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Protein

Vesicular integral-membrane protein VIP36

Gene

LMAN2

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Cofactori

Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961Carbohydrate
Binding sitei131 – 1311Carbohydrate
Metal bindingi162 – 1621Calcium
Metal bindingi164 – 1641Calcium; via carbonyl oxygen
Metal bindingi166 – 1661Calcium
Binding sitei190 – 1901Carbohydrate
Metal bindingi193 – 1931Calcium

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicular integral-membrane protein VIP36
Alternative name(s):
Lectin mannose-binding 2
Vesicular integral-membrane protein 36
Short name:
VIP36
Gene namesi
Name:LMAN2
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Chromosome 4

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini45 – 322278LumenalSequence analysisAdd
BLAST
Transmembranei323 – 34523HelicalSequence analysisAdd
BLAST
Topological domaini346 – 35611CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • COPI-coated vesicle Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 44441 PublicationAdd
BLAST
Chaini45 – 356312Vesicular integral-membrane protein VIP36PRO_0000017665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...)1 Publication
Disulfide bondi202 ↔ 239PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP49256.
PRIDEiP49256.

Expressioni

Tissue specificityi

Expressed in kidney, liver, intestine, lung, spleen and heart. Low expression in brain.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

MINTiMINT-4655606.
STRINGi9615.ENSCAFP00000040025.

Structurei

Secondary structure

1
356
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 583Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 714Combined sources
Beta strandi74 – 796Combined sources
Beta strandi88 – 914Combined sources
Beta strandi93 – 10513Combined sources
Beta strandi110 – 12112Combined sources
Beta strandi132 – 1398Combined sources
Beta strandi144 – 1507Combined sources
Beta strandi155 – 1628Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi174 – 18411Combined sources
Helixi190 – 1923Combined sources
Helixi195 – 1973Combined sources
Beta strandi200 – 2034Combined sources
Beta strandi213 – 2208Combined sources
Beta strandi223 – 2297Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi237 – 2426Combined sources
Beta strandi249 – 26214Combined sources
Beta strandi265 – 27511Combined sources
Helixi282 – 2865Combined sources
Helixi289 – 2913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP49256.
SMRiP49256. Positions 51-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49256.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 276225L-type lectin-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 1663Carbohydrate binding
Regioni260 – 2623Carbohydrate binding

Sequence similaritiesi

Contains 1 L-type lectin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3839. Eukaryota.
ENOG410YH8V. LUCA.
GeneTreeiENSGT00530000062977.
HOGENOMiHOG000164540.
HOVERGENiHBG052334.
InParanoidiP49256.
KOiK10082.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR005052. Lectin_leg.
[Graphical view]
PfamiPF03388. Lectin_leg-like. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51328. L_LECTIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49256-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAEGWIWRW GWGRRCLGRP GLPGPGPGPA TPLFLLLLLG PVVADITDGN
60 70 80 90 100
SEHLKREHSL IKPYQGVGSS SMPLWDFQGS TILTSQYVRL TPDERSKEGS
110 120 130 140 150
IWNHQPCFLK DWEMHVHFKV HGTGKKNLHG DGIALWYTRD RLVPGPVFGS
160 170 180 190 200
KDNFHGLAIF LDTYPNDETT ERVFPYISVM VNNGSLSYDH SKDGRWTELA
210 220 230 240 250
GCTADFRNRD HDTFLAVRYS RGRLTVMTDL EDKNEWKNCI DITGVRLPTG
260 270 280 290 300
YYFGASAGTG DLSDNHDIIS MKLFQLMVEH TPDEENIDWT KIEPSVNFLK
310 320 330 340 350
SPKDNVDDPT GNFRSGPLTG WRVFLLLLCA LLGIIVCAVV GAVVFQKRQE

RNKRFY
Length:356
Mass (Da):40,214
Last modified:February 1, 1996 - v1
Checksum:iAD9646E2BCB37A85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76392 mRNA. Translation: CAA53977.1.
RefSeqiNP_001003258.1. NM_001003258.2.
UniGeneiCfa.3799.

Genome annotation databases

EnsembliENSCAFT00000026045; ENSCAFP00000024181; ENSCAFG00000016430.
GeneIDi403938.
KEGGicfa:403938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76392 mRNA. Translation: CAA53977.1.
RefSeqiNP_001003258.1. NM_001003258.2.
UniGeneiCfa.3799.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP49256.
SMRiP49256. Positions 51-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4655606.
STRINGi9615.ENSCAFP00000040025.

Proteomic databases

PaxDbiP49256.
PRIDEiP49256.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000026045; ENSCAFP00000024181; ENSCAFG00000016430.
GeneIDi403938.
KEGGicfa:403938.

Organism-specific databases

CTDi10960.

Phylogenomic databases

eggNOGiKOG3839. Eukaryota.
ENOG410YH8V. LUCA.
GeneTreeiENSGT00530000062977.
HOGENOMiHOG000164540.
HOVERGENiHBG052334.
InParanoidiP49256.
KOiK10082.

Miscellaneous databases

EvolutionaryTraceiP49256.
NextBioi20817428.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR005052. Lectin_leg.
[Graphical view]
PfamiPF03388. Lectin_leg-like. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51328. L_LECTIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiLMAN2_CANLF
AccessioniPrimary (citable) accession number: P49256
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 9, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.