MPZL1_BOVIN
ID MPZL1_BOVIN Reviewed; 269 AA.
AC Q32PI9; A2SZV4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Myelin protein zero-like protein 1;
DE Flags: Precursor;
GN Name=MPZL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kusano K.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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-241 and
CC Tyr-263 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}.
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; DQ375557; ABD42945.1; -; mRNA.
DR EMBL; BC108099; AAI08100.1; -; mRNA.
DR RefSeq; NP_001069626.1; NM_001076158.1.
DR AlphaFoldDB; Q32PI9; -.
DR SMR; Q32PI9; -.
DR BioGRID; 195954; 1.
DR STRING; 9913.ENSBTAP00000003653; -.
DR PaxDb; Q32PI9; -.
DR PRIDE; Q32PI9; -.
DR Ensembl; ENSBTAT00000003653; ENSBTAP00000003653; ENSBTAG00000002823.
DR GeneID; 539387; -.
DR KEGG; bta:539387; -.
DR CTD; 9019; -.
DR VEuPathDB; HostDB:ENSBTAG00000002823; -.
DR VGNC; VGNC:31592; MPZL1.
DR eggNOG; ENOG502QUEQ; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_090350_3_0_1; -.
DR InParanoid; Q32PI9; -.
DR OMA; RDYTGCN; -.
DR OrthoDB; 1440680at2759; -.
DR TreeFam; TF331728; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000002823; Expressed in myometrium and 103 other tissues.
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..269
FT /note="Myelin protein zero-like protein 1"
FT /id="PRO_0000244395"
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 202..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 202..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 219
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 241
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT MOD_RES 263
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95297"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
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 269 AA; 29314 MW; 0DD2141220F67B27 CRC64;
MAAPAGAGAL IASPDRRRCL WSVLAAALGL LTYGVSALEV YTPKEIFVAN GTQGKLTCKF
KSTNTTGTLT SVSWSFQPEG TDTTVSFFHY SQGQVYAGNY PPFKDRVSWA GDLDKKDASI
NIENMQFIHN GTYICDVKNP PDIVVQPGHI RLYVVEKEIL PAFPVWVVVG IVTAVVLGLT
LLITMILAVI YRRRNSKRDY AGCNTSENVS PVKQVSRKSP SDTEGLVKSL PSGSHQGPVI
YAQLDHSGGH HSDRINKSES VVYADIRKN
