ERLEC_MOUSE
ID ERLEC_MOUSE Reviewed; 483 AA.
AC Q8VEH8; Q3UZF3; Q8BVN6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Endoplasmic reticulum lectin 1;
DE AltName: Full=ER lectin;
DE Short=Erlectin;
DE Flags: Precursor;
GN Name=Erlec1;
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=Testis;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen, and
RC Testis;
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: 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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; AK077120; BAC36623.1; -; mRNA.
DR EMBL; AK133874; BAE21904.1; -; mRNA.
DR EMBL; AL662891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018468; AAH18468.1; -; mRNA.
DR CCDS; CCDS24509.1; -.
DR RefSeq; NP_080021.3; NM_025745.3.
DR AlphaFoldDB; Q8VEH8; -.
DR SMR; Q8VEH8; -.
DR STRING; 10090.ENSMUSP00000072929; -.
DR GlyGen; Q8VEH8; 1 site.
DR PhosphoSitePlus; Q8VEH8; -.
DR SwissPalm; Q8VEH8; -.
DR EPD; Q8VEH8; -.
DR MaxQB; Q8VEH8; -.
DR PaxDb; Q8VEH8; -.
DR PeptideAtlas; Q8VEH8; -.
DR PRIDE; Q8VEH8; -.
DR ProteomicsDB; 275472; -.
DR Antibodypedia; 30214; 44 antibodies from 13 providers.
DR DNASU; 66753; -.
DR Ensembl; ENSMUST00000073192; ENSMUSP00000072929; ENSMUSG00000020311.
DR GeneID; 66753; -.
DR KEGG; mmu:66753; -.
DR UCSC; uc007iic.1; mouse.
DR CTD; 27248; -.
DR MGI; MGI:1914003; Erlec1.
DR VEuPathDB; HostDB:ENSMUSG00000020311; -.
DR eggNOG; KOG3394; Eukaryota.
DR GeneTree; ENSGT00530000063603; -.
DR HOGENOM; CLU_048035_1_0_1; -.
DR InParanoid; Q8VEH8; -.
DR OMA; QYHEERE; -.
DR OrthoDB; 1475416at2759; -.
DR PhylomeDB; Q8VEH8; -.
DR TreeFam; TF314309; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR BioGRID-ORCS; 66753; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Erlec1; mouse.
DR PRO; PR:Q8VEH8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VEH8; protein.
DR Bgee; ENSMUSG00000020311; Expressed in seminal vesicle and 252 other tissues.
DR ExpressionAtlas; Q8VEH8; baseline and differential.
DR Genevisible; Q8VEH8; MM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS: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 Disulfide bond; Endoplasmic reticulum; Glycoprotein; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..483
FT /note="Endoplasmic reticulum lectin 1"
FT /id="PRO_0000042183"
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 CONFLICT 10
FT /note="S -> T (in Ref. 1; BAC36623)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 54906 MW; BB521BB85C3595D2 CRC64;
MEEGDGGLRS LVPGGPLLLV LYGLLEASGG GRALPQLSDD IPFRVNWPGT EFSLPTTGVL
YKEDNYIIMT TAHKEKYKCI LPLVTSGDEE EEKDYKGPNP RELLEPLFKQ SSCSYRIESY
WTYEVCHGKH IRQYHEEKET GQKVNIHEYY LGNMLAKNLL YEKEREAKEN EKSNEIPTKN
IEGQMTPYYP VGMGNGTPCS LKQNRPRSST VMYICHPESK HEILSVAEVT TCEYEVVILT
PLLCSHPKYK FRASPVNDIF CQSLPGSPFK PLTLRQLEQQ EEILRVPFRR NKEEDLPSAK
EERFPAIHKP IAVGSQPVLT VGTTHISKLT DDQLIKEFLS GSYCFHGGVG WWKYEFCYGK
HVHQYHEDKD NGKTSVVVGT WNQEEHVEWA KKNTARAYHL QDDGTQTVRM VSHFYGNGDI
CDITDKPRQV TVKLKCKESD SPHAVTVYML EPHSCQYILG VESPVICKIL DTADENGLLS
LPN
