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Protein

Embigin

Gene

Emb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in targeting the monocarboxylate transporters SLC16A1 and SLC16A7 to the cell membrane (By similarity). 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 similarity1 Publication

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-433692. Proton-coupled monocarboxylate transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Embigin
Alternative name(s):
Teratocarcinoma glycoprotein Gp-70
Gene namesi
Name:Emb
Synonyms:Gp70
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:95321. Emb.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 254221ExtracellularSequence analysisAdd
BLAST
Transmembranei255 – 28329HelicalSequence analysisAdd
BLAST
Topological domaini284 – 33047CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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 – 330297EmbiginPRO_0000014750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)2 Publications
Glycosylationi62 – 621N-linked (GlcNAc...)1 Publication
Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
Glycosylationi76 – 761N-linked (GlcNAc...); atypical2 Publications
Disulfide bondi89 ↔ 145PROSITE-ProRule annotation
Glycosylationi98 – 981N-linked (GlcNAc...); atypical1 Publication
Glycosylationi101 – 1011N-linked (GlcNAc...)2 Publications
Glycosylationi118 – 1181N-linked (GlcNAc...)2 Publications
Disulfide bondi182 ↔ 240PROSITE-ProRule annotation
Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)2 Publications
Glycosylationi210 – 2101N-linked (GlcNAc...); atypical1 Publication
Glycosylationi216 – 2161N-linked (GlcNAc...)2 Publications
Glycosylationi221 – 2211N-linked (GlcNAc...)2 Publications
Modified residuei312 – 3121PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP21995.
MaxQBiP21995.
PaxDbiP21995.
PeptideAtlasiP21995.
PRIDEiP21995.

PTM databases

iPTMnetiP21995.
PhosphoSiteiP21995.
SwissPalmiP21995.

Expressioni

Tissue specificityi

Only member of the immunoglobulin superfamily to be expressed in embryonal carcinoma cells, which resemble multipotential cells of early embryos.1 Publication

Developmental stagei

At neuromuscular junctions, 5-fold higher expression levels at P0 compared to adult.1 Publication

Inductioni

Regulated by muscle activity. Strongly up-regulated after muscle denervation, including that of gastrocnemius muscle. Maximal expression is observed 10 days after denervation (at protein level).1 Publication

Gene expression databases

BgeeiP21995.
CleanExiMM_EMB.
GenevisibleiP21995. MM.

Interactioni

Subunit structurei

Interacts with SLC16A1 and SLC16A7.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022242.

Structurei

3D structure databases

ProteinModelPortaliP21995.
SMRiP21995. Positions 90-250.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 161124Ig-like V-type 1Add
BLAST
Domaini162 – 25695Ig-like V-type 2Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IVBC. Eukaryota.
ENOG41120A3. LUCA.
GeneTreeiENSGT00390000010516.
HOGENOMiHOG000082417.
HOVERGENiHBG051471.
InParanoidiP21995.
OMAiSKQMGSY.
OrthoDBiEOG7ZKSC2.
PhylomeDBiP21995.
TreeFamiTF326759.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR027114. Embigin.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
[Graphical view]
PANTHERiPTHR10075:SF4. PTHR10075:SF4. 1 hit.
PfamiPF07679. I-set. 1 hit.
[Graphical view]
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.

P21995-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSHTGLRAL VAPGYPLLLL CLLAATRPDP AEGDPTDPTF TSLPVREEMM
60 70 80 90 100
AKYSNLSLKS CNISVTEKSN VSVEENVILE KPSHVELKCV YTATKDLNLM
110 120 130 140 150
NVTWKKDDEP LETTGDFNTT KMGNTLTSQY RFIVFNSKQL GKYSCVFGEK
160 170 180 190 200
ELRGTFNIHV PKAHGKKKSL IAYVGDSTVL KCVCQDCLPL NWTWYMGNET
210 220 230 240 250
AQVPIDAHSN EKYIINGSHA NETRLKIKHL LEEDGGSYWC RATFQLGESE
260 270 280 290 300
EQNELVVLSF LVPLKPFLAI LAEVILLVAI ILLCEVYTHK KKNDPDAGKE
310 320 330
FEQIEQLKSD DSNGIENNVP RYRKTDSADQ
Length:330
Mass (Da):37,064
Last modified:February 1, 2005 - v2
Checksum:iFC4D729A993A1EDD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781I → S in BAC40381 (PubMed:16141072).Curated
Sequence conflicti98 – 981N → S in BAC37687 (PubMed:16141072).Curated
Sequence conflicti99 – 991L → S in BAC40381 (PubMed:16141072).Curated
Sequence conflicti162 – 1665KAHGK → QSSWE in AAA37730 (PubMed:2963822).Curated
Sequence conflicti294 – 2941D → G in AAA37730 (PubMed:2963822).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03535 mRNA. Translation: AAA37730.1.
AK079570 mRNA. Translation: BAC37687.1.
AK088480 mRNA. Translation: BAC40381.1.
AK138271 mRNA. Translation: BAE23603.1.
AK148540 mRNA. Translation: BAE28610.1.
AK150625 mRNA. Translation: BAE29715.1.
AK166602 mRNA. Translation: BAE38887.1.
BC014858 mRNA. Translation: AAH14858.1.
CCDSiCCDS26791.1.
PIRiA29915.
RefSeqiNP_034460.3. NM_010330.4.
UniGeneiMm.274926.

Genome annotation databases

EnsembliENSMUST00000022242; ENSMUSP00000022242; ENSMUSG00000021728.
GeneIDi13723.
KEGGimmu:13723.
UCSCiuc007rym.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03535 mRNA. Translation: AAA37730.1.
AK079570 mRNA. Translation: BAC37687.1.
AK088480 mRNA. Translation: BAC40381.1.
AK138271 mRNA. Translation: BAE23603.1.
AK148540 mRNA. Translation: BAE28610.1.
AK150625 mRNA. Translation: BAE29715.1.
AK166602 mRNA. Translation: BAE38887.1.
BC014858 mRNA. Translation: AAH14858.1.
CCDSiCCDS26791.1.
PIRiA29915.
RefSeqiNP_034460.3. NM_010330.4.
UniGeneiMm.274926.

3D structure databases

ProteinModelPortaliP21995.
SMRiP21995. Positions 90-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022242.

PTM databases

iPTMnetiP21995.
PhosphoSiteiP21995.
SwissPalmiP21995.

Proteomic databases

EPDiP21995.
MaxQBiP21995.
PaxDbiP21995.
PeptideAtlasiP21995.
PRIDEiP21995.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022242; ENSMUSP00000022242; ENSMUSG00000021728.
GeneIDi13723.
KEGGimmu:13723.
UCSCiuc007rym.2. mouse.

Organism-specific databases

CTDi133418.
MGIiMGI:95321. Emb.

Phylogenomic databases

eggNOGiENOG410IVBC. Eukaryota.
ENOG41120A3. LUCA.
GeneTreeiENSGT00390000010516.
HOGENOMiHOG000082417.
HOVERGENiHBG051471.
InParanoidiP21995.
OMAiSKQMGSY.
OrthoDBiEOG7ZKSC2.
PhylomeDBiP21995.
TreeFamiTF326759.

Enzyme and pathway databases

ReactomeiR-MMU-433692. Proton-coupled monocarboxylate transport.

Miscellaneous databases

PROiP21995.
SOURCEiSearch...

Gene expression databases

BgeeiP21995.
CleanExiMM_EMB.
GenevisibleiP21995. MM.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR027114. Embigin.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
[Graphical view]
PANTHERiPTHR10075:SF4. PTHR10075:SF4. 1 hit.
PfamiPF07679. I-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A teratocarcinoma glycoprotein carrying a developmentally regulated carbohydrate marker is a member of the immunoglobulin gene superfamily."
    Ozawa M., Huang R.-P., Furukawa T., Muramatsu T.
    J. Biol. Chem. 263:3059-3062(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Hypothalamus, Pancreas and Thymus.
  3. "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: Eye.
  4. "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: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION.
  5. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-70; ASN-76; ASN-101; ASN-118; ASN-198; ASN-210; ASN-216 AND ASN-221.
    Tissue: Myoblast.
  6. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-62; ASN-76; ASN-98; ASN-101; ASN-118; ASN-198; ASN-216 AND ASN-221.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung and Testis.

Entry informationi

Entry nameiEMB_MOUSE
AccessioniPrimary (citable) accession number: P21995
Secondary accession number(s): Q3UFF1
, Q8C2J8, Q8C543, Q96C38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 2005
Last modified: July 6, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.