EMP2_HUMAN
ID EMP2_HUMAN Reviewed; 167 AA.
AC P54851; B2R7V6; D3DUF8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Epithelial membrane protein 2;
DE Short=EMP-2;
DE AltName: Full=Protein XMP;
GN Name=EMP2; Synonyms=XMP;
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 [MRNA].
RC TISSUE=Spleen;
RX PubMed=8917086; DOI=10.1016/0378-1119(96)00134-5;
RA Taylor V., Suter U.;
RT "Epithelial membrane protein-2 and epithelial membrane protein-3: two novel
RT members of the peripheral myelin protein 22 gene family.";
RL Gene 175:115-120(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8996089; DOI=10.1016/s0378-1119(96)00475-1;
RA Ben-Porath I., Benvenisty N.;
RT "Characterization of a tumor-associated gene, a member of a novel family of
RT genes encoding membrane glycoproteins.";
RL Gene 183:69-75(1996).
RN [3]
RP SEQUENCE REVISION.
RA Ben-Porath I., Benvenisty N.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kim Y.-S., Ueda E., Borok Z., Kim S.-Y., Jetten A.M.;
RT "Genomic structure of the human epithelial membrane protein 2 (EMP2) gene;
RT regulation by two alternative promoters.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [8]
RP FUNCTION, INTERACTION WITH P2RX7, AND SUBCELLULAR LOCATION.
RX PubMed=12107182; DOI=10.1074/jbc.m205120200;
RA Wilson H.L., Wilson S.A., Surprenant A., North R.A.;
RT "Epithelial membrane proteins induce membrane blebbing and interact with
RT the P2X7 receptor C terminus.";
RL J. Biol. Chem. 277:34017-34023(2002).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=12710941; DOI=10.1016/s0014-4800(03)00009-1;
RA Wadehra M., Sulur G.G., Braun J., Gordon L.K., Goodglick L.;
RT "Epithelial membrane protein-2 is expressed in discrete anatomical regions
RT of the eye.";
RL Exp. Mol. Pathol. 74:106-112(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH ITGB3.
RX PubMed=16216233; DOI=10.1016/j.ydbio.2005.09.003;
RA Wadehra M., Forbes A., Pushkarna N., Goodglick L., Gordon L.K.,
RA Williams C.J., Braun J.;
RT "Epithelial membrane protein-2 regulates surface expression of alphavbeta3
RT integrin in the endometrium.";
RL Dev. Biol. 287:336-345(2005).
RN [11]
RP FUNCTION.
RX PubMed=16487956; DOI=10.1016/j.ydbio.2006.01.015;
RA Wadehra M., Dayal M., Mainigi M., Ord T., Iyer R., Braun J., Williams C.J.;
RT "Knockdown of the tetraspan protein epithelial membrane protein-2 inhibits
RT implantation in the mouse.";
RL Dev. Biol. 292:430-441(2006).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18400107; DOI=10.1186/1477-7827-6-15;
RA Wadehra M., Mainigi M., Morales S.A., Rao R.G., Gordon L.K., Williams C.J.,
RA Braun J.;
RT "Steroid hormone regulation of EMP2 expression and localization in the
RT endometrium.";
RL Reprod. Biol. Endocrinol. 6:15-15(2008).
RN [13]
RP INTERACTION WITH PTK2, AND FUNCTION.
RX PubMed=19494199; DOI=10.1167/iovs.08-3315;
RA Morales S.A., Mareninov S., Coulam P., Wadehra M., Goodglick L., Braun J.,
RA Gordon L.K.;
RT "Functional consequences of interactions between FAK and epithelial
RT membrane protein 2 (EMP2).";
RL Invest. Ophthalmol. Vis. Sci. 50:4949-4956(2009).
RN [14]
RP FUNCTION, INTERACTION WITH PTK2, AND SUBCELLULAR LOCATION.
RX PubMed=21637765; DOI=10.1371/journal.pone.0019945;
RA Fu M., Rao R., Sudhakar D., Hogue C.P., Rutta Z., Morales S., Gordon L.K.,
RA Braun J., Goodglick L., Wadehra M.;
RT "Epithelial membrane protein-2 promotes endometrial tumor formation through
RT activation of FAK and Src.";
RL PLoS ONE 6:E19945-E19945(2011).
RN [15]
RP FUNCTION.
RX PubMed=22728127; DOI=10.1016/j.exer.2012.06.002;
RA Morales S.A., Telander D.G., Mareninov S., Nagy A., Wadehra M., Braun J.,
RA Gordon L.K.;
RT "Anti-EMP2 diabody blocks epithelial membrane protein 2 (EMP2) and FAK
RT mediated collagen gel contraction in ARPE-19 cells.";
RL Exp. Eye Res. 102:10-16(2012).
RN [16]
RP FUNCTION.
RX PubMed=23439602; DOI=10.1167/iovs.12-11013;
RA Morales S.A., Telander D.G., Leon D., Forward K., Braun J., Wadehra M.,
RA Gordon L.K.;
RT "Epithelial membrane protein 2 controls VEGF expression in ARPE-19 cells.";
RL Invest. Ophthalmol. Vis. Sci. 54:2367-2372(2013).
RN [17]
RP FUNCTION.
RX PubMed=23334331; DOI=10.1038/onc.2012.622;
RA Gordon L.K., Kiyohara M., Fu M., Braun J., Dhawan P., Chan A.,
RA Goodglick L., Wadehra M.;
RT "EMP2 regulates angiogenesis in endometrial cancer cells through induction
RT of VEGF.";
RL Oncogene 32:5369-5376(2013).
RN [18]
RP FUNCTION, INVOLVEMENT IN NPHS10, VARIANTS NPHS10 LEU-7 AND THR-10, AND
RP CHARACTERIZATION OF VARIANTS NPHS10 LEU-7 AND THR-10.
RX PubMed=24814193; DOI=10.1016/j.ajhg.2014.04.010;
RA Gee H.Y., Ashraf S., Wan X., Vega-Warner V., Esteve-Rudd J., Lovric S.,
RA Fang H., Hurd T.W., Sadowski C.E., Allen S.J., Otto E.A., Korkmaz E.,
RA Washburn J., Levy S., Williams D.S., Bakkaloglu S.A., Zolotnitskaya A.,
RA Ozaltin F., Zhou W., Hildebrandt F.;
RT "Mutations in EMP2 cause childhood-onset nephrotic syndrome.";
RL Am. J. Hum. Genet. 94:884-890(2014).
RN [19]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28295343; DOI=10.1002/path.4893;
RA Williams C.J., Chu A., Jefferson W.N., Casero D., Sudhakar D., Khurana N.,
RA Hogue C.P., Aryasomayajula C., Patel P., Sullivan P., Padilla-Banks E.,
RA Mohandessi S., Janzen C., Wadehra M.;
RT "Epithelial membrane protein 2 (EMP2) deficiency alters placental
RT angiogenesis, mimicking features of human placental insufficiency.";
RL J. Pathol. 242:246-259(2017).
CC -!- FUNCTION: Functions as a key regulator of cell membrane composition by
CC regulating protein surface expression. Also, plays a role in regulation
CC of processes including cell migration, cell proliferation, cell
CC contraction and cell adhesion. Regulates transepithelial migration of
CC neutrophils into the alveolar lumen, potentially via mediation of cell
CC surface expression of adhesion markers and lipid raft formation (By
CC similarity). Negatively regulates caveolae formation by reducing CAV1
CC expression and CAV1 amount by increasing lysosomal degradation
CC (PubMed:24814193). Facilitates surface trafficking and formation of
CC lipid rafts bearing GPI-anchor proteins (By similarity). Regulates
CC surface expression of MHC1 and ICAM1 proteins increasing susceptibility
CC to T-cell mediated cytotoxicity (By similarity). Regulates the plasma
CC membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5-
CC ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion
CC (PubMed:16216233). Also regulates many processes through PTK2.
CC Regulates blood vessel endothelial cell migration and angiogenesis by
CC regulating VEGF protein expression through PTK2 activation
CC (PubMed:23439602). Regulates cell migration and cell contraction
CC through PTK2 and SRC activation (PubMed:21637765, PubMed:22728127).
CC Regulates focal adhesion density, F-actin conformation and cell
CC adhesion capacity through interaction with PTK2 (PubMed:19494199).
CC Positively regulates cell proliferation (PubMed:24814193). Plays a role
CC during cell death and cell blebbing (PubMed:12107182). Promotes
CC angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-
CC dependent pathway (PubMed:23334331). Also plays a role in embryo
CC implantation by regulating surface trafficking of integrin heterodimer
CC ITGA5-ITGB3 (PubMed:16487956). Plays a role in placental angiogenesis
CC and uterine natural killer cell regulation at the maternal-fetal
CC placental interface, however not required in the maternal tissues for a
CC viable pregnancy (By similarity). Involved in the early stages of
CC embryogenic development and cardiogenesis, potentially via regulation
CC of epithelial-mesenchymal transition timing (By similarity). May play a
CC role in glomerular filtration (By similarity).
CC {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662,
CC ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:16216233,
CC ECO:0000269|PubMed:16487956, ECO:0000269|PubMed:19494199,
CC ECO:0000269|PubMed:21637765, ECO:0000269|PubMed:22728127,
CC ECO:0000269|PubMed:23334331, ECO:0000269|PubMed:23439602,
CC ECO:0000269|PubMed:24814193}.
CC -!- SUBUNIT: Interacts with PTK2; regulates PTK2 activation and
CC localization (PubMed:19494199, PubMed:21637765). Interacts with ITGB3;
CC regulates the levels of the heterodimer ITGA5-ITGB3 integrin surface
CC expression (PubMed:16216233). Interacts with P2RX7 (via C-terminus)
CC (PubMed:12107182). Interacts with ITGB1; the interaction may be direct
CC or indirect and ITGB1 has a heterodimer form.
CC {ECO:0000250|UniProtKB:O88662, ECO:0000269|PubMed:12107182,
CC ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:19494199,
CC ECO:0000269|PubMed:21637765}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18400107}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12107182,
CC ECO:0000269|PubMed:18400107, ECO:0000269|PubMed:21637765,
CC ECO:0000269|PubMed:28295343}. Apical cell membrane
CC {ECO:0000250|UniProtKB:O88662}. Membrane raft
CC {ECO:0000269|PubMed:21637765}. Cytoplasm {ECO:0000269|PubMed:21637765}.
CC Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O88662}. Note=Localizes in cytoplasm, foot
CC processes and cell bodies of podocytes and nucleus of endothelial cells
CC of kidney. Localizes to the apical cell surface in the luminal
CC epithelium and glandular epithelium. Colocalized with ITGB1 and GPI-
CC anchor proteins on plasma membrane. {ECO:0000250|UniProtKB:O88662,
CC ECO:0000250|UniProtKB:Q66HH2}.
CC -!- TISSUE SPECIFICITY: Expressed in ciliary body epithelia, sclera,
CC cornea, and retinal pigment epithelium (at protein level)
CC (PubMed:12710941). Expressed in lung and endometrial tissue; expression
CC is particularly abundant in secretory endometrium (at protein level)
CC (PubMed:12710941). Expressed in placental villous syncytiotrophoblasts
CC and cytotrophoblasts and on the membrane of interstitial trophoblasts
CC (at protein level) (PubMed:28295343). {ECO:0000269|PubMed:12710941,
CC ECO:0000269|PubMed:28295343}.
CC -!- DISEASE: Nephrotic syndrome 10 (NPHS10) [MIM:615861]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by focal
CC segmental glomerulosclerosis, progressive renal failure, severe
CC proteinuria, hypoalbuminemia, hyperlipidemia and edema. NPHS10 is a
CC steroid-sensitive form characterized by onset in childhood and
CC remission without end-stage kidney disease.
CC {ECO:0000269|PubMed:24814193}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. {ECO:0000305}.
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DR EMBL; U52100; AAC51779.1; -; mRNA.
DR EMBL; X94770; CAA64393.1; -; mRNA.
DR EMBL; AY057060; AAL27085.1; -; Genomic_DNA.
DR EMBL; AK313134; BAG35953.1; -; mRNA.
DR EMBL; CH471112; EAW85180.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85181.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85182.1; -; Genomic_DNA.
DR EMBL; BC009687; AAH09687.1; -; mRNA.
DR CCDS; CCDS10541.1; -.
DR PIR; JC5044; JC5044.
DR PIR; JC5732; JC5732.
DR RefSeq; NP_001415.1; NM_001424.5.
DR RefSeq; XP_006720927.1; XM_006720864.3.
DR AlphaFoldDB; P54851; -.
DR SMR; P54851; -.
DR BioGRID; 108328; 2.
DR IntAct; P54851; 2.
DR STRING; 9606.ENSP00000352540; -.
DR GlyGen; P54851; 3 sites.
DR iPTMnet; P54851; -.
DR PhosphoSitePlus; P54851; -.
DR BioMuta; EMP2; -.
DR DMDM; 1706643; -.
DR MassIVE; P54851; -.
DR PaxDb; P54851; -.
DR PeptideAtlas; P54851; -.
DR PRIDE; P54851; -.
DR ProteomicsDB; 56740; -.
DR Antibodypedia; 11432; 131 antibodies from 23 providers.
DR DNASU; 2013; -.
DR Ensembl; ENST00000359543.8; ENSP00000352540.3; ENSG00000213853.10.
DR Ensembl; ENST00000536829.1; ENSP00000445712.1; ENSG00000213853.10.
DR GeneID; 2013; -.
DR KEGG; hsa:2013; -.
DR MANE-Select; ENST00000359543.8; ENSP00000352540.3; NM_001424.6; NP_001415.1.
DR UCSC; uc002czx.4; human.
DR CTD; 2013; -.
DR DisGeNET; 2013; -.
DR GeneCards; EMP2; -.
DR HGNC; HGNC:3334; EMP2.
DR HPA; ENSG00000213853; Tissue enhanced (lung).
DR MalaCards; EMP2; -.
DR MIM; 602334; gene.
DR MIM; 615861; phenotype.
DR neXtProt; NX_P54851; -.
DR OpenTargets; ENSG00000213853; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA27771; -.
DR VEuPathDB; HostDB:ENSG00000213853; -.
DR eggNOG; ENOG502RYYE; Eukaryota.
DR GeneTree; ENSGT00950000182696; -.
DR HOGENOM; CLU_138632_0_0_1; -.
DR InParanoid; P54851; -.
DR OMA; ADIWRVC; -.
DR OrthoDB; 1345659at2759; -.
DR PhylomeDB; P54851; -.
DR TreeFam; TF330414; -.
DR PathwayCommons; P54851; -.
DR SignaLink; P54851; -.
DR BioGRID-ORCS; 2013; 12 hits in 1022 CRISPR screens.
DR ChiTaRS; EMP2; human.
DR GeneWiki; EMP2; -.
DR GenomeRNAi; 2013; -.
DR Pharos; P54851; Tbio.
DR PRO; PR:P54851; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P54851; protein.
DR Bgee; ENSG00000213853; Expressed in upper leg skin and 185 other tissues.
DR Genevisible; P54851; HS.
DR GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IPI:MGI.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
DR GO; GO:0070252; P:actin-mediated cell contraction; IDA:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0032060; P:bleb assembly; IDA:UniProtKB.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0008219; P:cell death; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0007566; P:embryo implantation; IMP:UniProtKB.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; ISS:UniProtKB.
DR GO; GO:0060914; P:heart formation; ISS:UniProtKB.
DR GO; GO:0001765; P:membrane raft assembly; ISS:UniProtKB.
DR GO; GO:0001787; P:natural killer cell proliferation; ISS:UniProtKB.
DR GO; GO:1990266; P:neutrophil migration; ISS:UniProtKB.
DR GO; GO:0044854; P:plasma membrane raft assembly; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0062043; P:positive regulation of cardiac epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:MGI.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IDA:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0010594; P:regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0003093; P:regulation of glomerular filtration; IDA:UniProtKB.
DR GO; GO:0043549; P:regulation of kinase activity; IDA:UniProtKB.
DR GO; GO:2001212; P:regulation of vasculogenesis; IDA:UniProtKB.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; ISS:UniProtKB.
DR InterPro; IPR003933; EMP-2.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR004032; PMP22_EMP_MP20.
DR PANTHER; PTHR10671:SF32; PTHR10671:SF32; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01453; EPMEMFAMILY.
DR PRINTS; PR01455; EPMEMPROT2.
DR PROSITE; PS01221; PMP22_1; 1.
DR PROSITE; PS01222; PMP22_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Disease variant; Glycoprotein; Golgi apparatus;
KW Membrane; Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..167
FT /note="Epithelial membrane protein 2"
FT /id="PRO_0000164658"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 7
FT /note="F -> L (in NPHS10; decreased amount of CAV1;
FT dbSNP:rs730882194)"
FT /evidence="ECO:0000269|PubMed:24814193"
FT /id="VAR_071478"
FT VARIANT 10
FT /note="A -> T (in NPHS10; decreased amount of CAV1;
FT dbSNP:rs587777482)"
FT /evidence="ECO:0000269|PubMed:24814193"
FT /id="VAR_071479"
FT CONFLICT 20
FT /note="F -> L (in Ref. 3; CAA64393)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="V -> F (in Ref. 3; CAA64393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 19199 MW; 3E341DF3581EBCBF CRC64;
MLVLLAFIIA FHITSAALLF IATVDNAWWV GDEFFADVWR ICTNNTNCTV INDSFQEYST
LQAVQATMIL STILCCIAFF IFVLQLFRLK QGERFVLTSI IQLMSCLCVM IAASIYTDRR
EDIHDKNAKF YPVTREGSYG YSYILAWVAF ACTFISGMMY LILRKRK
