ID   ERLEC_XENTR             Reviewed;         481 AA.
AC   Q28IT1;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Endoplasmic reticulum lectin 1;
DE   AltName: Full=ER lectin;
DE            Short=Erlectin;
DE   Flags: Precursor;
GN   Name=erlec1; ORFNames=TNeu121c15.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   DISRUPTION PHENOTYPE.
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   -!- DISRUPTION PHENOTYPE: Embryos display head and axial defects during
CC       organogenesis. {ECO:0000269|PubMed:16531414}.
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DR   EMBL; CR760240; CAJ82824.1; -; mRNA.
DR   AlphaFoldDB; Q28IT1; -.
DR   STRING; 8364.ENSXETP00000062950; -.
DR   PaxDb; Q28IT1; -.
DR   eggNOG; KOG3394; Eukaryota.
DR   InParanoid; Q28IT1; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
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..481
FT                   /note="Endoplasmic reticulum lectin 1"
FT                   /id="PRO_0000386452"
FT   DOMAIN          108..245
FT                   /note="MRH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DOMAIN          340..467
FT                   /note="MRH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
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        342..355
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        419..453
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        434..465
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ   SEQUENCE   481 AA;  54698 MW;  6E63B226D12D93C3 CRC64;
     MRRSDRLRCA GASLLVVLCG VFRSSFGGRT LPALSDDIPF RLKWPGPDFT LPTAGIPYKE
     DNYIIMTTAD KEKYKCLLPL MANGNEEQDG EYKGPSPGAL LEPLFKLSSC SYRIESYWTY
     EVCHGKYIRQ YHEEKETGQK LSIQEYYLGK MMKKSTTEAG ENQEEKESAE SPKEIYTKNI
     EGQMTPYYPV EMINGTPCSL KQNQPRSSTV MYICHPESKH EILSVAEVTT CEYEVVILTP
     LLCNHPKYRF RTSPINDIFC QSMPGSPLRP QSLVKLEHQK EEIKSPLKPN KEEEQQLLRE
     KFSTIHKPVT VGSQQQVTVG TTHISRLTDE QLIKEFLSGS YCFHGGVGWW KYEFCYGKYV
     HQYHEDKDTG KTTVVVGTWK ADEHQEWAKK NLARAYMTTP DGVQTVKTVS HFYGGGDVCE
     VSEQPRQVIV KLKCKESESP HAVTVYMLEP QTCQYILGVE SPVICKILDT ADENGLLSIP
     N