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Vesicular integral-membrane protein VIP36 (Lectin mannose-binding 2) (Vesicular integral-membrane protein 36) (VIP36)

 LMAN2_CANLF             Reviewed;         356 AA.
P49256;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 117.
RecName: Full=Vesicular integral-membrane protein VIP36;
AltName: Full=Lectin mannose-binding 2;
AltName: Full=Vesicular integral-membrane protein 36;
Short=VIP36;
Flags: Precursor;
Name=LMAN2;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 45-55 AND 304-314.
STRAIN=Cocker spaniel; TISSUE=Kidney;
PubMed=8157011;
Fiedler K., Parton R.G., Kellner R., Etzold T., Simons K.;
"VIP36, a novel component of glycolipid rafts and exocytic carrier
vesicles in epithelial cells.";
EMBO J. 13:1729-1740(1994).
[2]
SIMILARITY TO LEGUMINOUS LECTINS.
PubMed=8205612; DOI=10.1016/0092-8674(94)90047-7;
Fiedler K., Simons K.;
"A putative novel class of animal lectins in the secretory pathway
homologous to leguminous lectins.";
Cell 77:625-626(1994).
[3]
CHARACTERIZATION, AND GLYCOSYLATION AT ASN-183.
PubMed=8834812;
Fiedler K., Simons K.;
"Characterization of VIP36, an animal lectin homologous to leguminous
lectins.";
J. Cell Sci. 109:271-276(1996).
[4]
FUNCTION.
PubMed=11872745; DOI=10.1074/jbc.M112188200;
Hara-Kuge S., Ohkura T., Ideo H., Shimada O., Atsumi S., Yamashita K.;
"Involvement of VIP36 in intracellular transport and secretion of
glycoproteins in polarized Madin-Darby canine kidney (MDCK) cells.";
J. Biol. Chem. 277:16332-16339(2002).
[5]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 51-301 ALONE AND IN COMPLEX
WITH HIGH MANNOSE GLYCANS AND CALCIUM IONS, SUBUNIT, FUNCTION, AND
DISULFIDE BOND.
PubMed=17652092; DOI=10.1074/jbc.M703064200;
Satoh T., Cowieson N.P., Hakamata W., Ideo H., Fukushima K.,
Kurihara M., Kato R., Yamashita K., Wakatsuki S.;
"Structural basis for recognition of high mannose type glycoproteins
by mammalian transport lectin VIP36.";
J. Biol. Chem. 282:28246-28255(2007).
-!- FUNCTION: Plays a role as an intracellular lectin in the early
secretory pathway. Interacts with N-acetyl-D-galactosamine and
high-mannose type glycans and may also bind to O-linked glycans.
Involved in the transport and sorting of glycoproteins carrying
high mannose-type glycans. {ECO:0000269|PubMed:11872745,
ECO:0000269|PubMed:17652092}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 2 calcium ions per subunit.;
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17652092}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I
membrane protein.
-!- TISSUE SPECIFICITY: Expressed in kidney, liver, intestine, lung,
spleen and heart. Low expression in brain.
-----------------------------------------------------------------------
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EMBL; X76392; CAA53977.1; -; mRNA.
RefSeq; NP_001003258.1; NM_001003258.2.
UniGene; Cfa.3799; -.
PDB; 2DUO; X-ray; 1.80 A; A/B=51-301.
PDB; 2DUP; X-ray; 2.10 A; A/B=51-301.
PDB; 2DUQ; X-ray; 1.80 A; A/B=51-301.
PDB; 2DUR; X-ray; 1.65 A; A/B=51-301.
PDB; 2E6V; X-ray; 2.50 A; A/B/C/D/E=51-301.
PDBsum; 2DUO; -.
PDBsum; 2DUP; -.
PDBsum; 2DUQ; -.
PDBsum; 2DUR; -.
PDBsum; 2E6V; -.
ProteinModelPortal; P49256; -.
SMR; P49256; -.
MINT; MINT-4655606; -.
STRING; 9615.ENSCAFP00000040025; -.
iPTMnet; P49256; -.
PaxDb; P49256; -.
PRIDE; P49256; -.
Ensembl; ENSCAFT00000026045; ENSCAFP00000024181; ENSCAFG00000016430.
GeneID; 403938; -.
KEGG; cfa:403938; -.
CTD; 10960; -.
eggNOG; KOG3839; Eukaryota.
eggNOG; ENOG410YH8V; LUCA.
GeneTree; ENSGT00530000062977; -.
HOGENOM; HOG000164540; -.
HOVERGEN; HBG052334; -.
InParanoid; P49256; -.
KO; K10082; -.
EvolutionaryTrace; P49256; -.
Proteomes; UP000002254; Chromosome 4.
Bgee; ENSCAFG00000016430; -.
GO; GO:0030137; C:COPI-coated vesicle; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
CDD; cd06901; lectin_VIP36_VIPL; 1.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR005052; Lectin_leg.
InterPro; IPR035664; VIP36_lectin.
Pfam; PF03388; Lectin_leg-like; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51328; L_LECTIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Golgi apparatus; Lectin; Membrane;
Metal-binding; Protein transport; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 44 {ECO:0000269|PubMed:8157011}.
CHAIN 45 356 Vesicular integral-membrane protein
VIP36.
/FTId=PRO_0000017665.
TOPO_DOM 45 322 Lumenal. {ECO:0000255}.
TRANSMEM 323 345 Helical. {ECO:0000255}.
TOPO_DOM 346 356 Cytoplasmic. {ECO:0000255}.
DOMAIN 52 276 L-type lectin-like. {ECO:0000255|PROSITE-
ProRule:PRU00658}.
REGION 164 166 Carbohydrate binding.
REGION 260 262 Carbohydrate binding.
METAL 162 162 Calcium.
METAL 164 164 Calcium; via carbonyl oxygen.
METAL 166 166 Calcium.
METAL 193 193 Calcium.
BINDING 96 96 Carbohydrate.
BINDING 131 131 Carbohydrate.
BINDING 190 190 Carbohydrate.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8834812}.
DISULFID 202 239 {ECO:0000255|PROSITE-ProRule:PRU00658,
ECO:0000269|PubMed:17652092}.
HELIX 56 58 {ECO:0000244|PDB:2DUR}.
TURN 65 67 {ECO:0000244|PDB:2DUR}.
STRAND 68 71 {ECO:0000244|PDB:2DUR}.
STRAND 74 79 {ECO:0000244|PDB:2DUR}.
STRAND 88 91 {ECO:0000244|PDB:2DUR}.
STRAND 93 105 {ECO:0000244|PDB:2DUR}.
STRAND 110 121 {ECO:0000244|PDB:2DUR}.
STRAND 132 139 {ECO:0000244|PDB:2DUR}.
STRAND 144 150 {ECO:0000244|PDB:2DUR}.
STRAND 155 162 {ECO:0000244|PDB:2DUR}.
STRAND 167 169 {ECO:0000244|PDB:2E6V}.
STRAND 174 184 {ECO:0000244|PDB:2DUR}.
HELIX 190 192 {ECO:0000244|PDB:2DUR}.
HELIX 195 197 {ECO:0000244|PDB:2DUR}.
STRAND 200 203 {ECO:0000244|PDB:2DUR}.
STRAND 213 220 {ECO:0000244|PDB:2DUR}.
STRAND 223 229 {ECO:0000244|PDB:2DUR}.
STRAND 231 234 {ECO:0000244|PDB:2DUR}.
STRAND 237 242 {ECO:0000244|PDB:2DUR}.
STRAND 249 262 {ECO:0000244|PDB:2DUR}.
STRAND 265 275 {ECO:0000244|PDB:2DUR}.
HELIX 282 286 {ECO:0000244|PDB:2DUR}.
HELIX 289 291 {ECO:0000244|PDB:2DUR}.
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


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