ID   MOR1B_CHICK             Reviewed;         243 AA.
AC   Q2YHT5; Q5ZIJ4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cell surface glycoprotein CD200 receptor 1-B;
DE   AltName: Full=CD200 cell surface glycoprotein receptor 1-B;
DE   AltName: Full=Cell surface glycoprotein OX2 receptor 1-B;
GN   Name=CD200R1B;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=M11;
RX   PubMed=18062907; DOI=10.1016/j.molimm.2007.10.012;
RA   Viertlboeck B.C., Hanczaruk M.A., Schmitt F.C., Schmitt R., Goebel T.W.;
RT   "Characterization of the chicken CD200 receptor family.";
RL   Mol. Immunol. 45:2097-2105(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in peripheral blood lymphocytes (PBL) and
CC       peripheral blood mononuclear cells (PBMC).
CC       {ECO:0000269|PubMed:18062907}.
CC   -!- SIMILARITY: Belongs to the CD200R family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG32449.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM076730; CAJ28372.1; -; mRNA.
DR   EMBL; AJ720790; CAG32449.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q2YHT5; -.
DR   SMR; Q2YHT5; -.
DR   STRING; 9031.ENSGALP00000029813; -.
DR   PaxDb; Q2YHT5; -.
DR   VEuPathDB; HostDB:geneid_418367; -.
DR   eggNOG; ENOG502SPS1; Eukaryota.
DR   InParanoid; Q2YHT5; -.
DR   PhylomeDB; Q2YHT5; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0150077; P:regulation of neuroinflammatory response; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR040012; CD200R.
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   InterPro; IPR013106; Ig_V-set.
DR   PANTHER; PTHR21462; PTHR21462; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW   Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..243
FT                   /note="Cell surface glycoprotein CD200 receptor 1-B"
FT                   /id="PRO_5000076442"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..47
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..243
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..146
FT                   /note="Ig-like V-type"
FT   DOMAIN          144..228
FT                   /note="Ig-like C2-type"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62..130
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        165..214
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   243 AA;  26233 MW;  0719785285D2985C CRC64;
     MEISQQAGWC KKPASPMNTR AALEAVRNTA WTIVLLTSAA VMGASGISRV SANLGHSTVM
     TCPNRTNISM VTWKINPKTG HQCTLAYLID KDSTGKNSCS DRINWRSRPD WDQALEIQQV
     GKADEGNYTC EVVNADGNFH YLYHLTVLVA PRMALYCDDH GNPVCEAETV KPAAEISWVP
     ESNSTPRADS HGNGTVTVVS RFAARSTNGK NPTCIVSHAT LNETRSINCS SRTLAQLPGG
     SAP