MPZL1_MOUSE
ID MPZL1_MOUSE Reviewed; 270 AA.
AC Q3TEW6; Q2VW02; Q6GQX5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Myelin protein zero-like protein 1;
DE AltName: Full=Protein zero-related;
DE Flags: Precursor;
GN Name=Mpzl1; Synonyms=Pzr;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Roubelakis M.G., Martin-Rendon E., Tsaknakis G., Watt S.M.;
RT "The murine ortholog of the SHP-2 binding molecule, PZR, is expressed
RT during mesodermal commitment and accelerates cell migration on
RT fibronectin.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130.
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).
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 2 seems to have a dominant negative role; it blocks tyrosine
CC phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2,
CC may be involved in regulation of integrin-mediated cell motility (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with phosphorylated PTPN11/SHP-2. {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=Q3TEW6-1; Sequence=Displayed;
CC Name=2; Synonyms=b;
CC IsoId=Q3TEW6-2; Sequence=VSP_019345;
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-242 and
CC Tyr-264 is required for interaction with PTPN11/SHP-2. Dephosphorylated
CC by PTPN11/SHP-2 (in vitro) (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; AK169385; BAE41132.1; -; mRNA.
DR EMBL; AY764247; AAX11678.1; -; mRNA.
DR EMBL; AY764248; AAX11679.1; -; mRNA.
DR EMBL; BC072563; AAH72563.1; -; mRNA.
DR CCDS; CCDS35757.1; -. [Q3TEW6-1]
DR RefSeq; NP_001001880.1; NM_001001880.2.
DR RefSeq; NP_001077366.1; NM_001083897.1. [Q3TEW6-1]
DR AlphaFoldDB; Q3TEW6; -.
DR SMR; Q3TEW6; -.
DR STRING; 10090.ENSMUSP00000107062; -.
DR GlyConnect; 2521; 2 N-Linked glycans (2 sites).
DR GlyGen; Q3TEW6; 2 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q3TEW6; -.
DR PhosphoSitePlus; Q3TEW6; -.
DR MaxQB; Q3TEW6; -.
DR PaxDb; Q3TEW6; -.
DR PeptideAtlas; Q3TEW6; -.
DR PRIDE; Q3TEW6; -.
DR ProteomicsDB; 252611; -. [Q3TEW6-1]
DR ProteomicsDB; 252612; -. [Q3TEW6-2]
DR Antibodypedia; 34343; 133 antibodies from 27 providers.
DR DNASU; 68481; -.
DR Ensembl; ENSMUST00000111435; ENSMUSP00000107062; ENSMUSG00000026566. [Q3TEW6-1]
DR GeneID; 68481; -.
DR KEGG; mmu:68481; -.
DR UCSC; uc007djh.1; mouse. [Q3TEW6-1]
DR UCSC; uc007dji.1; mouse. [Q3TEW6-2]
DR CTD; 9019; -.
DR MGI; MGI:1915731; Mpzl1.
DR VEuPathDB; HostDB:ENSMUSG00000026566; -.
DR eggNOG; ENOG502QUEQ; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_090350_3_0_1; -.
DR InParanoid; Q3TEW6; -.
DR OMA; RDYTGCN; -.
DR OrthoDB; 1440680at2759; -.
DR PhylomeDB; Q3TEW6; -.
DR TreeFam; TF331728; -.
DR BioGRID-ORCS; 68481; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Mpzl1; mouse.
DR PRO; PR:Q3TEW6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3TEW6; protein.
DR Bgee; ENSMUSG00000026566; Expressed in otolith organ and 231 other tissues.
DR ExpressionAtlas; Q3TEW6; baseline and differential.
DR Genevisible; Q3TEW6; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..270
FT /note="Myelin protein zero-like protein 1"
FT /id="PRO_0000240336"
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..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..151
FT /note="Ig-like V-type"
FT REGION 201..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 240..245
FT /note="ITIM motif 1"
FT MOTIF 262..267
FT /note="ITIM motif 2"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT MOD_RES 242
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT MOD_RES 264
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 58..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 203..270
FT /note="CSTSERLSPVKQAPRKCPSDTEGLVKSPPSAGSHQGPVIYAQLDHSGGHHSG
FT KINKSESVVYADIRKD -> AQSFT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_019345"
FT CONFLICT 202
FT /note="G -> GFIS (in Ref. 2; AAX11678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 29495 MW; 1E033F0F5F732C22 CRC64;
MAEAVGAVAL IAAPARRRWL WSVLAAMLGL LTARISALEV HTPKEIFVVN GTQGKLTCTF
DSPNTTGWLT TVSWSFQPDG TDSAVSFFHY SQGQVYIGDY PPFKDRVTWA GDLDKKDASI
NIENIQAVHN GTYICDVKNP PDIVVRPGHI RLHVVEIDNL LVFLVWVVVG TVTAVVLGLT
LLISLVLVVL YRRKHSKRDY TGCSTSERLS PVKQAPRKCP SDTEGLVKSP PSAGSHQGPV
IYAQLDHSGG HHSGKINKSE SVVYADIRKD
