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   02-SEP-2026, entry version 162.
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,
CC       SLC16A6 and SLC16A7 to the cell membrane (By similarity).
CC       {ECO:0000250|UniProtKB:O88775}.
CC   -!- SUBUNIT: Interacts with SLC16A1, SLC16A6 and SLC16A7.
CC       {ECO:0000250|UniProtKB:O88775}.
CC   -!- INTERACTION:
CC       Q6PCB8; Q9Y276: BCS1L; NbExp=2; IntAct=EBI-21518272, EBI-719257;
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_198449.3. [Q6PCB8-1]
DR   RefSeq; XP_011541448.1; XM_011543146.3. [Q6PCB8-2]
DR   RefSeq; XP_047272658.1; XM_047416702.1. [Q6PCB8-2]
DR   RefSeq; XP_054207551.1; XM_054351576.1. [Q6PCB8-2]
DR   PDB; 7YR5; EM; 3.63 A; B=1-327.
DR   PDB; 9L0B; EM; 3.70 A; B=1-327.
DR   PDB; 9L0C; EM; 3.20 A; B=1-327.
DR   AlphaFoldDB; Q6PCB8; -.
DR   EMDB; EMD-34046; -.
DR   EMDB; EMD-62694; -.
DR   EMDB; EMD-62696; -.
DR   SMR; Q6PCB8; -.
DR   BioGRID; 126358; 41.
DR   FunCoup; Q6PCB8; 743.
DR   IntAct; Q6PCB8; 39.
DR   STRING; 9606.ENSP00000302289; -.
DR   TCDB; 8.A.23.1.2; the basigin (basigin) family.
DR   GlyCosmos; Q6PCB8; 9 sites, No reported glycans.
DR   GlyGen; Q6PCB8; 9 sites, 3 N-linked glycans (3 sites).
DR   iPTMnet; Q6PCB8; -.
DR   PhosphoSitePlus; Q6PCB8; -.
DR   SwissPalm; Q6PCB8; -.
DR   BioMuta; EMB; -.
DR   DMDM; 83286878; -.
DR   jPOST; Q6PCB8; -.
DR   MassIVE; Q6PCB8; -.
DR   PaxDb; 9606-ENSP00000302289; -.
DR   PeptideAtlas; Q6PCB8; -.
DR   ProteomicsDB; 67061; -. [Q6PCB8-1]
DR   ProteomicsDB; 6995; -.
DR   Pumba; Q6PCB8; -.
DR   Antibodypedia; 2626; 193 antibodies from 29 providers.
DR   DNASU; 133418; -.
DR   Ensembl; ENST00000303221.10; ENSP00000302289.5; ENSG00000170571.13. [Q6PCB8-1]
DR   Ensembl; ENST00000514111.1; ENSP00000426404.1; ENSG00000170571.13. [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   AGR; HGNC:30465; -.
DR   ClinPGx; PA134917460; -.
DR   CTD; 133418; -.
DR   DisGeNET; 133418; -.
DR   GeneCards; EMB; -.
DR   HGNC; HGNC:30465; EMB.
DR   HPA; ENSG00000170571; Tissue enhanced (bone).
DR   MIM; 615669; gene.
DR   OpenTargets; ENSG00000170571; -.
DR   VEuPathDB; HostDB:ENSG00000170571; -.
DR   eggNOG; ENOG502RYF2; Eukaryota.
DR   GeneTree; ENSGT00940000158944; -.
DR   HOGENOM; CLU_065379_0_0_1; -.
DR   InParanoid; Q6PCB8; -.
DR   OMA; KGSYWCH; -.
DR   OrthoDB; 9932757at2759; -.
DR   PAN-GO; Q6PCB8; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; Q6PCB8; -.
DR   PathwayCommons; Q6PCB8; -.
DR   Reactome; R-HSA-433692; Proton-coupled monocarboxylate transport.
DR   SignaLink; Q6PCB8; -.
DR   Agora; ENSG00000170571; -.
DR   BioGRID-ORCS; 133418; 12 hits in 1106 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 99 other cell types or tissues.
DR   ExpressionAtlas; Q6PCB8; baseline and differential.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
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-cell adhesion; IBA:GO_Central.
DR   GO; GO:0035879; P:plasma membrane lactate transport; ISS:UniProtKB.
DR   CDD; cd00096; Ig; 1.
DR   FunFam; 2.60.40.10:FF:001012; Embigin; 1.
DR   FunFam; 2.60.40.10:FF:001288; Embigin; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; BASIGIN RELATED; 1.
DR   PANTHER; PTHR10075:SF4; EMBIGIN; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PDBsum; 7YR5; -.
DR   PDBsum; 9L0B; -.
DR   PDBsum; 9L0C; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Repeat; Signal; Synapse;
KW   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   COMPBIAS        291..308
FT                   /note="Basic and acidic residues"
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
//