EMB_HUMAN
ID EMB_HUMAN Reviewed; 327 AA.
AC Q6PCB8; B7Z6S3; B7Z902;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Embigin;
DE Flags: Precursor;
GN Name=EMB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Small intestine, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-213 AND ASN-218.
RC TISSUE=Leukemic T-cell;
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).
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. May
CC play a role in targeting the monocarboxylate transporters SLC16A1 and
CC SLC16A7 to the cell membrane (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:P21995}. Note=Localizes to the
CC neuromuscular junctions. {ECO:0000250|UniProtKB:P21995}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PCB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PCB8-2; Sequence=VSP_055593;
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DR EMBL; AK300860; BAH13359.1; -; mRNA.
DR EMBL; AK304226; BAH14138.1; -; mRNA.
DR EMBL; AC035145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471123; EAW54853.1; -; Genomic_DNA.
DR EMBL; CH471123; EAW54854.1; -; Genomic_DNA.
DR EMBL; BC059398; AAH59398.1; -; mRNA.
DR CCDS; CCDS3953.1; -. [Q6PCB8-1]
DR RefSeq; NP_940851.1; NM_198449.2. [Q6PCB8-1]
DR RefSeq; XP_011541448.1; XM_011543146.2. [Q6PCB8-2]
DR AlphaFoldDB; Q6PCB8; -.
DR SMR; Q6PCB8; -.
DR BioGRID; 126358; 35.
DR IntAct; Q6PCB8; 12.
DR STRING; 9606.ENSP00000302289; -.
DR TCDB; 8.A.23.1.2; the basigin (basigin) family.
DR GlyGen; Q6PCB8; 9 sites.
DR iPTMnet; Q6PCB8; -.
DR PhosphoSitePlus; Q6PCB8; -.
DR SwissPalm; Q6PCB8; -.
DR BioMuta; EMB; -.
DR DMDM; 83286878; -.
DR EPD; Q6PCB8; -.
DR jPOST; Q6PCB8; -.
DR MassIVE; Q6PCB8; -.
DR MaxQB; Q6PCB8; -.
DR PaxDb; Q6PCB8; -.
DR PeptideAtlas; Q6PCB8; -.
DR PRIDE; Q6PCB8; -.
DR ProteomicsDB; 67061; -. [Q6PCB8-1]
DR ProteomicsDB; 6995; -.
DR Antibodypedia; 2626; 188 antibodies from 28 providers.
DR DNASU; 133418; -.
DR Ensembl; ENST00000303221.10; ENSP00000302289.5; ENSG00000170571.12. [Q6PCB8-1]
DR Ensembl; ENST00000514111.1; ENSP00000426404.1; ENSG00000170571.12. [Q6PCB8-2]
DR GeneID; 133418; -.
DR KEGG; hsa:133418; -.
DR MANE-Select; ENST00000303221.10; ENSP00000302289.5; NM_198449.3; NP_940851.1.
DR UCSC; uc003jom.4; human. [Q6PCB8-1]
DR CTD; 133418; -.
DR DisGeNET; 133418; -.
DR GeneCards; EMB; -.
DR HGNC; HGNC:30465; EMB.
DR HPA; ENSG00000170571; Tissue enhanced (bone marrow, intestine).
DR MIM; 615669; gene.
DR neXtProt; NX_Q6PCB8; -.
DR OpenTargets; ENSG00000170571; -.
DR PharmGKB; PA134917460; -.
DR VEuPathDB; HostDB:ENSG00000170571; -.
DR eggNOG; ENOG502RYF2; Eukaryota.
DR GeneTree; ENSGT00940000158944; -.
DR HOGENOM; CLU_065379_0_0_1; -.
DR InParanoid; Q6PCB8; -.
DR OMA; WTWYRSN; -.
DR OrthoDB; 1101147at2759; -.
DR PhylomeDB; Q6PCB8; -.
DR TreeFam; TF326759; -.
DR PathwayCommons; Q6PCB8; -.
DR Reactome; R-HSA-433692; Proton-coupled monocarboxylate transport.
DR SignaLink; Q6PCB8; -.
DR BioGRID-ORCS; 133418; 11 hits in 1026 CRISPR screens.
DR ChiTaRS; EMB; human.
DR GenomeRNAi; 133418; -.
DR Pharos; Q6PCB8; Tbio.
DR PRO; PR:Q6PCB8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q6PCB8; protein.
DR Bgee; ENSG00000170571; Expressed in bone marrow cell and 97 other tissues.
DR ExpressionAtlas; Q6PCB8; baseline and differential.
DR Genevisible; Q6PCB8; HS.
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: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 InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF4; PTHR10075:SF4; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..327
FT /note="Embigin"
FT /id="PRO_0000014749"
FT TOPO_DOM 33..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 71..158
FT /note="Ig-like V-type 1"
FT DOMAIN 159..253
FT /note="Ig-like V-type 2"
FT REGION 287..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88775"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
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 85
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 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 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 88..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 180..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055593"
SQ SEQUENCE 327 AA; 36881 MW; E6B933DAF6A3B0D4 CRC64;
MRALPGLLEA RARTPRLLLL QCLLAAARPS SADGSAPDSP FTSPPLREEI MANNFSLESH
NISLTEHSSM PVEKNITLER PSNVNLTCQF TTSGDLNAVN VTWKKDGEQL ENNYLVSATG
STLYTQYRFT IINSKQMGSY SCFFREEKEQ RGTFNFKVPE LHGKNKPLIS YVGDSTVLTC
KCQNCFPLNW TWYSSNGSVK VPVGVQMNKY VINGTYANET KLKITQLLEE DGESYWCRAL
FQLGESEEHI ELVVLSYLVP LKPFLVIVAE VILLVATILL CEKYTQKKKK HSDEGKEFEQ
IEQLKSDDSN GIENNVPRHR KNESLGQ
