Skip Header

Contribute Send feedback
Read comments (?) or add your own

P49256 (LMAN2_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vesicular integral-membrane protein VIP36
Alternative name(s):
Lectin mannose-binding 2
Vesicular integral-membrane protein 36
Short name=VIP36
Gene names
Name:LMAN2
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.5

Cofactor

Binds 2 calcium ions per subunit.

Subunit structure

Monomer. Ref.5

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.

Sequence similarities

Contains 1 L-type lectin-like domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentGolgi apparatus
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCalcium
Lectin
Metal-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4444 Ref.1
Chain45 – 356312Vesicular integral-membrane protein VIP36
PRO_0000017665

Regions

Topological domain45 – 322278Lumenal Potential
Transmembrane323 – 34523Helical; Potential
Topological domain346 – 35611Cytoplasmic Potential
Domain52 – 276225L-type lectin-like
Region164 – 1663Carbohydrate binding
Region260 – 2623Carbohydrate binding

Sites

Metal binding1621Calcium
Metal binding1641Calcium; via carbonyl oxygen
Metal binding1661Calcium
Metal binding1931Calcium
Binding site961Carbohydrate
Binding site1311Carbohydrate
Binding site1901Carbohydrate

Amino acid modifications

Glycosylation1831N-linked (GlcNAc...) Ref.3
Disulfide bond202 ↔ 239 Ref.5

Secondary structure

1 .............................................. 356
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49256 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: AD9646E2BCB37A85

FASTA35640,214
        10         20         30         40         50         60 
MAAEGWIWRW GWGRRCLGRP GLPGPGPGPA TPLFLLLLLG PVVADITDGN SEHLKREHSL 

        70         80         90        100        110        120 
IKPYQGVGSS SMPLWDFQGS TILTSQYVRL TPDERSKEGS IWNHQPCFLK DWEMHVHFKV 

       130        140        150        160        170        180 
HGTGKKNLHG DGIALWYTRD RLVPGPVFGS KDNFHGLAIF LDTYPNDETT ERVFPYISVM 

       190        200        210        220        230        240 
VNNGSLSYDH SKDGRWTELA GCTADFRNRD HDTFLAVRYS RGRLTVMTDL EDKNEWKNCI 

       250        260        270        280        290        300 
DITGVRLPTG YYFGASAGTG DLSDNHDIIS MKLFQLMVEH TPDEENIDWT KIEPSVNFLK 

       310        320        330        340        350 
SPKDNVDDPT GNFRSGPLTG WRVFLLLLCA LLGIIVCAVV GAVVFQKRQE RNKRFY

« Hide

References

[1]"VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells."
Fiedler K., Parton R.G., Kellner R., Etzold T., Simons K.
EMBO J. 13:1729-1740(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-55 AND 304-314.
Strain: Cocker spaniel.
Tissue: Kidney.
[2]"A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins."
Fiedler K., Simons K.
Cell 77:625-626(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO LEGUMINOUS LECTINS.
[3]"Characterization of VIP36, an animal lectin homologous to leguminous lectins."
Fiedler K., Simons K.
J. Cell Sci. 109:271-276(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, GLYCOSYLATION AT ASN-183.
[4]"Involvement of VIP36 in intracellular transport and secretion of glycoproteins in polarized Madin-Darby canine kidney (MDCK) cells."
Hara-Kuge S., Ohkura T., Ideo H., Shimada O., Atsumi S., Yamashita K.
J. Biol. Chem. 277:16332-16339(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36."
Satoh T., Cowieson N.P., Hakamata W., Ideo H., Fukushima K., Kurihara M., Kato R., Yamashita K., Wakatsuki S.
J. Biol. Chem. 282:28246-28255(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 51-301 ALONE AND IN COMPLEX WITH HIGH MANNOSE GLYCANS AND CALCIUM IONS, SUBUNIT, FUNCTION, DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X76392 mRNA. Translation: CAA53977.1.
RefSeqNP_001003258.1. NM_001003258.2.
UniGeneCfa.3799.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DUOX-ray1.80A/B51-301[»]
2DUPX-ray2.10A/B51-301[»]
2DUQX-ray1.80A/B51-301[»]
2DURX-ray1.65A/B51-301[»]
2E6VX-ray2.50A/B/C/D/E51-301[»]
ProteinModelPortalP49256.
SMRP49256. Positions 51-301.
ModBaseSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000024181.

Proteomic databases

PaxDbP49256.
PRIDEP49256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000026045; ENSCAFP00000024181; ENSCAFG00000016430.
GeneID403938.
KEGGcfa:403938.

Organism-specific databases

CTD10960.

Phylogenomic databases

eggNOGNOG237434.
GeneTreeENSGT00530000062977.
HOGENOMHOG000164540.
HOVERGENHBG052334.
InParanoidP49256.
KOK10082.
OrthoDBEOG4Z0B63.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR005052. Lectin_leg.
[Graphical view]
PANTHERPTHR12223. PTHR12223. 1 hit.
PfamPF03388. Lectin_leg-like. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS51328. L_LECTIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP49256.
NextBio20817428.

Entry information

Entry nameLMAN2_CANFA
AccessionPrimary (citable) accession number: P49256
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents