ID   ERLEC_XENLA             Reviewed;         480 AA.
AC   Q08B78;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Endoplasmic reticulum lectin 1;
DE   AltName: Full=ER lectin;
DE            Short=Erlectin;
DE   Flags: Precursor;
GN   Name=erlec1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
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).
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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Maternally expressed. Levels decrease during
CC       gastrulation and are then increasingly up-regulated during neurulation
CC       and tailbud stages. Weak ubiquitous expression is detected at all
CC       stages of development. {ECO:0000269|PubMed:16531414}.
CC   -!- DISRUPTION PHENOTYPE: Embryos display head and axial defects during
CC       organogenesis. {ECO:0000269|PubMed:16531414}.
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DR   EMBL; BC124843; AAI24844.1; -; mRNA.
DR   RefSeq; NP_001116355.1; NM_001122883.1.
DR   AlphaFoldDB; Q08B78; -.
DR   DNASU; 495829; -.
DR   GeneID; 495829; -.
DR   KEGG; xla:495829; -.
DR   CTD; 495829; -.
DR   Xenbase; XB-GENE-989161; erlec1.S.
DR   OMA; QYHEERE; -.
DR   OrthoDB; 1475416at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 495829; Expressed in pancreas and 19 other tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..480
FT                   /note="Endoplasmic reticulum lectin 1"
FT                   /id="PRO_0000386451"
FT   DOMAIN          108..245
FT                   /note="MRH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DOMAIN          339..466
FT                   /note="MRH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   REGION          152..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        110..123
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        198..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        214..243
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        341..354
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        418..452
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        433..464
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ   SEQUENCE   480 AA;  54454 MW;  2A58E1D381B35EFA CRC64;
     MRRSDRFPCA GASLLVVLCG VFPSSFGGRT LPGLSDDIPF RLKWPGPDFT LPTAGIPYKE
     ENYIIMTTAD QETYKCMLPL MANGNEEEDR EYKGPSPGEL LDPLFKLSSC SYRIESYWTY
     EVCHGKYIRQ YHEEKEAGQK LNIQEYYLGK TVKKSPSEAG ENQEDKERTE GHKDIHTKNI
     EGQMTPYYPV EMTNGTPCSL KQNQARSSTV MYICHPEAKH EILSVAEITT CEYEVVILTP
     LLCNHPKYKF RPSPINDIFC QSMPGSPLRP QSLEKLEHQQ EEIKSPLKAK EEEQQLLKEK
     FSTIHKPVTV GSQQQVTVGT THISRLTDEQ LIKEFLSGSY CFHGGVGWWK YEFCYGKYVH
     QYHEDKDTGK TTVVVGTWKA EEHLDWAKKN LAKAYMSTAD GVQTVKTVSH FYGGGDLCEV
     NEQPRQVVVK LKCKQSESPH AVTVYMLEPQ TCQYILGVES PVICKILDTA DENGLLSIPN