PMP22_BOVIN
ID PMP22_BOVIN Reviewed; 160 AA.
AC Q9TQZ3; A6QLT1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Peripheral myelin protein 22;
DE Short=PMP-22;
DE AltName: Full=PAS positive glycoprotein;
DE Short=PASII;
GN Name=PMP22;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-44 AND 93-123.
RC TISSUE=Peripheral nerve;
RX PubMed=7568893; DOI=10.1016/s0079-6123(08)63309-9;
RA Uyemura K., Asou H., Takeda Y.;
RT "Structure and function of peripheral nerve myelin proteins.";
RL Prog. Brain Res. 105:311-318(1995).
RN [3]
RP GLYCOSYLATION AT ASN-41, AND STRUCTURE OF CARBOHYDRATES.
RX PubMed=10899964; DOI=10.1046/j.1471-4159.2000.0750853.x;
RA Kitamura K., Uyemura K., Shibuya K., Sakamoto Y., Yoshimura K., Nomura M.;
RT "Structure of a major oligosaccharide of PASII/PMP22 glycoprotein in bovine
RT peripheral nerve myelin.";
RL J. Neurochem. 75:853-860(2000).
CC -!- FUNCTION: Might be involved in growth regulation, and in myelinization
CC in the peripheral nervous system.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 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; BC148075; AAI48076.1; -; mRNA.
DR RefSeq; NP_001094626.1; NM_001101156.1.
DR RefSeq; XP_005220437.1; XM_005220380.3.
DR RefSeq; XP_010814341.1; XM_010816039.2.
DR AlphaFoldDB; Q9TQZ3; -.
DR SMR; Q9TQZ3; -.
DR STRING; 9913.ENSBTAP00000025389; -.
DR GlyConnect; 488; 1 N-Linked glycan (1 site).
DR PaxDb; Q9TQZ3; -.
DR Ensembl; ENSBTAT00000025389; ENSBTAP00000025389; ENSBTAG00000019070.
DR GeneID; 534497; -.
DR KEGG; bta:534497; -.
DR CTD; 5376; -.
DR VEuPathDB; HostDB:ENSBTAG00000019070; -.
DR VGNC; VGNC:33074; PMP22.
DR eggNOG; ENOG502S0F5; Eukaryota.
DR GeneTree; ENSGT00950000182696; -.
DR HOGENOM; CLU_138632_1_0_1; -.
DR InParanoid; Q9TQZ3; -.
DR OMA; VRHTDWH; -.
DR OrthoDB; 1513895at2759; -.
DR TreeFam; TF330414; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000019070; Expressed in intramuscular adipose tissue and 103 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032060; P:bleb assembly; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008219; P:cell death; IEA:Ensembl.
DR GO; GO:0032288; P:myelin assembly; IBA:GO_Central.
DR InterPro; IPR003936; PMP22.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR004032; PMP22_EMP_MP20.
DR PANTHER; PTHR10671:SF7; PTHR10671:SF7; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01453; EPMEMFAMILY.
DR PRINTS; PR01458; PMYELIN22.
DR PROSITE; PS01221; PMP22_1; 1.
DR PROSITE; PS01222; PMP22_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell membrane; Direct protein sequencing; Glycoprotein;
KW Growth arrest; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..160
FT /note="Peripheral myelin protein 22"
FT /id="PRO_0000164648"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..31
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 32..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..91
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 92..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..119
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 120..133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..156
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 157..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:10899964"
FT /id="CAR_000191"
FT CONFLICT 122
FT /note="P -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 17803 MW; 428B538661AD4AC3 CRC64;
MLLLLLGIIV LHVAVLVLLF VSTIVSQWMV GNGHATDLWQ NCSTSLMGSV QHCFSSSANE
WLQSVQATMI LSIIFSVLSL FLFFCQLFTL TKGGRFYITG VFQILAGLCV MSAASIYTVR
HPEWHFNSDG SYGFAYILAW VAFPLALLSG VIYVILRKRE