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Epithelial membrane protein 2 (EMP-2)

 EMP2_RAT                Reviewed;         172 AA.
Q66HH2;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
23-MAY-2018, entry version 94.
RecName: Full=Epithelial membrane protein 2;
Short=EMP-2;
Name=Emp2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000312|EMBL:AAH81865.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=24814193; DOI=10.1016/j.ajhg.2014.04.010;
Gee H.Y., Ashraf S., Wan X., Vega-Warner V., Esteve-Rudd J.,
Lovric S., Fang H., Hurd T.W., Sadowski C.E., Allen S.J., Otto E.A.,
Korkmaz E., Washburn J., Levy S., Williams D.S., Bakkaloglu S.A.,
Zolotnitskaya A., Ozaltin F., Zhou W., Hildebrandt F.;
"Mutations in EMP2 cause childhood-onset nephrotic syndrome.";
Am. J. Hum. Genet. 94:884-890(2014).
-!- FUNCTION: Functions as a key regulator of cell membrane
composition by regulating proteins surface expression. Also, plays
a role in regulation of processes including cell migration, cell
proliferation, cell contraction and cell adhesion. Negatively
regulates caveolae formation by reducing CAV1 expression and CAV1
amount by increasing lysosomal degradation. Facilitates surface
trafficking and the formation of lipid rafts bearing GPI-anchor
proteins. Regulates surface expression of MHC1 and ICAM1 proteins
increasing susceptibility to T-cell mediated cytotoxicity.
Regulates the plasma membrane expression of the integrin
heterodimers ITGA6-ITGB1, ITGA5-ITGB3 and ITGA5-ITGB1 resulting in
modulation of cell-matrix adhesion. Also regulates many processes
through PTK2. Regulates blood vessel endothelial cell migration
and angiogenesis by regulating VEGF protein expression through
PTK2 activation. Regulates cell migration and cell contraction
through PTK2 and SRC activation. Regulates focal adhesion density,
F-actin conformation and cell adhesion capacity through
interaction with PTK2. Positively regulates cell proliferation.
Plays a role during cell death and cell blebbing. Promotes
angiogenesis and vasculogenesis through induction of VEGFA via a
HIF1A-dependent pathway. Also plays a role in embryo implantation
by regulating surface trafficking of integrin heterodimer ITGA5-
ITGB3. May play a role in glomerular filtration.
{ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662,
ECO:0000250|UniProtKB:P54851}.
-!- SUBUNIT: Interacts with PTK2; regulates PTK2 activation and
localization. Interacts with ITGB3; regulates the levels of the
heterodimer ITGA5-ITGB3 integrin surface expression. Interacts
with P2RX7 (via C-terminus). Interacts with ITGB1; the interaction
may be direct or indirect and ITGB1 has a heterodimer form.
{ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein
{ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O88662,
ECO:0000250|UniProtKB:P54851}. Apical cell membrane
{ECO:0000250|UniProtKB:O88662}. Membrane raft
{ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}.
Cytoplasm {ECO:0000250|UniProtKB:O88662,
ECO:0000250|UniProtKB:P54851, ECO:0000269|PubMed:24814193}.
Nucleus {ECO:0000269|PubMed:24814193}. Note=Localizes in
cytoplasm, foot processes and cell bodies of podocytes and nucleus
of endothelial cells of kidney (PubMed:24814193). Localizes to the
apical cell surface in the luminal epithelium and glandular
epithelium. Colocalized with ITGB1 and GPI-anchor proteins on
plasma membrane (By similarity). {ECO:0000250|UniProtKB:O88662,
ECO:0000269|PubMed:24814193}.
-!- TISSUE SPECIFICITY: Expressed in glomeruli.
{ECO:0000269|PubMed:24814193}.
-!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AABR06062648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06062649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06062650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06062651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06062652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474017; EDL96228.1; -; Genomic_DNA.
EMBL; BC081865; AAH81865.1; -; mRNA.
RefSeq; NP_001007722.1; NM_001007721.1.
UniGene; Rn.21730; -.
STRING; 10116.ENSRNOP00000003615; -.
PaxDb; Q66HH2; -.
Ensembl; ENSRNOT00000003615; ENSRNOP00000003615; ENSRNOG00000002664.
GeneID; 360468; -.
KEGG; rno:360468; -.
UCSC; RGD:1359629; rat.
CTD; 2013; -.
RGD; 1359629; Emp2.
eggNOG; ENOG410IH06; Eukaryota.
eggNOG; ENOG4111QXD; LUCA.
GeneTree; ENSGT00510000046328; -.
HOGENOM; HOG000059542; -.
HOVERGEN; HBG001690; -.
InParanoid; Q66HH2; -.
OMA; IQLMSCL; -.
OrthoDB; EOG091G0RF4; -.
PhylomeDB; Q66HH2; -.
TreeFam; TF330414; -.
PRO; PR:Q66HH2; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000002664; -.
Genevisible; Q66HH2; RN.
GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
GO; GO:0070252; P:actin-mediated cell contraction; ISS:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
GO; GO:0032060; P:bleb assembly; ISS:UniProtKB.
GO; GO:0043534; P:blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0008219; P:cell death; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; ISS:UniProtKB.
GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
GO; GO:0001765; P:membrane raft assembly; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0010594; P:regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0003093; P:regulation of glomerular filtration; ISS:UniProtKB.
GO; GO:0043549; P:regulation of kinase activity; ISS:UniProtKB.
GO; GO:2001212; P:regulation of vasculogenesis; ISS:UniProtKB.
GO; GO:0001913; P:T cell mediated cytotoxicity; ISS:UniProtKB.
InterPro; IPR003933; EMP-2.
InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
InterPro; IPR004032; PMP22_EMP_MP20.
PANTHER; PTHR10671:SF32; PTHR10671:SF32; 1.
Pfam; PF00822; PMP22_Claudin; 1.
PRINTS; PR01453; EPMEMFAMILY.
PRINTS; PR01455; EPMEMPROT2.
PROSITE; PS01221; PMP22_1; 1.
PROSITE; PS01222; PMP22_2; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Cytoplasm; Golgi apparatus;
Membrane; Nucleus; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 172 Epithelial membrane protein 2.
/FTId=PRO_0000430724.
TRANSMEM 1 21 Helical; Name=1. {ECO:0000255}.
TRANSMEM 72 92 Helical; Name=2. {ECO:0000255}.
TRANSMEM 100 120 Helical; Name=3. {ECO:0000255}.
TRANSMEM 148 168 Helical; Name=4. {ECO:0000255}.
SEQUENCE 172 AA; 19649 MW; 2786C2686BDDBE2E CRC64;
MLVILAFIIV FHIVSTALLF ISTIDNAWWV GDGFSADIWR VCTNSTNCTE INDLSSTEEF
SGYSVMQAVQ ATMILSTILS CISFLIFLLQ LFRLKQGERF VLTAIIQLMS CLCVMIGASV
YTDRRQDLHH QNSQLYYLLQ EGSYGYSFIL AWVAFAFTFI SGLMYMILRK RK


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