MPZL1_HUMAN
ID MPZL1_HUMAN Reviewed; 269 AA.
AC O95297; B2REB9; B2REC0; Q5R332; Q8IX11; Q9BWZ3; Q9NYK4; Q9UL20;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Myelin protein zero-like protein 1;
DE AltName: Full=Protein zero-related;
DE Flags: Precursor;
GN Name=MPZL1; Synonyms=PZR {ECO:0000303|PubMed:9792637};
GN ORFNames=UNQ849/PRO1787;
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] (ISOFORMS 1 AND 3), PROTEIN SEQUENCE OF 105-115;
RP 139-157; 198-213 AND 229-254, PHOSPHORYLATION, GLYCOSYLATION, INTERACTION
RP WITH PTPN11, AND TISSUE SPECIFICITY.
RX PubMed=9792637; DOI=10.1074/jbc.273.45.29367;
RA Zhao Z.J., Zhao R.;
RT "Purification and cloning of PZR, a binding protein and putative
RT physiological substrate of tyrosine phosphatase SHP-2.";
RL J. Biol. Chem. 273:29367-29372(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Fetal liver;
RX PubMed=12075424;
RA Tang D.S., Yu K.P., Tang X.X., Zhang H.L., Pan Q., Dai H.P., Xia J.H.;
RT "Cloning of human myelin protein zero-like genes by bioinformatics
RT strategy.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 32:364-368(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION (ISOFORM 3), AND TISSUE
RP SPECIFICITY.
RX PubMed=12684038; DOI=10.1016/s0006-291x(03)00484-4;
RA Zhao R., Zhao Z.J.;
RT "Identification of a variant form of PZR lacking immunoreceptor tyrosine-
RT based inhibitory motifs.";
RL Biochem. Biophys. Res. Commun. 303:1028-1033(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING (ISOFORMS 2
RP AND 3), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12410637; DOI=10.1042/bj20020935;
RA Zannettino A.C.W., Roubelakis M., Welldon K.J., Jackson D.E., Simmons P.J.,
RA Bendall L.J., Henniker A., Harrison K.L., Niutta S., Bradstock K.F.,
RA Watt S.M.;
RT "Novel mesenchymal and haematopoietic cell isoforms of the SHP-2 docking
RT receptor, PZR: identification, molecular cloning and effects on cell
RT migration.";
RL Biochem. J. 370:537-549(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [11]
RP PHOSPHORYLATION AT TYR-241 AND TYR-263, INTERACTION WITH PTPN11,
RP DEPHOSPHORYLATION BY PTPN11, AND MUTAGENESIS OF TYR-241 AND TYR-263.
RX PubMed=10681522; DOI=10.1074/jbc.275.8.5453;
RA Zhao R., Zhao Z.J.;
RT "Dissecting the interaction of SHP-2 with PZR, an immunoglobulin family
RT protein containing immunoreceptor tyrosine-based inhibitory motifs.";
RL J. Biol. Chem. 275:5453-5459(2000).
RN [12]
RP FUNCTION, GLYCOSYLATION, AND PHOSPHORYLATION.
RX PubMed=11751924; DOI=10.1074/jbc.m111914200;
RA Zhao R., Guerrah A., Tang H., Zhao Z.J.;
RT "Cell surface glycoprotein PZR is a major mediator of concanavalin A-
RT induced cell signaling.";
RL J. Biol. Chem. 277:7882-7888(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-210; SER-219;
RP SER-260 AND TYR-263, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50.
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).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-241 AND TYR-263, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-219; SER-221 AND
RP TYR-263, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 AND SER-221, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-206; SER-208;
RP SER-210; SER-219; SER-221; SER-260 AND TYR-263, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23] {ECO:0007744|PDB:6IGO, ECO:0007744|PDB:6IGT, ECO:0007744|PDB:6IGW}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 36-162, GLYCOSYLATION AT ASN-50
RP AND ASN-130, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BONDS.
RX PubMed=30392906; DOI=10.1016/j.bbrc.2018.10.161;
RA Yu T., Liang L., Zhao X., Yin Y.;
RT "Structural and biochemical studies of the extracellular domain of Myelin
RT protein zero-like protein 1.";
RL Biochem. Biophys. Res. Commun. 506:883-890(2018).
CC -!- FUNCTION: Cell surface receptor, which is involved in signal
CC transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and
CC is a putative substrate of PTPN11/SHP-2. Is a major receptor for
CC concanavalin-A (ConA) and is involved in cellular signaling induced by
CC ConA, which probably includes Src family tyrosine-protein kinases.
CC Isoform 3 seems to have a dominant negative role; it blocks tyrosine
CC phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2
CC and isoform 3, may be involved in regulation of integrin-mediated cell
CC motility. {ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:12410637}.
CC -!- SUBUNIT: Interacts with phosphorylated PTPN11/SHP-2.
CC {ECO:0000269|PubMed:10681522, ECO:0000269|PubMed:9792637}.
CC -!- INTERACTION:
CC O95297; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-963338, EBI-11956541;
CC O95297; Q06124: PTPN11; NbExp=4; IntAct=EBI-963338, EBI-297779;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=MPZL1a;
CC IsoId=O95297-1; Sequence=Displayed;
CC Name=2; Synonyms=PZR1a;
CC IsoId=O95297-2; Sequence=VSP_019343;
CC Name=3; Synonyms=PZR1b;
CC IsoId=O95297-3; Sequence=VSP_019344;
CC Name=4; Synonyms=MPZL1b;
CC IsoId=O95297-4; Sequence=VSP_019342;
CC Name=5;
CC IsoId=O95297-5; Sequence=VSP_043341;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart,
CC placenta, kidney and pancreas. Isoform 3 is relatively abundant in
CC hematopoietic tissues and fetal liver. Isoform 1 and isoform 3 are
CC expressed in CD14- PB monocytes and pre-B cell progenitors. Isoform 3
CC appears to be the major isoform in CD34- promyelocytic and promonocytic
CC cells. During differentiation in monocytic cells, the expression level
CC of isoform 3 decreases and that of isoform 1 increases. Isoform 1 is
CC prominent in stromal cells and, to a lesser extent, in umbilical vein
CC endothelial cells and erythroid progenitors. Isoform 2 is expressed in
CC a erythroid progenitor cell line. {ECO:0000269|PubMed:12410637,
CC ECO:0000269|PubMed:12684038, ECO:0000269|PubMed:9792637}.
CC -!- DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- PTM: Phosphorylated on tyrosine residues upon stimulation with
CC pervanadate and concanavalin-A (ConA). Phosphorylation at Tyr-241 and
CC Tyr-263 is required for interaction with PTPN11/SHP-2. Dephosphorylated
CC by PTPN11/SHP-2 (in vitro). {ECO:0000269|PubMed:10681522,
CC ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:9792637}.
CC -!- PTM: N-glycosylated. N-glycosylation is required for concanavalin A
CC binding (PubMed:30392906). {ECO:0000269|PubMed:11751924,
CC ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:30392906,
CC ECO:0000269|PubMed:9792637}.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; AF087020; AAC72231.1; -; mRNA.
DR EMBL; AF092424; AAD55346.1; -; mRNA.
DR EMBL; AF092425; AAD55347.1; -; mRNA.
DR EMBL; AF095726; AAF00083.1; -; mRNA.
DR EMBL; AF095727; AAF00084.1; -; mRNA.
DR EMBL; AF239756; AAF63499.1; -; mRNA.
DR EMBL; AF478447; AAO14645.1; -; mRNA.
DR EMBL; AF478448; AAO14647.1; -; Genomic_DNA.
DR EMBL; AF478448; AAO14646.1; -; Genomic_DNA.
DR EMBL; AY359019; AAQ89378.1; -; mRNA.
DR EMBL; AK297112; BAH12501.1; -; mRNA.
DR EMBL; CR542160; CAG46957.1; -; mRNA.
DR EMBL; AL356532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z99943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90800.1; -; Genomic_DNA.
DR EMBL; BC007881; AAH07881.1; -; mRNA.
DR CCDS; CCDS1264.1; -. [O95297-1]
DR CCDS; CCDS44273.1; -. [O95297-3]
DR CCDS; CCDS53425.1; -. [O95297-5]
DR RefSeq; NP_001139663.1; NM_001146191.1. [O95297-5]
DR RefSeq; NP_003944.1; NM_003953.5. [O95297-1]
DR RefSeq; NP_078845.3; NM_024569.4. [O95297-3]
DR PDB; 6IGO; X-ray; 2.75 A; A/B/C/D/E/F=36-162.
DR PDB; 6IGT; X-ray; 2.40 A; A/B/C/D=36-162.
DR PDB; 6IGW; X-ray; 1.98 A; A=36-162.
DR PDBsum; 6IGO; -.
DR PDBsum; 6IGT; -.
DR PDBsum; 6IGW; -.
DR AlphaFoldDB; O95297; -.
DR SMR; O95297; -.
DR BioGRID; 114486; 124.
DR IntAct; O95297; 63.
DR MINT; O95297; -.
DR STRING; 9606.ENSP00000352513; -.
DR GlyConnect; 1527; 31 N-Linked glycans (2 sites).
DR GlyGen; O95297; 6 sites, 31 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; O95297; -.
DR PhosphoSitePlus; O95297; -.
DR BioMuta; MPZL1; -.
DR EPD; O95297; -.
DR jPOST; O95297; -.
DR MassIVE; O95297; -.
DR MaxQB; O95297; -.
DR PaxDb; O95297; -.
DR PeptideAtlas; O95297; -.
DR PRIDE; O95297; -.
DR ProteomicsDB; 50793; -. [O95297-1]
DR ProteomicsDB; 50794; -. [O95297-2]
DR ProteomicsDB; 50795; -. [O95297-3]
DR ProteomicsDB; 50796; -. [O95297-4]
DR ProteomicsDB; 50797; -. [O95297-5]
DR TopDownProteomics; O95297-1; -. [O95297-1]
DR Antibodypedia; 34343; 133 antibodies from 27 providers.
DR DNASU; 9019; -.
DR Ensembl; ENST00000359523.7; ENSP00000352513.2; ENSG00000197965.12. [O95297-1]
DR Ensembl; ENST00000392121.7; ENSP00000375968.3; ENSG00000197965.12. [O95297-5]
DR Ensembl; ENST00000474859.5; ENSP00000420455.1; ENSG00000197965.12. [O95297-3]
DR GeneID; 9019; -.
DR KEGG; hsa:9019; -.
DR MANE-Select; ENST00000359523.7; ENSP00000352513.2; NM_003953.6; NP_003944.1.
DR UCSC; uc001geo.3; human. [O95297-1]
DR CTD; 9019; -.
DR DisGeNET; 9019; -.
DR GeneCards; MPZL1; -.
DR HGNC; HGNC:7226; MPZL1.
DR HPA; ENSG00000197965; Low tissue specificity.
DR MIM; 604376; gene.
DR neXtProt; NX_O95297; -.
DR OpenTargets; ENSG00000197965; -.
DR PharmGKB; PA30931; -.
DR VEuPathDB; HostDB:ENSG00000197965; -.
DR eggNOG; ENOG502QUEQ; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_090350_3_0_1; -.
DR InParanoid; O95297; -.
DR OMA; RDYTGCN; -.
DR PhylomeDB; O95297; -.
DR TreeFam; TF331728; -.
DR PathwayCommons; O95297; -.
DR SignaLink; O95297; -.
DR SIGNOR; O95297; -.
DR BioGRID-ORCS; 9019; 22 hits in 1078 CRISPR screens.
DR ChiTaRS; MPZL1; human.
DR GeneWiki; MPZL1; -.
DR GenomeRNAi; 9019; -.
DR Pharos; O95297; Tbio.
DR PRO; PR:O95297; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95297; protein.
DR Bgee; ENSG00000197965; Expressed in stromal cell of endometrium and 193 other tissues.
DR ExpressionAtlas; O95297; baseline and differential.
DR Genevisible; O95297; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
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; IPR029870; MPZL1.
DR InterPro; IPR000920; Myelin_P0-rel.
DR PANTHER; PTHR13869; PTHR13869; 1.
DR PANTHER; PTHR13869:SF19; PTHR13869:SF19; 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 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..269
FT /note="Myelin protein zero-like protein 1"
FT /id="PRO_0000240335"
FT TOPO_DOM 36..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..146
FT /note="Ig-like V-type"
FT REGION 199..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 239..244
FT /note="ITIM motif 1"
FT MOTIF 261..266
FT /note="ITIM motif 2"
FT COMPBIAS 201..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 241
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10681522,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 263
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10681522,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:30392906"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30392906"
FT DISULFID 58..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:30392906, ECO:0007744|PDB:6IGO"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12075424"
FT /id="VSP_019342"
FT VAR_SEQ 42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_019343"
FT VAR_SEQ 87..236
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043341"
FT VAR_SEQ 203..269
FT /note="CSTSESLSPVKQAPRKSPSDTEGLVKSLPSGSHQGPVIYAQLDHSGGHHSDK
FT INKSESVVYADIRKN -> AQSYMHS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12684038,
FT ECO:0000303|PubMed:9792637"
FT /id="VSP_019344"
FT MUTAGEN 241
FT /note="Y->F: Significantly decreases phosphorylation.
FT Complete loss of phosphorylation; when associated with F-
FT 263."
FT /evidence="ECO:0000269|PubMed:10681522"
FT MUTAGEN 263
FT /note="Y->F: Significantly decreases phosphorylation.
FT Complete loss of phosphorylation; when associated with F-
FT 241."
FT /evidence="ECO:0000269|PubMed:10681522"
FT CONFLICT 42
FT /note="T -> A (in Ref. 4; AAO14646)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="L -> I (in Ref. 4; AAO14646)"
FT /evidence="ECO:0000305"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6IGO"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6IGW"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6IGW"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6IGW"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:6IGW"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6IGW"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:6IGW"
SQ SEQUENCE 269 AA; 29082 MW; A1B299041EE59425 CRC64;
MAASAGAGAV IAAPDSRRWL WSVLAAALGL LTAGVSALEV YTPKEIFVAN GTQGKLTCKF
KSTSTTGGLT SVSWSFQPEG ADTTVSFFHY SQGQVYLGNY PPFKDRISWA GDLDKKDASI
NIENMQFIHN GTYICDVKNP PDIVVQPGHI RLYVVEKENL PVFPVWVVVG IVTAVVLGLT
LLISMILAVL YRRKNSKRDY TGCSTSESLS PVKQAPRKSP SDTEGLVKSL PSGSHQGPVI
YAQLDHSGGH HSDKINKSES VVYADIRKN
