SMP_COTJA
ID SMP_COTJA Reviewed; 620 AA.
AC Q92154;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Schwann cell myelin protein;
DE AltName: Full=Siglec-4b;
DE Flags: Precursor;
GN Name=SMP;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-28; 120-132; 135-157
RP AND 563-571.
RX PubMed=1739462; DOI=10.1016/0896-6273(92)90298-r;
RA Dulac C., Tropak M.B., Cameron-Curry P., Rossier J., Marshak D.R.,
RA Roder J., le Douarin N.M.;
RT "Molecular characterization of the Schwann cell myelin protein, SMP:
RT structural similarities within the immunoglobulin superfamily.";
RL Neuron 8:323-334(1992).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Exclusively expressed by myelinating and
CC nonmyelinating Schwann cells and oligodendrocytes.
CC -!- DEVELOPMENTAL STAGE: First synthesized at embryonic day 5, it remains
CC expressed by cultured Schwann cells.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
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DR EMBL; S83711; AAB21466.1; -; mRNA.
DR PIR; JH0593; JH0593.
DR AlphaFoldDB; Q92154; -.
DR SMR; Q92154; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 4.
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; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Lectin; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:1739462"
FT CHAIN 18..620
FT /note="Schwann cell myelin protein"
FT /id="PRO_0000014967"
FT TOPO_DOM 18..516
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..106
FT /note="Ig-like V-type"
FT DOMAIN 151..233
FT /note="Ig-like C2-type 1"
FT DOMAIN 239..322
FT /note="Ig-like C2-type 2"
FT DOMAIN 325..407
FT /note="Ig-like C2-type 3"
FT DOMAIN 414..495
FT /note="Ig-like C2-type 4"
FT REGION 539..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 40..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 260..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 346..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 420..429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 431..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 620 AA; 66943 MW; 004B3EC7EDC18FBA CRC64;
MELLVLTVLL MGTGCISAPW AAWMPPKMAA LSGTCVQLPC RFDYPEELRP ASIGGLWYFG
SPYPKNYPPV VARSRPSSAV HESFAGRASF LGDPTGRDCT LNIARLSEEL AGKYYFRGDL
GGYNQYSFSE HAELDVWAAP HLEVPHELVA GSEAEILCRV PDNCPPLRPL LTWTGTEELL
DPIGKERIED DLGSKSLLGS LRFRPRKEDL GRRVGCGVTF INSSLSFQAD VGLDVQYEPQ
VVGLWGPTEV VEGSDVELGC EAEGRPAPLI SWFRGSEVLR EEPGRNLRLL LSNVGPDDGG
SFSCVAENRH GRHNRSLQLR VAYAPRAPVI NGSLWVVSGD PVSVTCRAES EPAAILTVLR
GGKVMAAAIY EDHVTMEMRP ARPEDGGTYS CVAENQHGAS STSFNISVEY PPLVLPASRC
TAGGDGVRCV CMVNSIPDSS LVFELPTRNQ TVSDGHRDFT AAPPGSDGSI TGILTLRGPL
EPRLLVLCAA RNRHGTTARQ LRFHHPGGLV WAKVGPVGAV VAFAIVIAVV CYLSQSRRKK
GAGSPEVTPV QPMAGPGGDP DLDLRPQQVR WLRGAMERWA LGVKEGSGAP QEVTPTSHPP
MKPTRGPLED PPEYAEIRVK
