LMAN1_HUMAN
ID LMAN1_HUMAN Reviewed; 510 AA.
AC P49257; Q12895; Q8N5I7; Q9UQG1; Q9UQG2; Q9UQG3; Q9UQG4; Q9UQG5; Q9UQG6;
AC Q9UQG7; Q9UQG8; Q9UQG9; Q9UQH0; Q9UQH1; Q9UQH2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Protein ERGIC-53;
DE AltName: Full=ER-Golgi intermediate compartment 53 kDa protein;
DE AltName: Full=Gp58;
DE AltName: Full=Intracellular mannose-specific lectin MR60;
DE AltName: Full=Lectin mannose-binding 1;
DE Flags: Precursor;
GN Name=LMAN1; Synonyms=ERGIC53, F5F8D;
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], AND PROTEIN SEQUENCE OF 31-59 AND 418-432.
RC TISSUE=Liver, and Placenta;
RX PubMed=8223692;
RA Schindler R., Itin C., Zerial M., Lottspeich F., Hauri H.-P.;
RT "ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment,
RT carries an ER retention motif.";
RL Eur. J. Cell Biol. 61:1-9(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 31-41.
RC TISSUE=Peripheral blood;
RX PubMed=7876089; DOI=10.1074/jbc.270.8.3551;
RA Arar C., Carpentier V., Le Caer J.-P., Monsigny M., Legrand A.,
RA Roche A.-C.;
RT "ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi
RT intermediate compartment, is identical to MR60, an intracellular mannose-
RT specific lectin of myelomonocytic cells.";
RL J. Biol. Chem. 270:3551-3553(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-14; ALA-39 AND LEU-410, AND
RP INVOLVEMENT IN F5F8D1.
RX PubMed=10090935;
RA Nichols W.C., Terry V.H., Wheatley M.A., Yang A., Zivelin A.,
RA Ciavarella N., Stefanile C., Matsushita T., Saito H., de Bosch N.B.,
RA Ruiz-Saez A., Torres A., Thompson A.R., Feinstein D.I., White G.C.,
RA Negrier C., Vinciguerra C., Aktan M., Kaufman R.J., Ginsburg D.,
RA Seligsohn U.;
RT "ERGIC-53 gene structure and mutation analysis in 19 combined factors V and
RT VIII deficiency families.";
RL Blood 93:2261-2266(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-410.
RC TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 31-44.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP SIMILARITY TO LEGUMINOUS LECTINS.
RX PubMed=8205612; DOI=10.1016/0092-8674(94)90047-7;
RA Fiedler K., Simons K.;
RT "A putative novel class of animal lectins in the secretory pathway
RT homologous to leguminous lectins.";
RL Cell 77:625-626(1994).
RN [7]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line protein
RT expression map database.";
RL Proteomics 2:212-223(2002).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MOTIF ER EXPORT, AND
RP DISULFIDE BOND.
RX PubMed=13130098; DOI=10.1242/jcs.00759;
RA Nufer O., Kappeler F., Guldbrandsen S., Hauri H.-P.;
RT "ER export of ERGIC-53 is controlled by cooperation of targeting
RT determinants in all three of its domains.";
RL J. Cell Sci. 116:4429-4440(2003).
RN [9]
RP INTERACTION WITH MCFD2, AND FUNCTION.
RX PubMed=12717434; DOI=10.1038/ng1153;
RA Zhang B., Cunningham M.A., Nichols W.C., Bernat J.A., Seligsohn U.,
RA Pipe S.W., McVey J.H., Schulte-Overberg U., de Bosch N.B., Ruiz-Saez A.,
RA White G.C., Tuddenham E.G., Kaufman R.J., Ginsburg D.;
RT "Bleeding due to disruption of a cargo-specific ER-to-Golgi transport
RT complex.";
RL Nat. Genet. 34:220-225(2003).
RN [10]
RP SUBCELLULAR LOCATION, SUBUNIT, AND INTERCHAIN DISULFIDE BONDS.
RX PubMed=16257008; DOI=10.1016/j.jmb.2005.09.077;
RA Neve E.P., Lahtinen U., Pettersson R.F.;
RT "Oligomerization and intracellular localization of the glycoprotein
RT receptor ERGIC-53 is independent of disulfide bonds.";
RL J. Mol. Biol. 354:556-568(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP INTERACTION WITH RAB3GAP1; RAB3GAP2 AND UBXN6, AND REGION.
RX PubMed=22337587; DOI=10.1074/mcp.m111.016444;
RA Haines D.S., Lee J.E., Beauparlant S.L., Kyle D.B., den Besten W.,
RA Sweredoski M.J., Graham R.L., Hess S., Deshaies R.J.;
RT "Protein interaction profiling of the p97 adaptor UBXD1 points to a role
RT for the complex in modulating ERGIC-53 trafficking.";
RL Mol. Cell. Proteomics 11:M111.016444-M111.016444(2012).
RN [13]
RP INTERACTION WITH TMEM115.
RX PubMed=24806965; DOI=10.1242/jcs.136754;
RA Ong Y.S., Tran T.H., Gounko N.V., Hong W.;
RT "TMEM115 is an integral membrane protein of the Golgi complex involved in
RT retrograde transport.";
RL J. Cell Sci. 127:2825-2839(2014).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-30, AND
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).
RN [16]
RP INTERACTION WITH SERPINA1.
RX PubMed=31142615; DOI=10.1074/jbc.ra119.007435;
RA Yoo W., Cho E.B., Kim S., Yoon J.B.;
RT "The E3 ubiquitin ligase MARCH2 regulates ERGIC3-dependent trafficking of
RT secretory proteins.";
RL J. Biol. Chem. 294:10900-10912(2019).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 32-277 IN COMPLEX WITH MCFD2 AND
RP CALCIUM IONS, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=20138881; DOI=10.1016/j.febslet.2010.02.009;
RA Wigren E., Bourhis J.M., Kursula I., Guy J.E., Lindqvist Y.;
RT "Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex
RT provides insight into combined deficiency of factor V and factor VIII.";
RL FEBS Lett. 584:878-882(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 31-285 IN COMPLEX WITH CALCIUM
RP IONS, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=20142513; DOI=10.1073/pnas.0908526107;
RA Nishio M., Kamiya Y., Mizushima T., Wakatsuki S., Sasakawa H., Yamamoto K.,
RA Uchiyama S., Noda M., McKay A.R., Fukui K., Hauri H.P., Kato K.;
RT "Structural basis for the cooperative interplay between the two causative
RT gene products of combined factor V and factor VIII deficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4034-4039(2010).
RN [19]
RP VARIANT F5F8D1 SER-67, CHARACTERIZATION OF VARIANT F5F8D1 SER-67, AND
RP INTERACTION WITH MCFD2.
RX PubMed=19787799; DOI=10.1002/ajh.21532;
RA Yamada T., Fujimori Y., Suzuki A., Miyawaki Y., Takagi A., Murate T.,
RA Sano M., Matsushita T., Saito H., Kojima T.;
RT "A novel missense mutation causing abnormal LMAN1 in a Japanese patient
RT with combined deficiency of factor V and factor VIII.";
RL Am. J. Hematol. 84:738-742(2009).
CC -!- FUNCTION: Mannose-specific lectin. May recognize sugar residues of
CC glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors
CC and may be involved in the sorting or recycling of proteins, lipids, or
CC both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the
CC ER-to-Golgi transport of selected proteins.
CC {ECO:0000269|PubMed:12717434, ECO:0000269|PubMed:13130098}.
CC -!- SUBUNIT: Exists both as a covalent disulfide-linked homohexamer, and a
CC complex of three disulfide-linked dimers non-covalently kept together.
CC Interacts with MCFD2. May interact with TMEM115. Interacts with
CC RAB3GAP1 and RAB3GAP2 (PubMed:22337587). Interacts with UBXN6
CC (PubMed:22337587). Interacts with SERPINA1/alpha1-antitrypsin
CC (PubMed:31142615). {ECO:0000269|PubMed:12717434,
CC ECO:0000269|PubMed:13130098, ECO:0000269|PubMed:16257008,
CC ECO:0000269|PubMed:19787799, ECO:0000269|PubMed:20138881,
CC ECO:0000269|PubMed:20142513, ECO:0000269|PubMed:22337587,
CC ECO:0000269|PubMed:24806965, ECO:0000269|PubMed:31142615}.
CC -!- INTERACTION:
CC P49257; Q9BS26: ERP44; NbExp=3; IntAct=EBI-1057738, EBI-541644;
CC P49257; Q8NI22: MCFD2; NbExp=12; IntAct=EBI-1057738, EBI-2689785;
CC P49257; O15260: SURF4; NbExp=3; IntAct=EBI-1057738, EBI-1044848;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Single-pass type I membrane protein. Golgi
CC apparatus membrane; Single-pass membrane protein. Endoplasmic reticulum
CC membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:13130098}.
CC -!- DOMAIN: The FF ER export motif at the C-terminus is not sufficient to
CC support endoplasmic reticulum exit, and needs assistance of Gln-501 for
CC proper recognition of COPII coat components.
CC -!- PTM: The N-terminal may be partly blocked.
CC -!- MASS SPECTROMETRY: Mass=54222.91; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11840567};
CC -!- DISEASE: Factor V and factor VIII combined deficiency 1 (F5F8D1)
CC [MIM:227300]: A blood coagulation disorder characterized by bleeding
CC symptoms similar to those in hemophilia or parahemophilia, that are
CC caused by single deficiency of FV or FVIII, respectively. The most
CC common symptoms are epistaxis, menorrhagia, and excessive bleeding
CC during or after trauma. Plasma levels of coagulation factors V and VIII
CC are in the range of 5 to 30% of normal. {ECO:0000269|PubMed:10090935,
CC ECO:0000269|PubMed:19787799}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; X71661; CAA50653.1; -; mRNA.
DR EMBL; U09716; AAA95960.1; -; mRNA.
DR EMBL; AF081866; AAD32479.1; -; Genomic_DNA.
DR EMBL; AF081865; AAD32479.1; JOINED; Genomic_DNA.
DR EMBL; AF081867; AAD32480.1; -; Genomic_DNA.
DR EMBL; AF081869; AAD32481.1; -; Genomic_DNA.
DR EMBL; AF081868; AAD32481.1; JOINED; Genomic_DNA.
DR EMBL; AF081871; AAD32482.1; -; Genomic_DNA.
DR EMBL; AF081870; AAD32482.1; JOINED; Genomic_DNA.
DR EMBL; AF081873; AAD32483.1; -; Genomic_DNA.
DR EMBL; AF081872; AAD32483.1; JOINED; Genomic_DNA.
DR EMBL; AF081875; AAD32484.1; -; Genomic_DNA.
DR EMBL; AF081874; AAD32484.1; JOINED; Genomic_DNA.
DR EMBL; AF081877; AAD32485.1; -; Genomic_DNA.
DR EMBL; AF081876; AAD32485.1; JOINED; Genomic_DNA.
DR EMBL; AF081879; AAD32486.1; -; Genomic_DNA.
DR EMBL; AF081878; AAD32486.1; JOINED; Genomic_DNA.
DR EMBL; AF081880; AAD32487.1; -; Genomic_DNA.
DR EMBL; AF081882; AAD32488.1; -; Genomic_DNA.
DR EMBL; AF081881; AAD32488.1; JOINED; Genomic_DNA.
DR EMBL; AF081884; AAD32489.1; -; Genomic_DNA.
DR EMBL; AF081883; AAD32489.1; JOINED; Genomic_DNA.
DR EMBL; AF081885; AAD32490.1; -; Genomic_DNA.
DR EMBL; BC032330; AAH32330.1; -; mRNA.
DR CCDS; CCDS11974.1; -.
DR PIR; S42626; S42626.
DR RefSeq; NP_005561.1; NM_005570.3.
DR PDB; 3A4U; X-ray; 1.84 A; A=31-285.
DR PDB; 3LCP; X-ray; 2.45 A; A/B=32-277.
DR PDB; 3WHT; X-ray; 1.80 A; A=31-269.
DR PDB; 3WHU; X-ray; 2.60 A; A=31-269.
DR PDB; 3WNX; X-ray; 2.75 A; A=31-269.
DR PDB; 4GKX; X-ray; 2.70 A; A/B/C/D/E/F=31-270.
DR PDB; 4GKY; X-ray; 2.42 A; A=31-270.
DR PDB; 4YGB; X-ray; 1.60 A; A/C=31-269.
DR PDB; 4YGC; X-ray; 2.40 A; A/C/E/G=31-269.
DR PDB; 4YGD; X-ray; 2.51 A; A/C/E/G=31-269.
DR PDB; 4YGE; X-ray; 3.05 A; A/C/E=31-269.
DR PDBsum; 3A4U; -.
DR PDBsum; 3LCP; -.
DR PDBsum; 3WHT; -.
DR PDBsum; 3WHU; -.
DR PDBsum; 3WNX; -.
DR PDBsum; 4GKX; -.
DR PDBsum; 4GKY; -.
DR PDBsum; 4YGB; -.
DR PDBsum; 4YGC; -.
DR PDBsum; 4YGD; -.
DR PDBsum; 4YGE; -.
DR AlphaFoldDB; P49257; -.
DR SMR; P49257; -.
DR BioGRID; 110185; 443.
DR DIP; DIP-42188N; -.
DR ELM; P49257; -.
DR IntAct; P49257; 37.
DR MINT; P49257; -.
DR STRING; 9606.ENSP00000251047; -.
DR DrugBank; DB00025; Antihemophilic factor, human recombinant.
DR DrugBank; DB13998; Lonoctocog alfa.
DR DrugBank; DB13999; Moroctocog alfa.
DR TCDB; 9.B.417.1.1; the mcfd2/lman1 complex receptor (mlm-cr) family.
DR UniLectin; P49257; -.
DR GlyGen; P49257; 3 sites, 4 O-linked glycans (3 sites).
DR iPTMnet; P49257; -.
DR MetOSite; P49257; -.
DR PhosphoSitePlus; P49257; -.
DR SwissPalm; P49257; -.
DR BioMuta; LMAN1; -.
DR DMDM; 22261801; -.
DR EPD; P49257; -.
DR jPOST; P49257; -.
DR MassIVE; P49257; -.
DR MaxQB; P49257; -.
DR PaxDb; P49257; -.
DR PeptideAtlas; P49257; -.
DR PRIDE; P49257; -.
DR ProteomicsDB; 55977; -.
DR Antibodypedia; 1115; 290 antibodies from 32 providers.
DR DNASU; 3998; -.
DR Ensembl; ENST00000251047.6; ENSP00000251047.4; ENSG00000074695.6.
DR GeneID; 3998; -.
DR KEGG; hsa:3998; -.
DR MANE-Select; ENST00000251047.6; ENSP00000251047.4; NM_005570.4; NP_005561.1.
DR UCSC; uc002lhz.4; human.
DR CTD; 3998; -.
DR DisGeNET; 3998; -.
DR GeneCards; LMAN1; -.
DR HGNC; HGNC:6631; LMAN1.
DR HPA; ENSG00000074695; Low tissue specificity.
DR MalaCards; LMAN1; -.
DR MIM; 227300; phenotype.
DR MIM; 601567; gene.
DR neXtProt; NX_P49257; -.
DR OpenTargets; ENSG00000074695; -.
DR Orphanet; 35909; Combined deficiency of factor V and factor VIII.
DR PharmGKB; PA30399; -.
DR VEuPathDB; HostDB:ENSG00000074695; -.
DR eggNOG; KOG3838; Eukaryota.
DR GeneTree; ENSGT00940000159146; -.
DR HOGENOM; CLU_041093_4_0_1; -.
DR InParanoid; P49257; -.
DR OMA; WSAEFQF; -.
DR OrthoDB; 1377709at2759; -.
DR PhylomeDB; P49257; -.
DR TreeFam; TF313311; -.
DR PathwayCommons; P49257; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-948021; Transport to the Golgi and subsequent modification.
DR SignaLink; P49257; -.
DR BioGRID-ORCS; 3998; 6 hits in 1081 CRISPR screens.
DR ChiTaRS; LMAN1; human.
DR EvolutionaryTrace; P49257; -.
DR GeneWiki; LMAN1; -.
DR GenomeRNAi; 3998; -.
DR Pharos; P49257; Tbio.
DR PRO; PR:P49257; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P49257; protein.
DR Bgee; ENSG00000074695; Expressed in germinal epithelium of ovary and 190 other tissues.
DR ExpressionAtlas; P49257; baseline and differential.
DR Genevisible; P49257; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030017; C:sarcomere; IEA:Ensembl.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:0010638; P:positive regulation of organelle organization; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR005052; Lectin_leg.
DR InterPro; IPR033085; LMAN1.
DR PANTHER; PTHR12223:SF32; PTHR12223:SF32; 1.
DR Pfam; PF03388; Lectin_leg-like; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51328; L_LECTIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Lectin;
KW Membrane; Metal-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:7876089, ECO:0000269|PubMed:8223692,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 31..510
FT /note="Protein ERGIC-53"
FT /id="PRO_0000017660"
FT TOPO_DOM 31..477
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..267
FT /note="L-type lectin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT REGION 499..510
FT /note="Mediates interaction with RAB3GAP1, RAB3GAP2 and
FT UBXN6"
FT /evidence="ECO:0000269|PubMed:22337587"
FT MOTIF 509..510
FT /note="ER export motif"
FT BINDING 88
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 121
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 156
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 178
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 251..253
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT SITE 501
FT /note="Required for ER export"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT DISULFID 190..230
FT DISULFID 466
FT /note="Interchain"
FT DISULFID 475
FT /note="Interchain"
FT VARIANT 14
FT /note="R -> Q (in dbSNP:rs1043302)"
FT /evidence="ECO:0000269|PubMed:10090935"
FT /id="VAR_013703"
FT VARIANT 39
FT /note="V -> A (in dbSNP:rs33926449)"
FT /evidence="ECO:0000269|PubMed:10090935"
FT /id="VAR_013704"
FT VARIANT 67
FT /note="W -> S (in F5F8D1; loss of interaction with MCFD2
FT and ability to bind D-mannose)"
FT /evidence="ECO:0000269|PubMed:19787799"
FT /id="VAR_071969"
FT VARIANT 355
FT /note="I -> T (in dbSNP:rs3737392)"
FT /id="VAR_049770"
FT VARIANT 410
FT /note="M -> L (in dbSNP:rs2298711)"
FT /evidence="ECO:0000269|PubMed:10090935,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_013705"
FT CONFLICT 153
FT /note="S -> T (in Ref. 1; CAA50653)"
FT /evidence="ECO:0000305"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:4YGB"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3WHU"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 102..113
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:3A4U"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4GKY"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:4YGB"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3A4U"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3A4U"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3WHT"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:4YGB"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4GKY"
FT STRAND 256..268
FT /evidence="ECO:0007829|PDB:4YGB"
SQ SEQUENCE 510 AA; 57549 MW; B87EF117C0CD386C CRC64;
MAGSRQRGLR ARVRPLFCAL LLSLGRFVRG DGVGGDPAVA LPHRRFEYKY SFKGPHLVQS
DGTVPFWAHA GNAIPSSDQI RVAPSLKSQR GSVWTKTKAA FENWEVEVTF RVTGRGRIGA
DGLAIWYAEN QGLEGPVFGS ADLWNGVGIF FDSFDNDGKK NNPAIVIIGN NGQIHYDHQN
DGASQALASC QRDFRNKPYP VRAKITYYQN TLTVMINNGF TPDKNDYEFC AKVENMIIPA
QGHFGISAAT GGLADDHDVL SFLTFQLTEP GKEPPTPDKE ISEKEKEKYQ EEFEHFQQEL
DKKKEEFQKG HPDLQGQPAE EIFESVGDRE LRQVFEGQNR IHLEIKQLNR QLDMILDEQR
RYVSSLTEEI SKRGAGMPGQ HGQITQQELD TVVKTQHEIL RQVNEMKNSM SETVRLVSGM
QHPGSAGGVY ETTQHFIDIK EHLHIVKRDI DNLVQRNMPS NEKPKCPELP PFPSCLSTVH
FIIFVVVQTV LFIGYIMYRS QQEAAAKKFF
