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Protein

Embigin

Gene

Emb

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

Functioni

Plays a role in the outgrowth of motoneurons and in the formation of neuromuscular junctions. Following muscle denervation, promotes nerve terminal sprouting and the formation of additional acetylcholine receptor clusters at synaptic sites without affecting terminal Schwann cell number or morphology. Delays the retraction of terminal sprouts following re-innervation of denervated endplates (By similarity). Plays a role in targeting the monocarboxylate transporters SLC16A1 and SLC16A7 to the cell membrane.By similarity2 Publications

GO - Biological processi

  • cell adhesion Source: RGD
  • plasma membrane lactate transport Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Embigin
Gene namesi
Name:Emb
Synonyms:Gp70
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621067. Emb.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 264231ExtracellularSequence analysisAdd
BLAST
Transmembranei265 – 28521HelicalSequence analysisAdd
BLAST
Topological domaini286 – 32843CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • integral component of plasma membrane Source: UniProtKB
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence analysisAdd
BLAST
Chaini34 – 328295EmbiginPRO_0000014751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence analysis
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence analysis
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi88 ↔ 144PROSITE-ProRule annotation
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi180 ↔ 238PROSITE-ProRule annotation
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence analysis
Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence analysis
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence analysis
Modified residuei310 – 3101PhosphoserineCombined sources

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO88775.
PRIDEiO88775.

PTM databases

PhosphoSiteiO88775.

Expressioni

Tissue specificityi

Detected in prostate, mammary gland and erythrocytes (at protein level). Detected in testis, brain, prostate, heart, kidney, liver, mammary gland and lung.2 Publications

Inductioni

Regulated by muscle activity. Strongly up-regulated after muscle denervation, including that of soleus muscle. Expression is significantly increased 3 days after denervation and reaches a maximum, about 130-fold increase, after 5 days.1 Publication

Interactioni

Subunit structurei

Interacts with SLC16A1 and SLC16A7.4 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015306.

Structurei

3D structure databases

ProteinModelPortaliO88775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 16094Ig-like 1Add
BLAST
Domaini159 – 25496Ig-like 2Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IVBC. Eukaryota.
ENOG41120A3. LUCA.
HOGENOMiHOG000082417.
HOVERGENiHBG051471.
InParanoidiO88775.
OMAiSKQMGSY.
OrthoDBiEOG7ZKSC2.
PhylomeDBiO88775.
TreeFamiTF326759.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR027114. Embigin.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PANTHERiPTHR10075:SF4. PTHR10075:SF4. 1 hit.
SMARTiSM00409. IG. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O88775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSHTGLRAL VAPGCSLLLL YLLAATRPDR AVGDPADSAF TSLPVREEMM
60 70 80 90 100
AKYANLSLET YNISLTEQTR VSEQNITLER PSHLELECTF TATEDVMSMN
110 120 130 140 150
VTWKKDDALL ETTDGFNTTK MGDTLYSQYR FTVFNSKQMG KYSCFLGEEL
160 170 180 190 200
RGTFNIRVPK VHGKNKPLIT YVGDSTVLKC ECQNCLPLNW TWYMSNGTAQ
210 220 230 240 250
VPIDVHVNDK FDINGSYANE TKLKVKHLLE EDGGSYWCRA AFPLGESEEH
260 270 280 290 300
IKLVVLSFMV PLKPFLAIIA EVILLVAIIL LCEVYTQKKK NDPDDGKEFE
310 320
QIEQLKSDDS NGIENNVPRY RKTDSGDQ
Length:328
Mass (Da):37,005
Last modified:November 1, 1998 - v1
Checksum:iC749A847ACE374B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009698 mRNA. Translation: CAA08796.1.
BC061846 mRNA. Translation: AAH61846.1.
RefSeqiNP_446171.1. NM_053719.1.
UniGeneiRn.16221.

Genome annotation databases

GeneIDi114511.
KEGGirno:114511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009698 mRNA. Translation: CAA08796.1.
BC061846 mRNA. Translation: AAH61846.1.
RefSeqiNP_446171.1. NM_053719.1.
UniGeneiRn.16221.

3D structure databases

ProteinModelPortaliO88775.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015306.

PTM databases

PhosphoSiteiO88775.

Proteomic databases

PaxDbiO88775.
PRIDEiO88775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi114511.
KEGGirno:114511.

Organism-specific databases

CTDi133418.
RGDi621067. Emb.

Phylogenomic databases

eggNOGiENOG410IVBC. Eukaryota.
ENOG41120A3. LUCA.
HOGENOMiHOG000082417.
HOVERGENiHBG051471.
InParanoidiO88775.
OMAiSKQMGSY.
OrthoDBiEOG7ZKSC2.
PhylomeDBiO88775.
TreeFamiTF326759.

Miscellaneous databases

NextBioi618619.
PROiO88775.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR027114. Embigin.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PANTHERiPTHR10075:SF4. PTHR10075:SF4. 1 hit.
SMARTiSM00409. IG. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Embigin, a developmentally expressed member of the immunoglobulin super family, is also expressed during regression of prostate and mammary gland."
    Guenette R., Sridhar S., Herley M., Mooibroek M., Wong P., Tenniswood M.
    Dev. Genet. 21:268-278(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Prostate.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Interaction of the erythrocyte lactate transporter (monocarboxylate transporter 1) with an integral 70-kDa membrane glycoprotein of the immunoglobulin superfamily."
    Poole R.C., Halestrap A.P.
    J. Biol. Chem. 272:14624-14628(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 121-135, INTERACTION WITH SLC16A1, GLYCOSYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  4. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 142-151; 165-179 AND 240-252, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  5. "Basigin (CD147) is the target for organomercurial inhibition of monocarboxylate transporter isoforms 1 and 4: the ancillary protein for the insensitive MCT2 is EMBIGIN (gp70)."
    Wilson M.C., Meredith D., Fox J.E., Manoharan C., Davies A.J., Halestrap A.P.
    J. Biol. Chem. 280:27213-27221(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC16A7.
  6. "A novel role for embigin to promote sprouting of motor nerve terminals at the neuromuscular junction."
    Lain E., Carnejac S., Escher P., Wilson M.C., Lomo T., Gajendran N., Brenner H.R.
    J. Biol. Chem. 284:8930-8939(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "Studies on the DIDS-binding site of monocarboxylate transporter 1 suggest a homology model of the open conformation and a plausible translocation cycle."
    Wilson M.C., Meredith D., Bunnun C., Sessions R.B., Halestrap A.P.
    J. Biol. Chem. 284:20011-20021(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC16A1, SUBCELLULAR LOCATION, TOPOLOGY.
  8. "The inhibition of monocarboxylate transporter 2 (MCT2) by AR-C155858 is modulated by the associated ancillary protein."
    Ovens M.J., Manoharan C., Wilson M.C., Murray C.M., Halestrap A.P.
    Biochem. J. 431:217-225(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC16A7, FUNCTION.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEMB_RAT
AccessioniPrimary (citable) accession number: O88775
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 102 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.