LMAN1_MOUSE
ID LMAN1_MOUSE Reviewed; 517 AA.
AC Q9D0F3;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK011495; BAB27655.1; -; mRNA.
DR EMBL; BC057165; AAH57165.1; -; mRNA.
DR CCDS; CCDS29313.1; -.
DR RefSeq; NP_001165533.1; NM_001172062.1.
DR RefSeq; NP_081676.1; NM_027400.3.
DR AlphaFoldDB; Q9D0F3; -.
DR SMR; Q9D0F3; -.
DR BioGRID; 214001; 10.
DR IntAct; Q9D0F3; 2.
DR MINT; Q9D0F3; -.
DR STRING; 10090.ENSMUSP00000040140; -.
DR iPTMnet; Q9D0F3; -.
DR PhosphoSitePlus; Q9D0F3; -.
DR SwissPalm; Q9D0F3; -.
DR EPD; Q9D0F3; -.
DR jPOST; Q9D0F3; -.
DR MaxQB; Q9D0F3; -.
DR PaxDb; Q9D0F3; -.
DR PeptideAtlas; Q9D0F3; -.
DR PRIDE; Q9D0F3; -.
DR ProteomicsDB; 292102; -.
DR Antibodypedia; 1115; 290 antibodies from 32 providers.
DR DNASU; 70361; -.
DR Ensembl; ENSMUST00000048260; ENSMUSP00000040140; ENSMUSG00000041891.
DR Ensembl; ENSMUST00000120461; ENSMUSP00000113326; ENSMUSG00000041891.
DR Ensembl; ENSMUST00000236866; ENSMUSP00000158495; ENSMUSG00000041891.
DR GeneID; 70361; -.
DR KEGG; mmu:70361; -.
DR UCSC; uc008ffn.2; mouse.
DR CTD; 3998; -.
DR MGI; MGI:1917611; Lman1.
DR VEuPathDB; HostDB:ENSMUSG00000041891; -.
DR eggNOG; KOG3838; Eukaryota.
DR GeneTree; ENSGT00940000159146; -.
DR HOGENOM; CLU_041093_4_0_1; -.
DR InParanoid; Q9D0F3; -.
DR OMA; WSAEFQF; -.
DR OrthoDB; 1377709at2759; -.
DR PhylomeDB; Q9D0F3; -.
DR TreeFam; TF313311; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 70361; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Lman1; mouse.
DR PRO; PR:Q9D0F3; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D0F3; protein.
DR Bgee; ENSMUSG00000041891; Expressed in metanephric loop of Henle and 265 other tissues.
DR ExpressionAtlas; Q9D0F3; baseline and differential.
DR Genevisible; Q9D0F3; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0010638; P:positive regulation of organelle organization; ISO:MGI.
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;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..517
FT /note="Protein ERGIC-53"
FT /id="PRO_0000017661"
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 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 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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
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 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"
SQ SEQUENCE 517 AA; 57789 MW; BA9FCFDEBCC5656D CRC64;
MAVSRRRVPQ AGARSFFCAL LLSFSQFTGS DGTGGDAAAP GAAGTQAELP HRRFEYKYSF
KGPHLVQSDG TVPFWAHAGN AIPSADQIRI APSLKSQRGS VWTKAKAAFE NWEVEVTFRV
TGRGRIGADG LAIWYTENQG LDGPVFGSAD TWNGVGIFFD SFDNDGKKNN PAIVVIGNNG
QINYDHQNDG ATQALASCQR DFRNKPYPVR AKITYYQKTL TVMINNGFTP DKNDYEFCAK
VENMVIPTQG HFGISAATGG LADDHDVLSF LTFQLTEPGK EPPTAEKDIS EKEKEKYQEE
FEHFQQELDK KKEEFQKGHP DLQGQPADDI FESIGDRELR QVFEGQNRIH LEIKQLNRQL
DMILDEQRRY VSSLTEEISR RGAGTPGQPG QVSQQELDTV VKSQQEILRQ VNEVKNSMSE
TVRLVSGIQH PGSAGVYETT QHFMDIKEHL HVVKRDIDSL AQRSMPSNEK PKCPDLPPFP
SCLSTIHFVI FVVVQTVLFV GYIMYRTQQE AAAKKFF
