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 13-FEB-2019, entry version 164. DE RecName: Full=Myelin protein zero-like protein 1; DE AltName: Full=Protein zero-related; DE Flags: Precursor; GN Name=MPZL1; Synonyms=PZR; ORFNames=UNQ849/PRO1787; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), PROTEIN SEQUENCE OF RP 105-115; 139-157; 198-213 AND 229-254, PHOSPHORYLATION, GLYCOSYLATION, RP INTERACTION 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 RP TISSUE 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 RT tyrosine-based inhibitory motifs."; RL Biochem. Biophys. Res. Commun. 303:1028-1033(2003). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING RP (ISOFORMS 2 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., RA Simmons P.J., Bendall L.J., Henniker A., Harrison K.L., Niutta S., RA Bradstock K.F., Watt S.M.; RT "Novel mesenchymal and haematopoietic cell isoforms of the SHP-2 RT docking receptor, PZR: identification, molecular cloning and effects RT on cell 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., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT family protein containing immunoreceptor tyrosine-based inhibitory RT 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling 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 RT the 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 RP SCALE 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- RT linked 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 RP AND TYR-263, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome 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 RP MASS 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., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Cell surface receptor, which is involved in signal CC transduction processes. Recruits PTPN11/SHP-2 to the cell membrane CC and is a putative substrate of PTPN11/SHP-2. Is a major receptor CC for concanavalin-A (ConA) and is involved in cellular signaling CC induced by ConA, which probably includes Src family tyrosine- CC protein kinases. Isoform 3 seems to have a dominant negative role; CC it blocks tyrosine phosphorylation of MPZL1 induced by ConA. CC Isoform 1, but not isoform 2 and isoform 3, may be involved in CC regulation of integrin-mediated cell motility. CC {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 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 Note=No experimental confirmation available.; 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. CC Isoform 3 appears to be the major isoform in CD34- promyelocytic CC and promonocytic cells. During differentiation in monocytic cells, CC the expression level of isoform 3 decreases and that of isoform 1 CC increases. Isoform 1 is prominent in stromal cells and, to a CC lesser extent, in umbilical vein endothelial cells and erythroid CC progenitors. Isoform 2 is expressed in a erythroid progenitor cell CC line. {ECO:0000269|PubMed:12410637, ECO:0000269|PubMed:12684038, CC ECO:0000269|PubMed:9792637}. CC -!- DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred CC to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). CC This motif is involved in modulation of cellular responses. The CC phosphorylated ITIM motif can bind the SH2 domain of several SH2- CC containing phosphatases. CC -!- PTM: Phosphorylated on tyrosine residues upon stimulation with CC pervanadate and concanavalin-A (ConA). Phosphorylation at Tyr-241 CC and Tyr-263 is required for interaction with PTPN11/SHP-2. CC Dephosphorylated by PTPN11/SHP-2 (in vitro). CC {ECO:0000269|PubMed:10681522, ECO:0000269|PubMed:11751924, CC ECO:0000269|PubMed:9792637}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11751924, CC ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:9792637}. CC -!- SIMILARITY: Belongs to the myelin P0 protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 UniGene; Hs.493919; -. 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 ProteinModelPortal; O95297; -. DR SMR; O95297; -. DR BioGrid; 114486; 63. DR IntAct; O95297; 23. DR MINT; O95297; -. DR STRING; 9606.ENSP00000352513; -. DR GlyConnect; 1527; -. DR iPTMnet; O95297; -. DR PhosphoSitePlus; O95297; -. DR BioMuta; MPZL1; -. DR EPD; O95297; -. DR jPOST; O95297; -. DR MaxQB; O95297; -. DR PaxDb; O95297; -. DR PeptideAtlas; O95297; -. DR PRIDE; O95297; -. DR ProteomicsDB; 50793; -. 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 DNASU; 9019; -. DR Ensembl; ENST00000359523; ENSP00000352513; ENSG00000197965. [O95297-1] DR Ensembl; ENST00000392121; ENSP00000375968; ENSG00000197965. [O95297-5] DR Ensembl; ENST00000474859; ENSP00000420455; ENSG00000197965. [O95297-3] DR GeneID; 9019; -. DR KEGG; hsa:9019; -. DR UCSC; uc001geo.3; human. [O95297-1] DR CTD; 9019; -. DR DisGeNET; 9019; -. DR EuPathDB; HostDB:ENSG00000197965.11; -. DR GeneCards; MPZL1; -. DR H-InvDB; HIX0001303; -. DR HGNC; HGNC:7226; MPZL1. DR HPA; HPA026966; -. DR HPA; HPA063538; -. DR MIM; 604376; gene. DR neXtProt; NX_O95297; -. DR OpenTargets; ENSG00000197965; -. DR PharmGKB; PA30931; -. DR eggNOG; ENOG410IVXC; Eukaryota. DR eggNOG; ENOG4111MDZ; LUCA. DR GeneTree; ENSGT00900000140913; -. DR HOGENOM; HOG000059672; -. DR HOVERGEN; HBG104511; -. DR InParanoid; O95297; -. DR KO; K06770; -. DR OMA; PGNYPPF; -. DR OrthoDB; 1440680at2759; -. DR PhylomeDB; O95297; -. DR TreeFam; TF331728; -. DR SignaLink; O95297; -. DR SIGNOR; O95297; -. DR ChiTaRS; MPZL1; human. DR GeneWiki; MPZL1; -. DR GenomeRNAi; 9019; -. DR PRO; PR:O95297; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000197965; Expressed in 219 organ(s), highest expression level in urinary bladder. 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: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; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 35 {ECO:0000255}. FT CHAIN 36 269 Myelin protein zero-like protein 1. FT /FTId=PRO_0000240335. FT TOPO_DOM 36 162 Extracellular. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TOPO_DOM 184 269 Cytoplasmic. {ECO:0000255}. FT DOMAIN 36 146 Ig-like V-type. FT MOTIF 239 244 ITIM motif 1. FT MOTIF 261 266 ITIM motif 2. FT MOD_RES 204 204 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 206 206 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 208 208 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 210 210 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 219 219 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 221 221 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 241 241 Phosphotyrosine. FT {ECO:0000244|PubMed:19690332, FT ECO:0000269|PubMed:10681522}. FT MOD_RES 260 260 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 263 263 Phosphotyrosine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163, FT ECO:0000269|PubMed:10681522}. FT CARBOHYD 50 50 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19349973}. FT CARBOHYD 130 130 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 58 135 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VAR_SEQ 1 124 Missing (in isoform 4). FT {ECO:0000303|PubMed:12075424}. FT /FTId=VSP_019342. FT VAR_SEQ 42 42 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_019343. FT VAR_SEQ 87 236 Missing (in isoform 5). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043341. FT VAR_SEQ 203 269 CSTSESLSPVKQAPRKSPSDTEGLVKSLPSGSHQGPVIYAQ FT LDHSGGHHSDKINKSESVVYADIRKN -> AQSYMHS (in FT isoform 3). {ECO:0000303|PubMed:12684038, FT ECO:0000303|PubMed:9792637}. FT /FTId=VSP_019344. FT MUTAGEN 241 241 Y->F: Significantly decreases FT phosphorylation. Complete loss of FT phosphorylation; when associated with F- FT 263. {ECO:0000269|PubMed:10681522}. FT MUTAGEN 263 263 Y->F: Significantly decreases FT phosphorylation. Complete loss of FT phosphorylation; when associated with F- FT 241. {ECO:0000269|PubMed:10681522}. FT CONFLICT 42 42 T -> A (in Ref. 4; AAO14646). FT {ECO:0000305}. FT CONFLICT 177 177 L -> I (in Ref. 4; AAO14646). FT {ECO:0000305}. 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 //