MPZL2_MOUSE
ID MPZL2_MOUSE Reviewed; 215 AA.
AC O70255;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Myelin protein zero-like protein 2;
DE AltName: Full=Epithelial V-like antigen 1;
DE Flags: Precursor;
GN Name=Mpzl2; Synonyms=Eva {ECO:0000303|PubMed:9585423}, Eva1;
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.
RC TISSUE=Thymus;
RX PubMed=9585423; DOI=10.1083/jcb.141.4.1061;
RA Guttinger M., Sutti F., Panigada M., Porcellini S., Merati B., Mariani M.,
RA Teesalu T., Consalez G.G., Grassi F.;
RT "Epithelial V-like antigen (EVA), a novel member of the immunoglobulin
RT superfamily, expressed in embryonic epithelia with a potential role as
RT homotypic adhesion molecule in thymus histogenesis.";
RL J. Cell Biol. 141:1061-1071(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-39.
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 [3]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=29961571; DOI=10.1016/j.ajhg.2018.05.011;
RA Wesdorp M., Murillo-Cuesta S., Peters T., Celaya A.M., Oonk A.,
RA Schraders M., Oostrik J., Gomez-Rosas E., Beynon A.J., Hartel B.P.,
RA Okkersen K., Koenen H.J.P.M., Weeda J., Lelieveld S., Voermans N.C.,
RA Joosten I., Hoyng C.B., Lichtner P., Kunst H.P.M., Feenstra I.,
RA de Bruijn S.E., Admiraal R.J.C., Yntema H.G., van Wijk E., Del Castillo I.,
RA Serra P., Varela-Nieto I., Pennings R.J.E., Kremer H.;
RT "MPZL2, encoding the epithelial junctional protein myelin protein zero-like
RT 2, is essential for hearing in man and mouse.";
RL Am. J. Hum. Genet. 103:74-88(2018).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=29982980; DOI=10.1007/s00439-018-1901-4;
RA Bademci G., Abad C., Incesulu A., Rad A., Alper O., Kolb S.M., Cengiz F.B.,
RA Diaz-Horta O., Silan F., Mihci E., Ocak E., Najafi M., Maroofian R.,
RA Yilmaz E., Nur B.G., Duman D., Guo S., Sant D.W., Wang G., Monje P.V.,
RA Haaf T., Blanton S.H., Vona B., Walz K., Tekin M.;
RT "MPZL2 is a novel gene associated with autosomal recessive nonsyndromic
RT moderate hearing loss.";
RL Hum. Genet. 137:479-486(2018).
CC -!- FUNCTION: Mediates homophilic cell-cell adhesion.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:9585423, PubMed:29982980).
CC Expressed in the cochlea, in Deiters' cells, possibly at contact sites
CC with the basilar membrane (PubMed:29961571, PubMed:29982980). Expressed
CC in both outer and inner auditory hair cells (PubMed:29961571,
CC PubMed:29982980). In the stria vascularis, detected in the basal cell
CC layer (PubMed:29961571). Not detected in thymocytes, lymphocytes,
CC macrophage or dendritic cells (PubMed:9585423).
CC {ECO:0000269|PubMed:29961571, ECO:0000269|PubMed:29982980,
CC ECO:0000269|PubMed:9585423}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice display early-onset progressive
CC sensorineural hearing impairment that is more pronounced in the high
CC frequencies. They show an altered organization of outer hair cells and
CC supporting cells and degeneration of the organ of Corti, accompanied by
CC mild degeneration of spiral ganglion neurons, that is most pronounced
CC at the cochlear base. {ECO:0000269|PubMed:29961571}.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; AF030454; AAC40128.1; -; mRNA.
DR CCDS; CCDS23126.1; -.
DR AlphaFoldDB; O70255; -.
DR SMR; O70255; -.
DR IntAct; O70255; 1.
DR STRING; 10090.ENSMUSP00000034600; -.
DR GlyGen; O70255; 2 sites.
DR iPTMnet; O70255; -.
DR PhosphoSitePlus; O70255; -.
DR jPOST; O70255; -.
DR PaxDb; O70255; -.
DR PRIDE; O70255; -.
DR ProteomicsDB; 252613; -.
DR MGI; MGI:1289160; Mpzl2.
DR eggNOG; ENOG502RYWU; Eukaryota.
DR InParanoid; O70255; -.
DR PhylomeDB; O70255; -.
DR ChiTaRS; Mpzl2; mouse.
DR PRO; PR:O70255; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70255; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR029863; MPZL2.
DR InterPro; IPR000920; Myelin_P0-rel.
DR PANTHER; PTHR13869; PTHR13869; 1.
DR PANTHER; PTHR13869:SF21; PTHR13869:SF21; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR00213; MYELINP0.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..215
FT /note="Myelin protein zero-like protein 2"
FT /id="PRO_0000014757"
FT TOPO_DOM 27..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..141
FT /note="Ig-like V-type"
FT REGION 187..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 215 AA; 24162 MW; F6E5E36787CE69D5 CRC64;
MYGKSPALVL PLLLSLQLTA LCPTEAVEIY TSGALEAVNG TDVRLKCTFS SFAPVGDALT
VTWNFRPRDG GREQFVFYYH MDPFRPMSGR FKDRVVWDGN PERYDVSILL WKLQFDDNGT
YTCQVKNPPD VDGLVGTIRL SVVHTVPFSE IYFLAVAIGS ACALMIIVVI VVVLFQHFRK
KRWADRADKA EGTKSKEEEK LNQGNKVSVF VEDTD
