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Embigin

 EMB_RAT                 Reviewed;         328 AA.
O88775;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 110.
RecName: Full=Embigin;
Flags: Precursor;
Name=Emb; Synonyms=Gp70;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Prostate;
PubMed=9438341;
DOI=10.1002/(SICI)1520-6408(1997)21:4<268::AID-DVG4>3.0.CO;2-5;
Guenette R., Sridhar S., Herley M., Mooibroek M., Wong P.,
Tenniswood M.;
"Embigin, a developmentally expressed member of the immunoglobulin
super family, is also expressed during regression of prostate and
mammary gland.";
Dev. Genet. 21:268-278(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 121-135, INTERACTION WITH SLC16A1, GLYCOSYLATION,
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=9169423; DOI=10.1074/jbc.272.23.14624;
Poole R.C., Halestrap A.P.;
"Interaction of the erythrocyte lactate transporter (monocarboxylate
transporter 1) with an integral 70-kDa membrane glycoprotein of the
immunoglobulin superfamily.";
J. Biol. Chem. 272:14624-14628(1997).
[4]
PROTEIN SEQUENCE OF 142-151; 165-179 AND 240-252, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[5]
INTERACTION WITH SLC16A7.
PubMed=15917240; DOI=10.1074/jbc.M411950200;
Wilson M.C., Meredith D., Fox J.E., Manoharan C., Davies A.J.,
Halestrap A.P.;
"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).";
J. Biol. Chem. 280:27213-27221(2005).
[6]
INDUCTION.
PubMed=19164284; DOI=10.1074/jbc.M809491200;
Lain E., Carnejac S., Escher P., Wilson M.C., Lomo T., Gajendran N.,
Brenner H.R.;
"A novel role for embigin to promote sprouting of motor nerve
terminals at the neuromuscular junction.";
J. Biol. Chem. 284:8930-8939(2009).
[7]
FUNCTION, INTERACTION WITH SLC16A1, SUBCELLULAR LOCATION, AND
TOPOLOGY.
PubMed=19473976; DOI=10.1074/jbc.M109.014217;
Wilson M.C., Meredith D., Bunnun C., Sessions R.B., Halestrap A.P.;
"Studies on the DIDS-binding site of monocarboxylate transporter 1
suggest a homology model of the open conformation and a plausible
translocation cycle.";
J. Biol. Chem. 284:20011-20021(2009).
[8]
INTERACTION WITH SLC16A7, AND FUNCTION.
PubMed=20695846; DOI=10.1042/BJ20100890;
Ovens M.J., Manoharan C., Wilson M.C., Murray C.M., Halestrap A.P.;
"The inhibition of monocarboxylate transporter 2 (MCT2) by AR-C155858
is modulated by the associated ancillary protein.";
Biochem. J. 431:217-225(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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. {ECO:0000250, ECO:0000269|PubMed:19473976,
ECO:0000269|PubMed:20695846}.
-!- SUBUNIT: Interacts with SLC16A1 and SLC16A7.
{ECO:0000269|PubMed:15917240, ECO:0000269|PubMed:19473976,
ECO:0000269|PubMed:20695846, ECO:0000269|PubMed:9169423}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20695846,
ECO:0000269|PubMed:9169423}; Single-pass type I membrane protein
{ECO:0000305|PubMed:19473976, ECO:0000305|PubMed:9169423}. Cell
junction, synapse {ECO:0000250|UniProtKB:P21995}. Note=Localizes
to the neuromuscular junctions. {ECO:0000250|UniProtKB:P21995}.
-!- TISSUE SPECIFICITY: Detected in prostate, mammary gland and
erythrocytes (at protein level). Detected in testis, brain,
prostate, heart, kidney, liver, mammary gland and lung.
{ECO:0000269|PubMed:9169423, ECO:0000269|PubMed:9438341}.
-!- INDUCTION: 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.
{ECO:0000269|PubMed:19164284}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:9169423}.
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EMBL; AJ009698; CAA08796.1; -; mRNA.
EMBL; BC061846; AAH61846.1; -; mRNA.
RefSeq; NP_446171.1; NM_053719.1.
UniGene; Rn.16221; -.
ProteinModelPortal; O88775; -.
SMR; O88775; -.
STRING; 10116.ENSRNOP00000015306; -.
iPTMnet; O88775; -.
PhosphoSitePlus; O88775; -.
PaxDb; O88775; -.
PRIDE; O88775; -.
GeneID; 114511; -.
KEGG; rno:114511; -.
CTD; 133418; -.
RGD; 621067; Emb.
eggNOG; ENOG410IVBC; Eukaryota.
eggNOG; ENOG41120A3; LUCA.
HOGENOM; HOG000082417; -.
HOVERGEN; HBG051471; -.
InParanoid; O88775; -.
PhylomeDB; O88775; -.
TreeFam; TF326759; -.
PRO; PR:O88775; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0007155; P:cell adhesion; IDA:RGD.
GO; GO:0035879; P:plasma membrane lactate transport; IDA:RGD.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027114; Embigin.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
PANTHER; PTHR10075:SF4; PTHR10075:SF4; 1.
SMART; SM00409; IG; 2.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 328 Embigin.
/FTId=PRO_0000014751.
TOPO_DOM 34 264 Extracellular. {ECO:0000255}.
TRANSMEM 265 285 Helical. {ECO:0000255}.
TOPO_DOM 286 328 Cytoplasmic. {ECO:0000255}.
DOMAIN 67 160 Ig-like 1.
DOMAIN 159 254 Ig-like 2.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 189 189 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 88 144 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 180 238 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 328 AA; 37005 MW; C749A847ACE374B1 CRC64;
MRSHTGLRAL VAPGCSLLLL YLLAATRPDR AVGDPADSAF TSLPVREEMM AKYANLSLET
YNISLTEQTR VSEQNITLER PSHLELECTF TATEDVMSMN VTWKKDDALL ETTDGFNTTK
MGDTLYSQYR FTVFNSKQMG KYSCFLGEEL RGTFNIRVPK VHGKNKPLIT YVGDSTVLKC
ECQNCLPLNW TWYMSNGTAQ VPIDVHVNDK FDINGSYANE TKLKVKHLLE EDGGSYWCRA
AFPLGESEEH IKLVVLSFMV PLKPFLAIIA EVILLVAIIL LCEVYTQKKK NDPDDGKEFE
QIEQLKSDDS NGIENNVPRY RKTDSGDQ


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