GenomeNet

Database: RefSeq
Entry: NP_001166520
LinkDB: NP_001166520
Original site: NP_001166520 
LOCUS       NP_001166520             341 aa            linear   ROD 20-JUN-2025
DEFINITION  low affinity immunoglobulin gamma Fc region receptor II precursor
            [Cavia porcellus].
ACCESSION   NP_001166520
VERSION     NP_001166520.1
DBSOURCE    REFSEQ: accession NM_001173049.1
KEYWORDS    RefSeq.
SOURCE      Cavia porcellus (domestic guinea pig)
  ORGANISM  Cavia porcellus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
            Hystricomorpha; Caviidae; Cavia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Yamashita,T., Shinohara,K. and Yamashita,Y.
  TITLE     Expression cloning of complementary DNA encoding three distinct
            isoforms of guinea pig Fc receptor for IgG1 and IgG2
  JOURNAL   J Immunol 151 (4), 2014-2023 (1993)
   PUBMED   8345193
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Tominaga,M., Sakata,A., Ohmura,T., Yamashita,T., Koyama,J. and
            Onoue,K.
  TITLE     The structure and expression of the guinea pig Fc receptor for IgG1
            and IgG2 (Fc gamma 1/gamma 2R)
  JOURNAL   Biochem Biophys Res Commun 168 (2), 683-689 (1990)
   PUBMED   1692213
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D13693.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D13693.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02693769, SAMN02693772
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Cavia porcellus"
                     /db_xref="taxon:10141"
     Protein         1..341
                     /product="low affinity immunoglobulin gamma Fc region
                     receptor II precursor"
                     /note="Fc-gamma RII; IgG Fc receptor II; Low affinity
                     immunoglobulin gamma Fc region receptor II;
                     Fc-gamma-1/gamma-2 receptor"
                     /calculated_mol_wt=32374
     sig_peptide     1..43
                     /calculated_mol_wt=4736
     mat_peptide     44..341
                     /product="low affinity immunoglobulin gamma Fc region
                     receptor II"
                     /calculated_mol_wt=32374
     Region          50..128
                     /region_name="Ig1_FcgammaR_like"
                     /note="First immunoglobulin (Ig)-like domain of
                     Fcgamma-receptors (FcgammaRs), and similar domains;
                     cd05752"
                     /db_xref="CDD:409410"
     Region          51..54
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409410"
     Site            order(53..54,72,80..83)
                     /site_type="other"
                     /note="pentraxin binding site [polypeptide binding]"
                     /db_xref="CDD:409410"
     Region          59..62
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409410"
     Region          66..72
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409410"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60513.1)"
     Region          82..87
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409410"
     Region          89..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409410"
     Region          97..102
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409410"
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60513.1)"
     Region          109..114
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409410"
     Region          122..128
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409410"
     Region          132..214
                     /region_name="Ig2_FcgammaR_like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     Fcgamma-receptors (FcgammaRs), and similar domains;
                     cd05753"
                     /db_xref="CDD:409411"
     Site            order(132,155,161..162)
                     /site_type="other"
                     /note="Fc binding site [polypeptide binding]"
                     /db_xref="CDD:409411"
     Region          132..136
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409411"
     Region          141..143
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409411"
     Site            order(145..147,156,161,200)
                     /site_type="other"
                     /note="pentraxin binding site [polypeptide binding]"
                     /db_xref="CDD:409411"
     Region          147..154
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409411"
     Region          161..167
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409411"
     Region          170..175
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409411"
     Region          179..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409411"
     Site            180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60513.1)"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60513.1)"
     Region          193..198
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409411"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q60513.1)"
     Region          204..214
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409411"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60513.1)"
     Region          255..274
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60513.1)"
     Region          289..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60513.1)"
     Region          318..323
                     /region_name="ITIM motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60513.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC-type Tyr-kinases.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q60513.1)"
     Region          322..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60513.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P08101; propagated from
                     UniProtKB/Swiss-Prot (Q60513.1)"
     CDS             1..341
                     /gene="Fcgr2b"
                     /gene_synonym="FCGR2; FcRII; Gpifcgr"
                     /coded_by="NM_001173049.1:75..1100"
                     /db_xref="GeneID:100192391"
ORIGIN      
        1 maipsflpvl gtkshradyk plqtlshmll witvlflapv agtsadppka vvrleppwiq
       61 vlrgdrvtlt cegapspgnh stqwlhngrl iptqvlpsyr ftakgndsge yrcqaggtsl
      121 sdpvrldvis dwlvlqtsql ifqegdvivl rchswnnwpl akvtfyhngv akkyfsiskn
      181 fsipqanhsh sgaynctgli grtshtsppv titvqgpkss dssmvviiva avigiataai
      241 vvavvaiicl kkkqppgnpe hremgetlpe dpgeysvvfg gsmmscpglp dglepartdl
      301 snlsdpeeva kseventity sllkhpeaqd ddtehdyqnh i
//
DBGET integrated database retrieval system