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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961CarbohydratePROSITE-ProRule annotation
Binding sitei129 – 1291CarbohydratePROSITE-ProRule annotation
Metal bindingi160 – 1601Calcium 1
Metal bindingi162 – 1621Calcium 1; via carbonyl oxygen
Metal bindingi163 – 1631Calcium 2
Metal bindingi164 – 1641Calcium 1
Binding sitei164 – 1641CarbohydratePROSITE-ProRule annotation
Metal bindingi165 – 1651Calcium 2
Metal bindingi169 – 1691Calcium 2
Metal bindingi170 – 1701Calcium 2
Binding sitei186 – 1861CarbohydratePROSITE-ProRule annotation
Metal bindingi189 – 1891Calcium 1
Metal bindingi189 – 1891Calcium 2
Sitei508 – 5081Required for ER exportBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: RGD
  • protein transport Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 484454LumenalSequence analysisAdd
BLAST
Transmembranei485 – 50521HelicalSequence analysisAdd
BLAST
Topological domaini506 – 51712CytoplasmicSequence analysisAdd
BLAST

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: UniProtKB-SubCell
  • Golgi apparatus Source: RGD
  • Golgi membrane Source: UniProtKB-SubCell
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 517487Protein ERGIC-53PRO_0000017662Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi198 ↔ 238PROSITE-ProRule annotation2 Publications
Modified residuei433 – 4331PhosphoserineBy similarity
Disulfide bondi473 – 473InterchainPROSITE-ProRule annotation
Disulfide bondi482 – 482InterchainPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ62902.
PeptideAtlasiQ62902.
PRIDEiQ62902.

PTM databases

iPTMnetiQ62902.

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 interaction.
IntActiQ62902. 5 interactions.
MINTiMINT-4571318.
STRINGi10116.ENSRNOP00000035966.

Structurei

Secondary structure

1
517
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 464Combined sources
Beta strandi51 – 544Combined sources
Helixi56 – 583Combined sources
Beta strandi60 – 645Combined sources
Beta strandi75 – 795Combined sources
Beta strandi88 – 914Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi110 – 12112Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi153 – 1608Combined sources
Beta strandi172 – 1809Combined sources
Helixi186 – 1938Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi209 – 2168Combined sources
Beta strandi219 – 2257Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi248 – 25710Combined sources
Beta strandi264 – 27613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GV9X-ray1.46A25-284[»]
1R1ZX-ray2.40A/B/C/D43-284[»]
ProteinModelPortaliQ62902.
SMRiQ62902. Positions 43-277.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62902.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 275224L-type lectin-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni259 – 2613Carbohydrate bindingPROSITE-ProRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi516 – 5172ER export motifBy similarity

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1GV9X-ray1.46A25-284[»]
1R1ZX-ray2.40A/B/C/D43-284[»]
ProteinModelPortaliQ62902.
SMRiQ62902. Positions 43-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250550. 1 interaction.
IntActiQ62902. 5 interactions.
MINTiMINT-4571318.
STRINGi10116.ENSRNOP00000035966.

PTM databases

iPTMnetiQ62902.

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...

Publicationsi

  1. "Molecular cloning and expression of a 58-kDa cis-Golgi and intermediate compartment protein."
    Lahtinen U., Hellman U., Wernstedt C., Saraste J., Pettersson R.F.
    J. Biol. Chem. 271:4031-4037(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum."
    Velloso L.M., Svensson K., Schneider G., Pettersson R.F., Lindqvist Y.
    J. Biol. Chem. 277:15979-15984(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS), DISULFIDE BOND.
  3. "The crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding."
    Velloso L.M., Svensson K., Pettersson R.F., Lindqvist Y.
    J. Mol. Biol. 334:845-851(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 43-284 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BOND.

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: July 6, 2016
This is version 126 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.