MPZL1_RAT
ID MPZL1_RAT Reviewed; 270 AA.
AC Q6AYT8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Myelin protein zero-like protein 1;
DE Flags: Precursor;
GN Name=Mpzl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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: 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. May
CC 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 -!- 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 -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the myelin P0 protein family. {ECO:0000305}.
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DR EMBL; BC078916; AAH78916.1; -; mRNA.
DR RefSeq; NP_001007729.1; NM_001007728.1.
DR AlphaFoldDB; Q6AYT8; -.
DR SMR; Q6AYT8; -.
DR STRING; 10116.ENSRNOP00000004376; -.
DR GlyGen; Q6AYT8; 2 sites.
DR iPTMnet; Q6AYT8; -.
DR PhosphoSitePlus; Q6AYT8; -.
DR PaxDb; Q6AYT8; -.
DR Ensembl; ENSRNOT00000004376; ENSRNOP00000004376; ENSRNOG00000003248.
DR GeneID; 360871; -.
DR KEGG; rno:360871; -.
DR UCSC; RGD:1359140; rat.
DR CTD; 9019; -.
DR RGD; 1359140; Mpzl1.
DR eggNOG; ENOG502QUEQ; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_090350_3_0_1; -.
DR InParanoid; Q6AYT8; -.
DR OMA; RDYTGCN; -.
DR OrthoDB; 1440680at2759; -.
DR PhylomeDB; Q6AYT8; -.
DR TreeFam; TF331728; -.
DR PRO; PR:Q6AYT8; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003248; Expressed in lung and 20 other tissues.
DR Genevisible; Q6AYT8; RN.
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 2: Evidence at transcript level;
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..270
FT /note="Myelin protein zero-like protein 1"
FT /id="PRO_0000240337"
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:0000255"
FT DISULFID 58..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 270 AA; 29502 MW; C1B6FBEBBBC45C3D CRC64;
MAEAVGAVTL IAAPARRRWL WSALAAMLGL LTARISALEV HTPKEIFVVN GTQGKLTCTF
DSPNTTGWLT TVSWSFQPEG TDSAVSFFHY SQGQVYIGDY PPFKDRVTWA GDLDKKDASI
NIENIQAVHN GTYICDVKNP PDIVVRPGQI RLHVVEIDNL LVFLVWVVVG TVTAVVLGLT
LLISLVLVVL YRRKHSKRDY TGCSTSERLS PVKQAPRKCP SDTEGLVKSP PSAGSHQGPV
IYAQLDHSGG HHSGKINKSE SVVYADIRKD
