ID Q8K4V6_MOUSE Unreviewed; 697 AA.
AC Q8K4V6;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Paired immunoglobulin-like receptor B {ECO:0000313|EMBL:AAG01012.1};
DE Flags: Fragment;
GN Name=Pirb {ECO:0000313|EMBL:AAG01012.1, ECO:0000313|MGI:MGI:894311};
GN Synonyms=Lilrb3 {ECO:0000313|MGI:MGI:894311};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAG01012.1};
RN [1] {ECO:0000313|EMBL:AAG01012.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/cJ {ECO:0000313|EMBL:AAG01012.1};
RC TISSUE=Spleen {ECO:0000313|EMBL:AAG01012.1};
RA Chen C.-C., Hurez V., Kubagawa Y., Kubagawa H., Cooper M.D.;
RT "Mus musculus strain BALB/cJ paired immunoglobulin-like receptor B (Pirb)
RT mRNA.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:6GRQ, ECO:0007829|PDB:6GRS}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 25-619, AND DISULFIDE BONDS.
RX PubMed=30674550; DOI=10.1074/jbc.RA118.004396;
RA Vlieg H.C., Huizinga E.G., Janssen B.J.C.;
RT "Structure and flexibility of the extracellular region of the PirB
RT receptor.";
RL J. Biol. Chem. 294:4634-4643(2019).
CC -!- INTERACTION:
CC Q8K4V6; P15209: Ntrk2; NbExp=4; IntAct=EBI-8602514, EBI-309647;
CC Q8K4V6; P35235: Ptpn11; NbExp=3; IntAct=EBI-8602514, EBI-397236;
CC Q8K4V6; P04629: NTRK1; Xeno; NbExp=2; IntAct=EBI-8602514, EBI-1028226;
CC Q8K4V6; Q63604: Ntrk2; Xeno; NbExp=3; IntAct=EBI-8602514, EBI-7287667;
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DR EMBL; AF288356; AAG01012.1; -; mRNA.
DR PDB; 6GRQ; X-ray; 3.30 A; A=25-619.
DR PDB; 6GRS; X-ray; 3.40 A; A/B=25-619.
DR PDB; 6GRT; X-ray; 4.50 A; A/B=25-619.
DR PDBsum; 6GRQ; -.
DR PDBsum; 6GRS; -.
DR PDBsum; 6GRT; -.
DR AlphaFoldDB; Q8K4V6; -.
DR SMR; Q8K4V6; -.
DR IntAct; Q8K4V6; 5.
DR MINT; Q8K4V6; -.
DR AGR; MGI:894311; -.
DR MGI; MGI:894311; Pirb.
DR ChiTaRS; Pirb; mouse.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR CDD; cd16843; IgC2_D1_D2_LILR_KIR_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 6.
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; IPR013151; Immunoglobulin.
DR PANTHER; PTHR11738:SF182; LEUKOCYTE IMMUNOGLOBULIN-LIKE RECEPTOR SUBFAMILY B MEMBER 3-RELATED; 1.
DR PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6GRQ, ECO:0007829|PDB:6GRS};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius}; Receptor {ECO:0000313|EMBL:AAG01012.1};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..697
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004310505"
FT TRANSMEM 639..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 524..618
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 674..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 129
FT /note="N-acetyl-D-glucosamine 1"
FT /evidence="ECO:0007829|PDB:6GRT"
FT CARBOHYD 172
FT /note="N-acetyl-D-glucosamine 1"
FT /evidence="ECO:0007829|PDB:6GRT"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:6GRT"
FT CARBOHYD 338
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:6GRQ"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:6GRQ"
FT CARBOHYD 467
FT /note="N-acetyl-D-glucosamine 3"
FT /evidence="ECO:0007829|PDB:6GRT"
FT CARBOHYD 500
FT /note="N-acetyl-D-glucosamine 3"
FT /evidence="ECO:0007829|PDB:6GRT"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:6GRT"
FT CARBOHYD 531
FT /note="N-acetyl-D-glucosamine 4"
FT /evidence="ECO:0007829|PDB:6GRS"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:6GRS"
FT DISULFID 49..98
FT /evidence="ECO:0007829|PDB:6GRQ, ECO:0007829|PDB:6GRS"
FT DISULFID 144..197
FT /evidence="ECO:0007829|PDB:6GRQ, ECO:0007829|PDB:6GRS"
FT DISULFID 246..295
FT /evidence="ECO:0007829|PDB:6GRQ, ECO:0007829|PDB:6GRS"
FT DISULFID 343..395
FT /evidence="ECO:0007829|PDB:6GRQ, ECO:0007829|PDB:6GRS"
FT DISULFID 444..495
FT /evidence="ECO:0007829|PDB:6GRQ, ECO:0007829|PDB:6GRS"
FT DISULFID 544..595
FT /evidence="ECO:0007829|PDB:6GRS, ECO:0007829|PDB:6GRT"
FT NON_TER 697
FT /evidence="ECO:0000313|EMBL:AAG01012.1"
SQ SEQUENCE 697 AA; 77508 MW; CFD0D3BDDF55D776 CRC64;
MSCTFTALLC LGLTLSLWIP VLTGSLPKPI LRVQPDSVVS RWTKVTFFCE ETIGANEYRL
YKDGKLYKTV TKNKQKPANK AEFSLSNVDL SNAGQYECSY STQYKSSGYS DPLKLVVTGH
YWTPSLLAQA SPVVTSGGYV TLQCESWHND HKFILTVEGP QKLSWTQDSQ YNYSTRKYHA
LFSVGPVTPN QRWICRCYSY DRNRPYVWSP PSESVELLVS GNLQKPTIKA EPGSVITSKR
AMTIWCQGNL DAEVYFLHNE GSQKTQSTQT LQQPGNKGKF FIPSMTRQHA GQYRCYCYGS
AGWSQPSDTL ELVVTGIYEH YKPRLSVLPS PVVTAGGNMT LHCASDFHYD KFILTKEDKK
FGNSLDTEHI SSSRQYRALF IIGPTTPTHT GTFRCYGYFK NAPQLWSVPS DLQQILISGL
SKKPSLLTHQ GHILDPGMTL TLQCYSDINY DRFALHKVGG ADIMQHSSQQ TDTGFSVANF
TLGYVSSSTG GQYRCYGAHN LSSEWSASSE PLDILITGQL PLTPSLSVKP NHTVHSGETV
SLLCWSMDSV DTFILSKEGS AQQPLRLKSK SHDQQSQAEF SMSAVTSHLS GTYRCYGAQN
SSFYLLSSAS APVELTVSGP IETSTPPPTM SMPLGGLHMY LKALIGVSVA FILFLFILIF
ILLRRRHRGK FRKDVQKEKD LQLSSGAEEP ITRKGKG
//
