LMAN1_CHLAE
ID LMAN1_CHLAE Reviewed; 510 AA.
AC Q9TU32;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein ERGIC-53;
DE AltName: Full=ER-Golgi intermediate compartment 53 kDa protein;
DE AltName: Full=Lectin mannose-binding 1;
DE Flags: Precursor;
GN Name=LMAN1; Synonyms=ERGIC53;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10542336; DOI=10.1016/s0167-4781(99)00177-3;
RA Sarnataro S., Caporaso M.G., Bonatti S., Remondelli P.;
RT "Sequence and expression of the monkey homologue of the ER-Golgi
RT intermediate compartment lectin, ERGIC-53.";
RL Biochim. Biophys. Acta 1447:334-340(1999).
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 -!- INTERACTION:
CC Q9TU32; Q8NI22: MCFD2; Xeno; NbExp=2; IntAct=EBI-25399342, EBI-2689785;
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-501 for
CC proper recognition of COPII coat components. {ECO:0000250}.
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DR EMBL; AF160877; AAF13155.1; -; mRNA.
DR AlphaFoldDB; Q9TU32; -.
DR SMR; Q9TU32; -.
DR IntAct; Q9TU32; 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005537; F:mannose binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
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 Disulfide bond; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Lectin; Membrane; Metal-binding; Phosphoprotein; Protein transport; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..510
FT /note="Protein ERGIC-53"
FT /id="PRO_0000017659"
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:0000250|UniProtKB:P49257"
FT MOTIF 509..510
FT /note="ER export motif"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
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 /evidence="ECO:0000250"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49257"
FT DISULFID 190..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT DISULFID 466
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT DISULFID 475
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
SQ SEQUENCE 510 AA; 57391 MW; 02D82CD3C89E4F5F CRC64;
MAGSRRRGLQ ARVRPLFCAL LLSLSRFVGG DGVGGDPAAG LPHRRFEYKY SFKGPHLVQS
DGTVPFWAHA GNAIPSSDQI RVAPSLKSQR GSVWTKAKAA FENWEVEVTF RVTGRGRIGA
DGLAIWYTEN QGLEGPVFGS ADLWNGVGIF FDSFDNDGKK NNPAIVIIGN NGQIHYDHQN
DGASQALASC QRDFRNKPYP VRAKIIYYQK TLTVMINNGF TPDKNDYEFC AKVENMIIPA
QGHFGVSAAT GGLADDHDVL SFLTFQLTEP GKEPPTPDKE ISEKEKEKYQ EEFEHFQQEL
DKKKEEFQKG HPDLQGQPAE EIFESVGDRE LRQVFEGQNR IHLEIKQLNR QLDMILDEQR
RYVSSLTEEI SKRGAGMPGQ HGQISQQELD TVVKTQHEIL RQVNEMKNSM SETVRLVSGM
QHPGSAGGVY ETAQHFADIK EHLHTVKRDI DNLVQRHMLS NEKPKCPELP PFPSCLSTVH
FIIFVVVQTV LFIGYIMYRS QQEAAAKKFF
