MPZL1
entrez
9019
canonical
uniprot
O95297
canonical
ensembl
ENSG00000197965
resolver
ensp
ENSP00000352513
resolver
ensp
ENSP00000375968
resolver
ensp
ENSP00000420455
resolver
genesymbol
MPZL1
resolver
genesymbol_syn
PZR
resolver
hgnc
HGNC:7226
resolver
uniprot
A0A024R8Y6
resolver
uniprot
A8K5D4
resolver
uniprot
B2REB9
resolver
uniprot
B2REC0
resolver
uniprot
Q5R332
resolver
uniprot
Q8IX11
resolver
uniprot
Q9BWZ3
resolver
uniprot
Q9NYK4
resolver
uniprot
Q9UL20
resolver
uniprot_entry
A8K5D4_HUMAN
resolver
uniprot_entry
MPZL1_HUMAN
resolver
uniprot_sec
A0A024R8Y6
resolver
uniprot_sec
B2REB9
resolver
uniprot_sec
B2REC0
resolver
uniprot_sec
Q5R332
resolver
uniprot_sec
Q8IX11
resolver
uniprot_sec
Q9BWZ3
resolver
uniprot_sec
Q9NYK4
resolver
uniprot_sec
Q9UL20
resolver
amino_acid_sequence
MAASAGAGAVIAAPDSRRWLWSVLAAALGLLTAGVSALEVYTPKEIFVANGTQGKLTCKFKSTSTTGGLTSVSWSFQPEGADTTVSFFHYSQGQVYLGNYPPFKDRISWAGDLDKKDASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYVVEKENLPVFPVWVVVGIVTAVVLGLTLLISMILAVLYRRKNSKRDYTGCSTSESLSPVKQAPRKSPSDTEGLVKSLPSGSHQGPVIYAQLDHSGGHHSDKINKSESVVYADIRKN
uniprot
proteins
function
FUNCTION: Cell surface receptor, which is involved in signal transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. Is a major receptor for concanavalin-A (ConA) and is involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases. Isoform 3 seems to have a dominant negative role; it blocks tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, may be involved in regulation of integrin-mediated cell motility. {ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:12410637}.
uniprot
proteins
mass_dalton
29082
uniprot
proteins
mutagenesis
MUTAGEN 241; /note="Y->F: Significantly decreases phosphorylation. Complete loss of phosphorylation; when associated with F-263."; /evidence="ECO:0000269|PubMed:10681522"; MUTAGEN 263; /note="Y->F: Significantly decreases phosphorylation. Complete loss of phosphorylation; when associated with F-241."; /evidence="ECO:0000269|PubMed:10681522
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues upon stimulation with pervanadate and concanavalin-A (ConA). Phosphorylation at Tyr-241 and Tyr-263 is required for interaction with PTPN11/SHP-2. Dephosphorylated by PTPN11/SHP-2 (in vitro). {ECO:0000269|PubMed:10681522, ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:9792637}.; PTM: N-glycosylated. N-glycosylation is required for concanavalin A binding (PubMed:30392906). {ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:30392906, ECO:0000269|PubMed:9792637}.
uniprot
proteins
protein_family
Myelin P0 protein family
uniprot
proteins
pubmed
10681522
uniprot
proteins
pubmed
11751924
uniprot
proteins
pubmed
12075424
uniprot
proteins
pubmed
12410637
uniprot
proteins
pubmed
12684038
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
30392906
uniprot
proteins
pubmed
9792637
uniprot
proteins
sequence_length
269
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 163..183; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins