LMAN1_RAT
ID LMAN1_RAT Reviewed; 517 AA.
AC Q62902;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein ERGIC-53;
DE AltName: Full=ER-Golgi intermediate compartment 53 kDa protein;
DE AltName: Full=Lectin mannose-binding 1;
DE AltName: Full=p58;
DE Flags: Precursor;
GN Name=Lman1; Synonyms=Ergic53;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8626736; DOI=10.1074/jbc.271.8.4031;
RA Lahtinen U., Hellman U., Wernstedt C., Saraste J., Pettersson R.F.;
RT "Molecular cloning and expression of a 58-kDa cis-Golgi and intermediate
RT compartment protein.";
RL J. Biol. Chem. 271:4031-4037(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=11850423; DOI=10.1074/jbc.m112098200;
RA Velloso L.M., Svensson K., Schneider G., Pettersson R.F., Lindqvist Y.;
RT "Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53,
RT a protein involved in glycoprotein export from the endoplasmic reticulum.";
RL J. Biol. Chem. 277:15979-15984(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 43-284 IN COMPLEX WITH CALCIUM
RP IONS, AND DISULFIDE BOND.
RX PubMed=14643651; DOI=10.1016/j.jmb.2003.10.031;
RA Velloso L.M., Svensson K., Pettersson R.F., Lindqvist Y.;
RT "The crystal structure of the carbohydrate-recognition domain of the
RT glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-
RT binding site and conformational changes associated with calcium ion
RT binding.";
RL J. Mol. Biol. 334:845-851(2003).
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 (By similarity).
CC {ECO:0000250}.
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. Interacts with UBXN6. Interacts with
CC SERPINA1/alpha1-antitrypsin (By similarity).
CC {ECO:0000250|UniProtKB:P49257}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
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-508 for
CC proper recognition of COPII coat components. {ECO:0000250}.
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DR EMBL; U44129; AAC52434.1; -; mRNA.
DR RefSeq; NP_446338.1; NM_053886.2.
DR PDB; 1GV9; X-ray; 1.46 A; A=25-284.
DR PDB; 1R1Z; X-ray; 2.40 A; A/B/C/D=43-284.
DR PDBsum; 1GV9; -.
DR PDBsum; 1R1Z; -.
DR AlphaFoldDB; Q62902; -.
DR SMR; Q62902; -.
DR BioGRID; 250550; 1.
DR IntAct; Q62902; 6.
DR MINT; Q62902; -.
DR STRING; 10116.ENSRNOP00000035966; -.
DR UniLectin; Q62902; -.
DR iPTMnet; Q62902; -.
DR PhosphoSitePlus; Q62902; -.
DR jPOST; Q62902; -.
DR PaxDb; Q62902; -.
DR PeptideAtlas; Q62902; -.
DR PRIDE; Q62902; -.
DR GeneID; 116666; -.
DR KEGG; rno:116666; -.
DR UCSC; RGD:71020; rat.
DR CTD; 3998; -.
DR RGD; 71020; Lman1.
DR eggNOG; KOG3838; Eukaryota.
DR InParanoid; Q62902; -.
DR OrthoDB; 1377709at2759; -.
DR PhylomeDB; Q62902; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR EvolutionaryTrace; Q62902; -.
DR PRO; PR:Q62902; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0030017; C:sarcomere; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; TAS:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0010638; P:positive regulation of organelle organization; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR DisProt; DP02789; -.
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; Disulfide bond; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Lectin; Membrane; Metal-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..517
FT /note="Protein ERGIC-53"
FT /id="PRO_0000017662"
FT TOPO_DOM 31..484
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 52..275
FT /note="L-type lectin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT REGION 276..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..517
FT /note="Mediates interaction with RAB3GAP1, RAB3GAP2 and
FT UBXN6"
FT /evidence="ECO:0000250|UniProtKB:P49257"
FT MOTIF 516..517
FT /note="ER export motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 281..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 129
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 164
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 186
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 259..261
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT SITE 508
FT /note="Required for ER export"
FT /evidence="ECO:0000250"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49257"
FT DISULFID 198..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658,
FT ECO:0000269|PubMed:11850423, ECO:0000269|PubMed:14643651"
FT DISULFID 473
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT DISULFID 482
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1R1Z"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1GV9"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:1R1Z"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 110..121
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:1GV9"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1R1Z"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:1GV9"
FT STRAND 264..276
FT /evidence="ECO:0007829|PDB:1GV9"
SQ SEQUENCE 517 AA; 57957 MW; DFD9036C6773F7EE CRC64;
MAVSRRRGPQ AGAQSFFCAL LLSFSQFVGS DGMGGDAAAP GAAGTQAELP HRRFEYKYSF
KGPHLVQSDG TVPFWAHAGN AIPSADQIRI APSLKSQRGS VWTKTKAAFE NWEVEVTFRV
TGRGRIGADG LAIWYTENQG LDGPVFGSAD MWNGVGIFFD SFDNDGKKNN PAIVVVGNNG
QINYDHQNDG ATQALASCQR DFRNKPYPVR AKITYYQKTL TVMINNGFTP DKNDYEFCAK
VENMVIPTQG HFGISAATGG LADDHDVLSF LTFQLTEPGK EPPTPEKDIS EKEKEKYQEE
FEHFQQELDK KKEEFQKGHP DLQGQPADDI FESIGDRELR QVFEGQNRIH LEIKQLNRQL
DMILDEQRRY VSSLTEEISR RGAGTPGQPG QVSQQELDTV VRTQLEILRQ VNEMKNSMRE
TMRLVSGVQH PGSAGVYETT QHFMDIKEHL HIVKRDIDSL AQRSMSSNEK PKCPDLPAFP
SCLSTVHFVI FIVVQTVLFI GYIMYRTQQE AAAKKFF
