LMAN2_CANLF
ID LMAN2_CANLF Reviewed; 356 AA.
AC P49256;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Vesicular integral-membrane protein VIP36;
DE AltName: Full=Lectin mannose-binding 2;
DE AltName: Full=Vesicular integral-membrane protein 36;
DE Short=VIP36;
DE Flags: Precursor;
GN Name=LMAN2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 45-55 AND 304-314.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=8157011; DOI=10.1002/j.1460-2075.1994.tb06437.x;
RA Fiedler K., Parton R.G., Kellner R., Etzold T., Simons K.;
RT "VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles
RT in epithelial cells.";
RL EMBO J. 13:1729-1740(1994).
RN [2]
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 [3]
RP CHARACTERIZATION, AND GLYCOSYLATION AT ASN-183.
RX PubMed=8834812; DOI=10.1242/jcs.109.1.271;
RA Fiedler K., Simons K.;
RT "Characterization of VIP36, an animal lectin homologous to leguminous
RT lectins.";
RL J. Cell Sci. 109:271-276(1996).
RN [4]
RP FUNCTION.
RX PubMed=11872745; DOI=10.1074/jbc.m112188200;
RA Hara-Kuge S., Ohkura T., Ideo H., Shimada O., Atsumi S., Yamashita K.;
RT "Involvement of VIP36 in intracellular transport and secretion of
RT glycoproteins in polarized Madin-Darby canine kidney (MDCK) cells.";
RL J. Biol. Chem. 277:16332-16339(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 51-301 ALONE AND IN COMPLEX WITH
RP HIGH MANNOSE GLYCANS AND CALCIUM IONS, SUBUNIT, FUNCTION, AND DISULFIDE
RP BOND.
RX PubMed=17652092; DOI=10.1074/jbc.m703064200;
RA Satoh T., Cowieson N.P., Hakamata W., Ideo H., Fukushima K., Kurihara M.,
RA Kato R., Yamashita K., Wakatsuki S.;
RT "Structural basis for recognition of high mannose type glycoproteins by
RT mammalian transport lectin VIP36.";
RL J. Biol. Chem. 282:28246-28255(2007).
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. {ECO:0000269|PubMed:11872745, ECO:0000269|PubMed:17652092}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17652092}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, intestine, lung, spleen
CC and heart. Low expression in brain.
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DR EMBL; X76392; CAA53977.1; -; mRNA.
DR RefSeq; NP_001003258.1; NM_001003258.2.
DR PDB; 2DUO; X-ray; 1.80 A; A/B=51-301.
DR PDB; 2DUP; X-ray; 2.10 A; A/B=51-301.
DR PDB; 2DUQ; X-ray; 1.80 A; A/B=51-301.
DR PDB; 2DUR; X-ray; 1.65 A; A/B=51-301.
DR PDB; 2E6V; X-ray; 2.50 A; A/B/C/D/E=51-301.
DR PDBsum; 2DUO; -.
DR PDBsum; 2DUP; -.
DR PDBsum; 2DUQ; -.
DR PDBsum; 2DUR; -.
DR PDBsum; 2E6V; -.
DR AlphaFoldDB; P49256; -.
DR SMR; P49256; -.
DR STRING; 9612.ENSCAFP00000040025; -.
DR UniLectin; P49256; -.
DR iPTMnet; P49256; -.
DR PaxDb; P49256; -.
DR PRIDE; P49256; -.
DR Ensembl; ENSCAFT00000047011; ENSCAFP00000040025; ENSCAFG00000016430.
DR Ensembl; ENSCAFT00030005676; ENSCAFP00030005052; ENSCAFG00030003029.
DR Ensembl; ENSCAFT00040028322; ENSCAFP00040024605; ENSCAFG00040015376.
DR Ensembl; ENSCAFT00845018663; ENSCAFP00845014570; ENSCAFG00845010502.
DR GeneID; 403938; -.
DR KEGG; cfa:403938; -.
DR CTD; 10960; -.
DR VEuPathDB; HostDB:ENSCAFG00845010502; -.
DR VGNC; VGNC:42708; LMAN2.
DR eggNOG; KOG3839; Eukaryota.
DR GeneTree; ENSGT00940000158355; -.
DR HOGENOM; CLU_041093_0_0_1; -.
DR InParanoid; P49256; -.
DR OrthoDB; 1377709at2759; -.
DR Reactome; R-CFA-204005; COPII-mediated vesicle transport.
DR Reactome; R-CFA-5694530; Cargo concentration in the ER.
DR EvolutionaryTrace; P49256; -.
DR Proteomes; UP000002254; Chromosome 4.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
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; 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; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:Ensembl.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Lectin; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..44
FT /evidence="ECO:0000269|PubMed:8157011"
FT CHAIN 45..356
FT /note="Vesicular integral-membrane protein VIP36"
FT /id="PRO_0000017665"
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 BINDING 131
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 164..166
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 190
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 260..262
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8834812"
FT DISULFID 202..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00658,
FT ECO:0000269|PubMed:17652092"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2DUR"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 93..105
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 110..121
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2E6V"
FT STRAND 174..184
FT /evidence="ECO:0007829|PDB:2DUR"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2DUR"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 249..262
FT /evidence="ECO:0007829|PDB:2DUR"
FT STRAND 265..275
FT /evidence="ECO:0007829|PDB:2DUR"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:2DUR"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2DUR"
SQ SEQUENCE 356 AA; 40214 MW; AD9646E2BCB37A85 CRC64;
MAAEGWIWRW GWGRRCLGRP GLPGPGPGPA TPLFLLLLLG PVVADITDGN SEHLKREHSL
IKPYQGVGSS SMPLWDFQGS TILTSQYVRL TPDERSKEGS IWNHQPCFLK DWEMHVHFKV
HGTGKKNLHG DGIALWYTRD RLVPGPVFGS KDNFHGLAIF LDTYPNDETT ERVFPYISVM
VNNGSLSYDH SKDGRWTELA GCTADFRNRD HDTFLAVRYS RGRLTVMTDL EDKNEWKNCI
DITGVRLPTG YYFGASAGTG DLSDNHDIIS MKLFQLMVEH TPDEENIDWT KIEPSVNFLK
SPKDNVDDPT GNFRSGPLTG WRVFLLLLCA LLGIIVCAVV GAVVFQKRQE RNKRFY
