OPALI_BOVIN
ID OPALI_BOVIN Reviewed; 142 AA.
AC Q5E9I3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Opalin;
DE AltName: Full=Oligodendrocytic myelin paranodal and inner loop protein;
DE AltName: Full=Transmembrane protein 10;
GN Name=OPALIN; Synonyms=TMEM10;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Central nervous system-specific myelin protein that increase
CC myelin genes expression during oligodendrocyte differentiation.
CC Promotes oligodendrocyte terminal differentiation.
CC {ECO:0000250|UniProtKB:Q7M750}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7M750};
CC Single-pass type I membrane protein {ECO:0000255}. Note=In the CNS,
CC enriched in the myelin paranodal and inner loop membranes, but not that
CC of the PNS. Enriched in the leading edge of extending processes.
CC {ECO:0000250|UniProtKB:Q7M750}.
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DR EMBL; BT020937; AAX08954.1; -; mRNA.
DR AlphaFoldDB; Q5E9I3; -.
DR InParanoid; Q5E9I3; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0044291; C:cell-cell contact zone; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR InterPro; IPR026609; Opalin.
DR PANTHER; PTHR21102; PTHR21102; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..142
FT /note="Opalin"
FT /id="PRO_0000072590"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 78..94
FT /note="Required for plasma membrane localization"
FT /evidence="ECO:0000250|UniProtKB:Q7M750"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 14
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 142 AA; 15771 MW; FEF979931F237B8D CRC64;
MSFSLNFTLP ANTTSSPVVT SGKGADCGPS LGLAAGIPSL VATALLVALL LILIHRRRRS
SESTEEIERP CEISEIYDNP RVAENPRRSP THEKNIMGAE EAHIYVKTVS GSQEPMRDTY
RPAVEMERRR GLWWLIPRLS LE