EMB_RAT
ID EMB_RAT Reviewed; 328 AA.
AC O88775;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Embigin;
DE Flags: Precursor;
GN Name=Emb; Synonyms=Gp70;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX PubMed=9438341;
RX DOI=10.1002/(sici)1520-6408(1997)21:4<268::aid-dvg4>3.0.co;2-5;
RA Guenette R., Sridhar S., Herley M., Mooibroek M., Wong P., Tenniswood M.;
RT "Embigin, a developmentally expressed member of the immunoglobulin super
RT family, is also expressed during regression of prostate and mammary
RT gland.";
RL Dev. Genet. 21:268-278(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 121-135, INTERACTION WITH SLC16A1, GLYCOSYLATION,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9169423; DOI=10.1074/jbc.272.23.14624;
RA Poole R.C., Halestrap A.P.;
RT "Interaction of the erythrocyte lactate transporter (monocarboxylate
RT transporter 1) with an integral 70-kDa membrane glycoprotein of the
RT immunoglobulin superfamily.";
RL J. Biol. Chem. 272:14624-14628(1997).
RN [4]
RP PROTEIN SEQUENCE OF 142-151; 165-179 AND 240-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH SLC16A7.
RX PubMed=15917240; DOI=10.1074/jbc.m411950200;
RA Wilson M.C., Meredith D., Fox J.E., Manoharan C., Davies A.J.,
RA Halestrap A.P.;
RT "Basigin (CD147) is the target for organomercurial inhibition of
RT monocarboxylate transporter isoforms 1 and 4: the ancillary protein for the
RT insensitive MCT2 is EMBIGIN (gp70).";
RL J. Biol. Chem. 280:27213-27221(2005).
RN [6]
RP INDUCTION.
RX PubMed=19164284; DOI=10.1074/jbc.m809491200;
RA Lain E., Carnejac S., Escher P., Wilson M.C., Lomo T., Gajendran N.,
RA Brenner H.R.;
RT "A novel role for embigin to promote sprouting of motor nerve terminals at
RT the neuromuscular junction.";
RL J. Biol. Chem. 284:8930-8939(2009).
RN [7]
RP FUNCTION, INTERACTION WITH SLC16A1, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=19473976; DOI=10.1074/jbc.m109.014217;
RA Wilson M.C., Meredith D., Bunnun C., Sessions R.B., Halestrap A.P.;
RT "Studies on the DIDS-binding site of monocarboxylate transporter 1 suggest
RT a homology model of the open conformation and a plausible translocation
RT cycle.";
RL J. Biol. Chem. 284:20011-20021(2009).
RN [8]
RP INTERACTION WITH SLC16A7, AND FUNCTION.
RX PubMed=20695846; DOI=10.1042/bj20100890;
RA Ovens M.J., Manoharan C., Wilson M.C., Murray C.M., Halestrap A.P.;
RT "The inhibition of monocarboxylate transporter 2 (MCT2) by AR-C155858 is
RT modulated by the associated ancillary protein.";
RL Biochem. J. 431:217-225(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in the outgrowth of motoneurons and in the
CC formation of neuromuscular junctions. Following muscle denervation,
CC promotes nerve terminal sprouting and the formation of additional
CC acetylcholine receptor clusters at synaptic sites without affecting
CC terminal Schwann cell number or morphology. Delays the retraction of
CC terminal sprouts following re-innervation of denervated endplates (By
CC similarity). Plays a role in targeting the monocarboxylate transporters
CC SLC16A1 and SLC16A7 to the cell membrane. {ECO:0000250,
CC ECO:0000269|PubMed:19473976, ECO:0000269|PubMed:20695846}.
CC -!- SUBUNIT: Interacts with SLC16A1 and SLC16A7.
CC {ECO:0000269|PubMed:15917240, ECO:0000269|PubMed:19473976,
CC ECO:0000269|PubMed:20695846, ECO:0000269|PubMed:9169423}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20695846,
CC ECO:0000269|PubMed:9169423}; Single-pass type I membrane protein
CC {ECO:0000305|PubMed:19473976, ECO:0000305|PubMed:9169423}. Synapse
CC {ECO:0000250|UniProtKB:P21995}. Note=Localizes to the neuromuscular
CC junctions. {ECO:0000250|UniProtKB:P21995}.
CC -!- TISSUE SPECIFICITY: Detected in prostate, mammary gland and
CC erythrocytes (at protein level). Detected in testis, brain, prostate,
CC heart, kidney, liver, mammary gland and lung.
CC {ECO:0000269|PubMed:9169423, ECO:0000269|PubMed:9438341}.
CC -!- INDUCTION: Regulated by muscle activity. Strongly up-regulated after
CC muscle denervation, including that of soleus muscle. Expression is
CC significantly increased 3 days after denervation and reaches a maximum,
CC about 130-fold increase, after 5 days. {ECO:0000269|PubMed:19164284}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9169423}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ009698; CAA08796.1; -; mRNA.
DR EMBL; BC061846; AAH61846.1; -; mRNA.
DR RefSeq; NP_446171.1; NM_053719.1.
DR AlphaFoldDB; O88775; -.
DR STRING; 10116.ENSRNOP00000015306; -.
DR GlyGen; O88775; 9 sites.
DR iPTMnet; O88775; -.
DR PhosphoSitePlus; O88775; -.
DR jPOST; O88775; -.
DR PaxDb; O88775; -.
DR PRIDE; O88775; -.
DR Ensembl; ENSRNOT00000085576; ENSRNOP00000069959; ENSRNOG00000060329.
DR GeneID; 114511; -.
DR KEGG; rno:114511; -.
DR CTD; 133418; -.
DR RGD; 621067; Emb.
DR eggNOG; ENOG502RXAE; Eukaryota.
DR GeneTree; ENSGT00940000158944; -.
DR InParanoid; O88775; -.
DR OrthoDB; 1101147at2759; -.
DR PhylomeDB; O88775; -.
DR TreeFam; TF326759; -.
DR Reactome; R-RNO-433692; Proton-coupled monocarboxylate transport.
DR PRO; PR:O88775; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IDA:RGD.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0035879; P:plasma membrane lactate transport; IDA:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR027114; Embigin.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF4; PTHR10075:SF4; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..328
FT /note="Embigin"
FT /id="PRO_0000014751"
FT TOPO_DOM 34..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 67..160
FT /note="Ig-like 1"
FT DOMAIN 159..254
FT /note="Ig-like 2"
FT REGION 289..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 180..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ 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
