LMAN2_HUMAN
ID LMAN2_HUMAN Reviewed; 356 AA.
AC Q12907; Q53HH1;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Vesicular integral-membrane protein VIP36;
DE AltName: Full=Glycoprotein GP36b;
DE AltName: Full=Lectin mannose-binding 2;
DE AltName: Full=Vesicular integral-membrane protein 36;
DE Short=VIP36;
DE Flags: Precursor;
GN Name=LMAN2; Synonyms=C5orf8;
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].
RA Hartmann E., Reimann B., Goerlich D., Rapoport T.A., Prehn S.;
RT "Human GP36b glycoprotein of the endoplasmic reticulum.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Smooth muscle;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10444376; DOI=10.1242/jcs.112.17.2813;
RA Fullekrug J., Scheiffele P., Simons K.;
RT "VIP36 localisation to the early secretory pathway.";
RL J. Cell Sci. 112:2813-2821(1999).
RN [5]
RP GLYCOSYLATION AT ASN-183.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [6]
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 [7]
RP IDENTIFICATION BY 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 [8]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-44, 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).
CC -!- FUNCTION: Plays a role as an intracellular lectin in the early
CC secretory pathway. Interacts with N-acetyl-D-galactosamine and high-
CC mannose type glycans and may also bind to O-linked glycans. Involved in
CC the transport and sorting of glycoproteins carrying high mannose-type
CC glycans (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:10444376}; Single-pass type I
CC membrane protein {ECO:0000269|PubMed:10444376}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:10444376}; Single-pass membrane protein
CC {ECO:0000269|PubMed:10444376}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10444376}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:10444376}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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; U10362; AAA19572.1; -; mRNA.
DR EMBL; AK222609; BAD96329.1; -; mRNA.
DR EMBL; BC017263; AAH17263.1; -; mRNA.
DR CCDS; CCDS4417.1; -.
DR PIR; G01447; G01447.
DR RefSeq; NP_006807.1; NM_006816.2.
DR AlphaFoldDB; Q12907; -.
DR SMR; Q12907; -.
DR BioGRID; 116159; 117.
DR IntAct; Q12907; 25.
DR MINT; Q12907; -.
DR STRING; 9606.ENSP00000303366; -.
DR GlyConnect; 1892; 9 N-Linked glycans (1 site).
DR GlyGen; Q12907; 3 sites, 10 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q12907; -.
DR PhosphoSitePlus; Q12907; -.
DR SwissPalm; Q12907; -.
DR BioMuta; LMAN2; -.
DR DMDM; 21264108; -.
DR EPD; Q12907; -.
DR jPOST; Q12907; -.
DR MassIVE; Q12907; -.
DR MaxQB; Q12907; -.
DR PaxDb; Q12907; -.
DR PeptideAtlas; Q12907; -.
DR PRIDE; Q12907; -.
DR ProteomicsDB; 59020; -.
DR TopDownProteomics; Q12907; -.
DR Antibodypedia; 1119; 159 antibodies from 24 providers.
DR DNASU; 10960; -.
DR Ensembl; ENST00000303127.12; ENSP00000303366.7; ENSG00000169223.15.
DR GeneID; 10960; -.
DR KEGG; hsa:10960; -.
DR MANE-Select; ENST00000303127.12; ENSP00000303366.7; NM_006816.3; NP_006807.1.
DR UCSC; uc003mge.4; human.
DR CTD; 10960; -.
DR DisGeNET; 10960; -.
DR GeneCards; LMAN2; -.
DR HGNC; HGNC:16986; LMAN2.
DR HPA; ENSG00000169223; Low tissue specificity.
DR MIM; 609551; gene.
DR neXtProt; NX_Q12907; -.
DR OpenTargets; ENSG00000169223; -.
DR PharmGKB; PA25919; -.
DR VEuPathDB; HostDB:ENSG00000169223; -.
DR eggNOG; KOG3839; Eukaryota.
DR GeneTree; ENSGT00940000158355; -.
DR InParanoid; Q12907; -.
DR OMA; QGWIFSR; -.
DR OrthoDB; 1377709at2759; -.
DR PhylomeDB; Q12907; -.
DR TreeFam; TF313311; -.
DR PathwayCommons; Q12907; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR SignaLink; Q12907; -.
DR SIGNOR; Q12907; -.
DR BioGRID-ORCS; 10960; 27 hits in 1081 CRISPR screens.
DR ChiTaRS; LMAN2; human.
DR GeneWiki; LMAN2; -.
DR GenomeRNAi; 10960; -.
DR Pharos; Q12907; Tbio.
DR PRO; PR:Q12907; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q12907; protein.
DR Bgee; ENSG00000169223; Expressed in stromal cell of endometrium and 202 other tissues.
DR ExpressionAtlas; Q12907; baseline and differential.
DR Genevisible; Q12907; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR CDD; cd06901; lectin_VIP36_VIPL; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR005052; Lectin_leg.
DR InterPro; IPR035664; VIP36_lectin.
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 Calcium; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Lectin; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..44
FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT CHAIN 45..356
FT /note="Vesicular integral-membrane protein VIP36"
FT /id="PRO_0000017666"
FT TOPO_DOM 45..322
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 52..276
FT /note="L-type lectin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 96
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 131
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
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..166
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 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 190
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT BINDING 260..262
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT DISULFID 202..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658"
FT CONFLICT 266
FT /note="H -> R (in Ref. 2; BAD96329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 40229 MW; 196193C8E655141C CRC64;
MAAEGWIWRW GWGRRCLGRP GLLGPGPGPT TPLFLLLLLG SVTADITDGN SEHLKREHSL
IKPYQGVGSS SMPLWDFQGS TMLTSQYVRL TPDERSKEGS IWNHQPCFLK DWEMHVHFKV
HGTGKKNLHG DGIALWYTRD RLVPGPVFGS KDNFHGLAIF LDTYPNDETT ERVFPYISVM
VNNGSLSYDH SKDGRWTELA GCTADFRNRD HDTFLAVRYS RGRLTVMTDL EDKNEWKNCI
DITGVRLPTG YYFGASAGTG DLSDNHDIIS MKLFQLMVEH TPDEESIDWT KIEPSVNFLK
SPKDNVDDPT GNFRSGPLTG WRVFLLLLCA LLGIVVCAVV GAVVFQKRQE RNKRFY
