cell of pancreas and 191 other tissues.
DR ExpressionAtlas; Q96DZ1; baseline and differential.
DR Genevisible; Q96DZ1; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; TAS:Reactome.
DR GO; GO:0051082; F:unfolded protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0036503; P:ERAD pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR Gene3D; 2.70.130.10; -; 2.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR045149; OS-9-like.
DR InterPro; IPR012913; OS9-like_dom.
DR PANTHER; PTHR15414; PTHR15414; 1.
DR Pfam; PF07915; PRKCSH; 2.
DR SUPFAM; SSF50911; SSF50911; 2.
DR PROSITE; PS51914; MRH; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..483
FT /note="Endoplasmic reticulum lectin 1"
FT /id="PRO_0000042182"
FT DOMAIN 111..246
FT /note="MRH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 342..469
FT /note="MRH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 199..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 215..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 344..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 421..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 436..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT VAR_SEQ 294..347
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015790"
FT VAR_SEQ 410..435
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047155"
FT VARIANT 318
FT /note="V -> L (in dbSNP:rs2287345)"
FT /id="VAR_051493"
FT MUTAGEN 207
FT /note="R->A: Abolishes interaction with SEL1L."
FT /evidence="ECO:0000269|PubMed:18264092"
FT MUTAGEN 379
FT /note="G->S: Abolishes binding to KREMEN2."
FT /evidence="ECO:0000269|PubMed:16531414"
FT MUTAGEN 428
FT /note="R->A: Abolishes interaction with SEL1L."
FT /evidence="ECO:0000269|PubMed:18264092"
FT CONFLICT 331
FT /note="D -> G (in Ref. 3; BAA91974)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="K -> E (in Ref. 3; BAA91974)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 54858 MW; 35F78A1468457468 CRC64;
MEEGGGGVRS LVPGGPVLLV LCGLLEASGG GRALPQLSDD IPFRVNWPGT EFSLPTTGVL
YKEDNYVIMT TAHKEKYKCI LPLVTSGDEE EEKDYKGPNP RELLEPLFKQ SSCSYRIESY
WTYEVCHGKH IRQYHEEKET GQKINIHEYY LGNMLAKNLL FEKEREAEEK EKSNEIPTKN
IEGQMTPYYP VGMGNGTPCS LKQNRPRSST VMYICHPESK HEILSVAEVT TCEYEVVILT
PLLCSHPKYR FRASPVNDIF CQSLPGSPFK PLTLRQLEQQ EEILRVPFRR NKEEDLQSTK
EERFPAIHKS IAIGSQPVLT VGTTHISKLT DDQLIKEFLS GSYCFRGGVG WWKYEFCYGK
HVHQYHEDKD SGKTSVVVGT WNQEEHIEWA KKNTARAYHL QDDGTQTVRM VSHFYGNGDI
CDITDKPRQV TVKLKCKESD SPHAVTVYML EPHSCQYILG VESPVICKIL DTADENGLLS
LPN
