EMB_MOUSE
ID EMB_MOUSE Reviewed; 330 AA.
AC P21995; Q3UFF1; Q8C2J8; Q8C543; Q96C38;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Embigin;
DE AltName: Full=Teratocarcinoma glycoprotein Gp-70;
DE Flags: Precursor;
GN Name=Emb; Synonyms=Gp70;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2963822; DOI=10.1016/s0021-9258(18)69032-5;
RA Ozawa M., Huang R.-P., Furukawa T., Muramatsu T.;
RT "A teratocarcinoma glycoprotein carrying a developmentally regulated
RT carbohydrate marker is a member of the immunoglobulin gene superfamily.";
RL J. Biol. Chem. 263:3059-3062(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Hypothalamus, Pancreas, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND 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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-70; ASN-101; ASN-118;
RP ASN-198; ASN-216 AND ASN-221.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-62; ASN-101; ASN-118;
RP ASN-198; ASN-216 AND ASN-221.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in targeting the monocarboxylate transporters
CC SLC16A1 and SLC16A7 to the cell membrane (By similarity). Plays a role
CC in the outgrowth of motoneurons and in the formation of neuromuscular
CC junctions. Following muscle denervation, promotes nerve terminal
CC sprouting and the formation of additional acetylcholine receptor
CC clusters at synaptic sites without affecting terminal Schwann cell
CC number or morphology. Delays the retraction of terminal sprouts
CC following re-innervation of denervated endplates. {ECO:0000250,
CC ECO:0000269|PubMed:19164284}.
CC -!- SUBUNIT: Interacts with SLC16A1 and SLC16A7. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O88775};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:O88775}.
CC Synapse {ECO:0000269|PubMed:19164284}. Note=Localizes to the
CC neuromuscular junctions. {ECO:0000269|PubMed:19164284}.
CC -!- TISSUE SPECIFICITY: Only member of the immunoglobulin superfamily to be
CC expressed in embryonal carcinoma cells, which resemble multipotential
CC cells of early embryos. {ECO:0000269|PubMed:2963822}.
CC -!- DEVELOPMENTAL STAGE: At neuromuscular junctions, 5-fold higher
CC expression levels at P0 compared to adult.
CC {ECO:0000269|PubMed:19164284}.
CC -!- INDUCTION: Regulated by muscle activity. Strongly up-regulated after
CC muscle denervation, including that of gastrocnemius muscle. Maximal
CC expression is observed 10 days after denervation (at protein level).
CC {ECO:0000269|PubMed:19164284}.
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DR EMBL; J03535; AAA37730.1; -; mRNA.
DR EMBL; AK079570; BAC37687.1; -; mRNA.
DR EMBL; AK088480; BAC40381.1; -; mRNA.
DR EMBL; AK138271; BAE23603.1; -; mRNA.
DR EMBL; AK148540; BAE28610.1; -; mRNA.
DR EMBL; AK150625; BAE29715.1; -; mRNA.
DR EMBL; AK166602; BAE38887.1; -; mRNA.
DR EMBL; BC014858; AAH14858.1; -; mRNA.
DR CCDS; CCDS26791.1; -.
DR PIR; A29915; A29915.
DR RefSeq; NP_034460.3; NM_010330.4.
DR AlphaFoldDB; P21995; -.
DR SMR; P21995; -.
DR BioGRID; 199435; 1.
DR STRING; 10090.ENSMUSP00000022242; -.
DR GlyConnect; 2281; 13 N-Linked glycans (4 sites).
DR GlyGen; P21995; 9 sites, 12 N-linked glycans (4 sites).
DR iPTMnet; P21995; -.
DR PhosphoSitePlus; P21995; -.
DR SwissPalm; P21995; -.
DR EPD; P21995; -.
DR jPOST; P21995; -.
DR MaxQB; P21995; -.
DR PaxDb; P21995; -.
DR PeptideAtlas; P21995; -.
DR PRIDE; P21995; -.
DR ProteomicsDB; 275606; -.
DR ABCD; P21995; 2 sequenced antibodies.
DR Antibodypedia; 2626; 188 antibodies from 28 providers.
DR DNASU; 13723; -.
DR Ensembl; ENSMUST00000022242; ENSMUSP00000022242; ENSMUSG00000021728.
DR GeneID; 13723; -.
DR KEGG; mmu:13723; -.
DR UCSC; uc007rym.2; mouse.
DR CTD; 133418; -.
DR MGI; MGI:95321; Emb.
DR VEuPathDB; HostDB:ENSMUSG00000021728; -.
DR eggNOG; ENOG502RXAE; Eukaryota.
DR GeneTree; ENSGT00940000158944; -.
DR HOGENOM; CLU_065379_0_0_1; -.
DR InParanoid; P21995; -.
DR OMA; WTWYRSN; -.
DR OrthoDB; 1101147at2759; -.
DR PhylomeDB; P21995; -.
DR TreeFam; TF326759; -.
DR Reactome; R-MMU-433692; Proton-coupled monocarboxylate transport.
DR BioGRID-ORCS; 13723; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Emb; mouse.
DR PRO; PR:P21995; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P21995; protein.
DR Bgee; ENSMUSG00000021728; Expressed in primitive streak and 271 other tissues.
DR ExpressionAtlas; P21995; baseline and differential.
DR Genevisible; P21995; MM.
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; ISS: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; ISO:MGI.
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; ISS:UniProtKB.
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; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..330
FT /note="Embigin"
FT /id="PRO_0000014750"
FT TOPO_DOM 34..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..161
FT /note="Ig-like V-type 1"
FT DOMAIN 162..256
FT /note="Ig-like V-type 2"
FT REGION 293..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88775"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT DISULFID 89..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 182..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 78
FT /note="I -> S (in Ref. 2; BAC40381)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="N -> S (in Ref. 2; BAC37687)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="L -> S (in Ref. 2; BAC40381)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..166
FT /note="KAHGK -> QSSWE (in Ref. 1; AAA37730)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="D -> G (in Ref. 1; AAA37730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 37064 MW; FC4D729A993A1EDD CRC64;
MRSHTGLRAL VAPGYPLLLL CLLAATRPDP AEGDPTDPTF TSLPVREEMM AKYSNLSLKS
CNISVTEKSN VSVEENVILE KPSHVELKCV YTATKDLNLM NVTWKKDDEP LETTGDFNTT
KMGNTLTSQY RFIVFNSKQL GKYSCVFGEK ELRGTFNIHV PKAHGKKKSL IAYVGDSTVL
KCVCQDCLPL NWTWYMGNET AQVPIDAHSN EKYIINGSHA NETRLKIKHL LEEDGGSYWC
RATFQLGESE EQNELVVLSF LVPLKPFLAI LAEVILLVAI ILLCEVYTHK KKNDPDAGKE
FEQIEQLKSD DSNGIENNVP RYRKTDSADQ
