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Protein

Protein ERGIC-53

Gene

Lman1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei96CarbohydratePROSITE-ProRule annotation1
Binding sitei129CarbohydratePROSITE-ProRule annotation1
Metal bindingi160Calcium 11
Metal bindingi162Calcium 1; via carbonyl oxygen1
Metal bindingi163Calcium 21
Metal bindingi164Calcium 11
Binding sitei164CarbohydratePROSITE-ProRule annotation1
Metal bindingi165Calcium 21
Metal bindingi169Calcium 21
Metal bindingi170Calcium 21
Binding sitei186CarbohydratePROSITE-ProRule annotation1
Metal bindingi189Calcium 11
Metal bindingi189Calcium 21
Sitei508Required for ER exportBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: RGD
  • identical protein binding Source: RGD
  • mannose binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

Lectin, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ERGIC-53
Alternative name(s):
ER-Golgi intermediate compartment 53 kDa protein
Lectin mannose-binding 1
p58
Gene namesi
Name:Lman1
Synonyms:Ergic53
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71020. Lman1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini31 – 484LumenalSequence analysisAdd BLAST454
Transmembranei485 – 505HelicalSequence analysisAdd BLAST21
Topological domaini506 – 517CytoplasmicSequence analysisAdd BLAST12

GO - Cellular componenti

  • endoplasmic reticulum Source: RGD
  • endoplasmic reticulum-Golgi intermediate compartment Source: RGD
  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
  • endoplasmic reticulum membrane Source: GO_Central
  • ER to Golgi transport vesicle Source: GO_Central
  • Golgi apparatus Source: RGD
  • Golgi membrane Source: GO_Central
  • integral component of membrane Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000001766231 – 517Protein ERGIC-53Add BLAST487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi198 ↔ 238PROSITE-ProRule annotation2 Publications
Modified residuei433PhosphoserineBy similarity1
Disulfide bondi473InterchainPROSITE-ProRule annotation
Disulfide bondi482InterchainPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ62902.
PeptideAtlasiQ62902.
PRIDEiQ62902.

PTM databases

iPTMnetiQ62902.
PhosphoSitePlusiQ62902.

Interactioni

Subunit structurei

Exists both as a covalent disulfide-linked homohexamer, and a complex of three disulfide-linked dimers non-covalently kept together. Interacts with MCFD2. May interact with TMEM115.By similarity

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

BioGridi250550. 1 interactor.
IntActiQ62902. 5 interactors.
MINTiMINT-4571318.
STRINGi10116.ENSRNOP00000035966.

Structurei

Secondary structure

1517
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 46Combined sources4
Beta strandi51 – 54Combined sources4
Helixi56 – 58Combined sources3
Beta strandi60 – 64Combined sources5
Beta strandi75 – 79Combined sources5
Beta strandi88 – 91Combined sources4
Beta strandi98 – 105Combined sources8
Beta strandi110 – 121Combined sources12
Beta strandi123 – 125Combined sources3
Beta strandi130 – 138Combined sources9
Beta strandi153 – 160Combined sources8
Beta strandi172 – 180Combined sources9
Helixi186 – 193Combined sources8
Beta strandi195 – 198Combined sources4
Beta strandi209 – 216Combined sources8
Beta strandi219 – 225Combined sources7
Beta strandi227 – 230Combined sources4
Beta strandi236 – 241Combined sources6
Beta strandi248 – 257Combined sources10
Beta strandi264 – 276Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GV9X-ray1.46A25-284[»]
1R1ZX-ray2.40A/B/C/D43-284[»]
ProteinModelPortaliQ62902.
SMRiQ62902.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62902.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini52 – 275L-type lectin-likePROSITE-ProRule annotationAdd BLAST224

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni259 – 261Carbohydrate bindingPROSITE-ProRule annotation3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi516 – 517ER export motifBy similarity2

Domaini

The FF ER export motif at the C-terminus is not sufficient to support endoplasmic reticulum exit, and needs assistance of Gln-508 for proper recognition of COPII coat components.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3838. Eukaryota.
ENOG410ZFRX. LUCA.
HOGENOMiHOG000017354.
HOVERGENiHBG052332.
InParanoidiQ62902.
KOiK10080.
PhylomeDBiQ62902.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR005052. Lectin_leg.
IPR033085. LMAN1.
[Graphical view]
PANTHERiPTHR12223:SF32. PTHR12223:SF32. 1 hit.
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.

Q62902-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSRRRGPQ AGAQSFFCAL LLSFSQFVGS DGMGGDAAAP GAAGTQAELP
60 70 80 90 100
HRRFEYKYSF KGPHLVQSDG TVPFWAHAGN AIPSADQIRI APSLKSQRGS
110 120 130 140 150
VWTKTKAAFE NWEVEVTFRV TGRGRIGADG LAIWYTENQG LDGPVFGSAD
160 170 180 190 200
MWNGVGIFFD SFDNDGKKNN PAIVVVGNNG QINYDHQNDG ATQALASCQR
210 220 230 240 250
DFRNKPYPVR AKITYYQKTL TVMINNGFTP DKNDYEFCAK VENMVIPTQG
260 270 280 290 300
HFGISAATGG LADDHDVLSF LTFQLTEPGK EPPTPEKDIS EKEKEKYQEE
310 320 330 340 350
FEHFQQELDK KKEEFQKGHP DLQGQPADDI FESIGDRELR QVFEGQNRIH
360 370 380 390 400
LEIKQLNRQL DMILDEQRRY VSSLTEEISR RGAGTPGQPG QVSQQELDTV
410 420 430 440 450
VRTQLEILRQ VNEMKNSMRE TMRLVSGVQH PGSAGVYETT QHFMDIKEHL
460 470 480 490 500
HIVKRDIDSL AQRSMSSNEK PKCPDLPAFP SCLSTVHFVI FIVVQTVLFI
510
GYIMYRTQQE AAAKKFF
Length:517
Mass (Da):57,957
Last modified:November 1, 1996 - v1
Checksum:iDFD9036C6773F7EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44129 mRNA. Translation: AAC52434.1.
RefSeqiNP_446338.1. NM_053886.2.
UniGeneiRn.25734.

Genome annotation databases

GeneIDi116666.
KEGGirno:116666.
UCSCiRGD:71020. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44129 mRNA. Translation: AAC52434.1.
RefSeqiNP_446338.1. NM_053886.2.
UniGeneiRn.25734.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GV9X-ray1.46A25-284[»]
1R1ZX-ray2.40A/B/C/D43-284[»]
ProteinModelPortaliQ62902.
SMRiQ62902.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250550. 1 interactor.
IntActiQ62902. 5 interactors.
MINTiMINT-4571318.
STRINGi10116.ENSRNOP00000035966.

PTM databases

iPTMnetiQ62902.
PhosphoSitePlusiQ62902.

Proteomic databases

PaxDbiQ62902.
PeptideAtlasiQ62902.
PRIDEiQ62902.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi116666.
KEGGirno:116666.
UCSCiRGD:71020. rat.

Organism-specific databases

CTDi3998.
RGDi71020. Lman1.

Phylogenomic databases

eggNOGiKOG3838. Eukaryota.
ENOG410ZFRX. LUCA.
HOGENOMiHOG000017354.
HOVERGENiHBG052332.
InParanoidiQ62902.
KOiK10080.
PhylomeDBiQ62902.

Miscellaneous databases

EvolutionaryTraceiQ62902.
PROiQ62902.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR005052. Lectin_leg.
IPR033085. LMAN1.
[Graphical view]
PANTHERiPTHR12223:SF32. PTHR12223:SF32. 1 hit.
PfamiPF03388. Lectin_leg-like. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51328. L_LECTIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLMAN1_RAT
AccessioniPrimary (citable) accession number: Q62902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 129 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, 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.