ID   ERLEC_PONAB             Reviewed;         483 AA.
AC   Q5R8S4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Endoplasmic reticulum lectin 1;
DE   AltName: Full=ER lectin;
DE            Short=Erlectin;
DE   Flags: Precursor;
GN   Name=ERLEC1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859675; CAH91836.1; -; mRNA.
DR   RefSeq; NP_001126061.1; NM_001132589.1.
DR   AlphaFoldDB; Q5R8S4; -.
DR   STRING; 9601.ENSPPYP00000013854; -.
DR   Ensembl; ENSPPYT00000046707; ENSPPYP00000024782; ENSPPYG00000033647.
DR   GeneID; 100173013; -.
DR   KEGG; pon:100173013; -.
DR   CTD; 27248; -.
DR   eggNOG; KOG3394; Eukaryota.
DR   GeneTree; ENSGT00530000063603; -.
DR   InParanoid; Q5R8S4; -.
DR   OrthoDB; 1475416at2759; -.
DR   Proteomes; UP000001595; Chromosome 2A.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
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; IEA:Ensembl.
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; 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_0000042184"
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"
SQ   SEQUENCE   483 AA;  54849 MW;  E36516FAD1297845 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
     EERFPAIHKP IAIGSQPVLT VGTTHISKLT DDQLIKEFLS GSYCFHGGVG WWKYEFCYGK
     HVHQYHEDKD SGKTSVVVGT WNQEEHIEWA KKNTARAYHL QDDGTQTVRM VSHFYGNGDI
     CDITDKPRQV TVKLKCKESD SPHAVTVYML EPHSCQYILG VESPVICKIL DTADENGLLS
     LPN