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 10-JUN-2026, entry version 230. 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; DOI=10.1182/blood.v93.7.2261; 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 INTERACTION WITH BET1. RX PubMed=34779586; DOI=10.15252/emmm.202013787; RA Donkervoort S., Krause N., Dergai M., Yun P., Koliwer J., Gorokhova S., RA Geist Hauserman J., Cummings B.B., Hu Y., Smith R., Uapinyoying P., RA Ganesh V.S., Ghosh P.S., Monaghan K.G., Edassery S.L., Ferle P.E., RA Silverstein S., Chao K.R., Snyder M., Ellingwood S., Bharucha-Goebel D., RA Iannaccone S.T., Dal Peraro M., Foley A.R., Savas J.N., Bolduc V., RA Fasshauer D., Boennemann C.G., Schwake M.; RT "BET1 variants establish impaired vesicular transport as a cause for RT muscular dystrophy with epilepsy."; RL EMBO Mol. Med. 13:e13787-e13787(2021). RN [18] 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 [19] 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 [20] 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). Interacts with BET1 (PubMed:34779586). CC {ECO:0000269|PubMed:12717434, ECO:0000269|PubMed:13130098, CC ECO:0000269|PubMed:16257008, ECO:0000269|PubMed:19787799, CC ECO:0000269|PubMed:20138881, ECO:0000269|PubMed:20142513, CC ECO:0000269|PubMed:22337587, ECO:0000269|PubMed:24806965, CC ECO:0000269|PubMed:31142615, ECO:0000269|PubMed:34779586}. CC -!- INTERACTION: CC P49257; Q9BS26: ERP44; NbExp=3; IntAct=EBI-1057738, EBI-541644; CC P49257; Q8NI22: MCFD2; NbExp=15; 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_005570.4. 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 PDB; 8JP4; EM; 2.53 A; A/B/E/F=1-510. DR PDB; 8JP5; EM; 2.59 A; A/B/E/F=1-510. DR PDB; 8JP6; EM; 3.29 A; A/B/E/F=1-510. DR PDB; 8JP7; EM; 3.51 A; A/B/E/F=1-510. DR PDB; 8JP8; EM; 3.39 A; A/B/E/F=1-510. DR PDB; 8JP9; EM; 3.37 A; A/B/E/F=1-510. DR PDB; 8JPG; EM; 6.76 A; A/B/E/F=1-510. 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 PDBsum; 8JP4; -. DR PDBsum; 8JP5; -. DR PDBsum; 8JP6; -. DR PDBsum; 8JP7; -. DR PDBsum; 8JP8; -. DR PDBsum; 8JP9; -. DR PDBsum; 8JPG; -. DR AlphaFoldDB; P49257; -. DR EMDB; EMD-36467; -. DR EMDB; EMD-36468; -. DR EMDB; EMD-36469; -. DR EMDB; EMD-36470; -. DR EMDB; EMD-36471; -. DR EMDB; EMD-36472; -. DR EMDB; EMD-36479; -. DR SMR; P49257; -. DR BioGRID; 110185; 493. DR ComplexPortal; CPX-8001; LMAN1-MCFD2 cargo receptor complex. DR CORUM; P49257; -. DR DIP; DIP-42188N; -. DR ELM; P49257; -. DR FunCoup; P49257; 1500. DR IntAct; P49257; 74. DR MINT; P49257; -. DR NDEx; IQUERY-CP-LMAN1; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000251047; -. DR ChEMBL; CHEMBL6066884; -. 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 GlyCosmos; P49257; 3 sites, 4 glycans. DR GlyGen; P49257; 9 sites, 5 O-linked glycans (9 sites). DR iPTMnet; P49257; -. DR MetOSite; P49257; -. DR PhosphoSitePlus; P49257; -. DR SwissPalm; P49257; -. DR BioMuta; LMAN1; -. DR DMDM; 22261801; -. DR jPOST; P49257; -. DR MassIVE; P49257; -. DR PaxDb; 9606-ENSP00000251047; -. DR PeptideAtlas; P49257; -. DR ProteomicsDB; 55977; -. DR Pumba; P49257; -. DR Antibodypedia; 1115; 299 antibodies from 33 providers. DR DNASU; 3998; -. DR Ensembl; ENST00000251047.6; ENSP00000251047.4; ENSG00000074695.7. 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 AGR; HGNC:6631; -. DR ClinPGx; PA30399; -. 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 OpenTargets; ENSG00000074695; -. DR Orphanet; 35909; Combined deficiency of factor V and factor VIII. 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; 10265193at2759; -. DR PAN-GO; P49257; 6 GO annotations based on evolutionary models. DR PhylomeDB; P49257; -. 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 Agora; ENSG00000074695; -. DR BioGRID-ORCS; 3998; 9 hits in 1157 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 192 other cell types or tissues. 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; IDA:ComplexPortal. 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:0031012; C:extracellular matrix; HDA:BHF-UCL. DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0030017; C:sarcomere; IEA:Ensembl. DR GO; GO:0005537; F:D-mannose binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; EXP:DisProt. DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc. DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc. 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 CDD; cd06902; lectin_ERGIC-53_ERGL; 1. DR DisProt; DP03190; -. DR FunFam; 2.60.120.200:FF:000028; Blast:Protein ERGIC-53; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR051136; Intracellular_Lectin-GPT. DR InterPro; IPR005052; Lectin_leg. DR PANTHER; PTHR12223:SF32; PROTEIN ERGIC-53; 1. DR PANTHER; PTHR12223; VESICULAR MANNOSE-BINDING LECTIN; 1. DR Pfam; PF03388; Lectin_leg-like; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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 Proteomics identification; Reference proteome; Signal; Transmembrane; KW 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 44..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 60..63 FT /evidence="ECO:0007829|PDB:8JP4" 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:3WHT" FT STRAND 146..152 FT /evidence="ECO:0007829|PDB:4YGB" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:4GKY" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:4YGB" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:3A4U" 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..267 FT /evidence="ECO:0007829|PDB:4YGB" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:8JP5" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:8JP9" FT HELIX 283..308 FT /evidence="ECO:0007829|PDB:8JP4" FT TURN 320..322 FT /evidence="ECO:0007829|PDB:8JP4" FT HELIX 326..366 FT /evidence="ECO:0007829|PDB:8JP4" 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 //