MPZL3_MOUSE
ID MPZL3_MOUSE Reviewed; 237 AA.
AC Q3V3F6; A5H7F1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Myelin protein zero-like protein 3;
DE Flags: Precursor;
GN Name=Mpzl3;
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], TISSUE SPECIFICITY, AND VARIANT RC GLN-100.
RC STRAIN=C57BL/6J;
RX PubMed=17273165; DOI=10.1038/sj.jid.5700706;
RA Cao T., Racz P., Szauter K.M., Groma G., Nakamatsu G.Y., Fogelgren B.,
RA Pankotai E., He Q.-P., Csiszar K.;
RT "Mutation in Mpzl3, a novel gene encoding a predicted adhesion protein, in
RT rough coat (rc) mice with severe skin and hair abnormalities.";
RL J. Invest. Dermatol. 127:1375-1386(2007).
RN [2]
RP ERRATUM OF PUBMED:17273165.
RA Aul R.B., Oko R.J.;
RL J. Invest. Dermatol. 127:2678-2678(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
CC -!- FUNCTION: Mediates homophilic cell-cell adhesion. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3V3F6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3V3F6-2; Sequence=VSP_023606, VSP_023607;
CC -!- TISSUE SPECIFICITY: Present in all tissues tested, including the skin.
CC Present in the keratinocytes and sebocytes in the skin (at protein
CC level). {ECO:0000269|PubMed:17273165}.
CC -!- DISEASE: Note=Defects in Mpzl3 are the cause of rough coat (rc)
CC phenotype, an autosomal-recessive mutation, arose spontaneously in
CC C57BL/6J mice. Rc mice develop severe skin and hair abnormalities,
CC including cyclic and progressive hair loss and sebaceous gland
CC hypertrophy.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; EF102773; ABO21574.1; -; mRNA.
DR EMBL; AK041037; BAC30792.1; -; mRNA.
DR EMBL; AC122305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132150; AAI32151.1; -; mRNA.
DR CCDS; CCDS52781.1; -. [Q3V3F6-1]
DR RefSeq; NP_001087218.1; NM_001093749.2. [Q3V3F6-1]
DR AlphaFoldDB; Q3V3F6; -.
DR SMR; Q3V3F6; -.
DR STRING; 10090.ENSMUSP00000110312; -.
DR GlyGen; Q3V3F6; 1 site.
DR PhosphoSitePlus; Q3V3F6; -.
DR SwissPalm; Q3V3F6; -.
DR PaxDb; Q3V3F6; -.
DR PRIDE; Q3V3F6; -.
DR ProteomicsDB; 252614; -. [Q3V3F6-1]
DR ProteomicsDB; 252615; -. [Q3V3F6-2]
DR Antibodypedia; 32439; 95 antibodies from 17 providers.
DR Ensembl; ENSMUST00000114664; ENSMUSP00000110312; ENSMUSG00000070305. [Q3V3F6-1]
DR GeneID; 319742; -.
DR KEGG; mmu:319742; -.
DR UCSC; uc009pfb.3; mouse. [Q3V3F6-2]
DR UCSC; uc009pfc.2; mouse. [Q3V3F6-1]
DR CTD; 196264; -.
DR MGI; MGI:2442647; Mpzl3.
DR VEuPathDB; HostDB:ENSMUSG00000070305; -.
DR eggNOG; ENOG502RYH4; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_090350_1_0_1; -.
DR InParanoid; Q3V3F6; -.
DR OMA; FFQGVHI; -.
DR OrthoDB; 1437254at2759; -.
DR PhylomeDB; Q3V3F6; -.
DR BioGRID-ORCS; 319742; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Mpzl3; mouse.
DR PRO; PR:Q3V3F6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3V3F6; protein.
DR Bgee; ENSMUSG00000070305; Expressed in tail skin and 131 other tissues.
DR ExpressionAtlas; Q3V3F6; baseline and differential.
DR Genevisible; Q3V3F6; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0042633; P:hair cycle; 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; IPR029862; MPZL3.
DR InterPro; IPR000920; Myelin_P0-rel.
DR PANTHER; PTHR13869; PTHR13869; 1.
DR PANTHER; PTHR13869:SF20; PTHR13869:SF20; 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 Alternative splicing; Cell adhesion; Disease variant; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000250"
FT CHAIN 33..237
FT /note="Myelin protein zero-like protein 3"
FT /id="PRO_0000280283"
FT TOPO_DOM 33..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..149
FT /note="Ig-like V-type"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 82..96
FT /note="IFHYQSFQYPTTAGT -> VSVGFPERPLECLAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023606"
FT VAR_SEQ 97..237
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023607"
FT VARIANT 100
FT /note="R -> Q (in rc)"
FT /evidence="ECO:0000269|PubMed:17273165"
SQ SEQUENCE 237 AA; 26058 MW; CC2DCF60801A4EE1 CRC64;
MQLARGTVGG RGCALFPLLS ILVVQGARIV LSLEISADAH VRGYVGEKIK LKCTFKSSSD
VTDKLTIDWT YRPPSSSRTE SIFHYQSFQY PTTAGTFRDR ISWAGNVYKG DASISISNPT
LKDNGTFSCA VKNPPDVYHN IPLTELTVTE RGFGTMLSSV ALLSILVFVP SAVVVILLLV
RMGRKATGVQ KRSRSGYKKS SIEVSDDTDQ EDSNDCMTRL CVRCAECLDS DYEEEAY
