LOCUS       NP_203502                366 aa            linear   ROD 03-JUN-2024
DEFINITION  IgG receptor FcRn large subunit p51 precursor [Rattus norvegicus].
ACCESSION   NP_203502
VERSION     NP_203502.1
DBSOURCE    REFSEQ: accession NM_033351.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Yadav,S.P.S., Sandoval,R.M., Zhao,J., Huang,Y., Wang,E., Kumar,S.,
            Campos-Bilderback,S.B., Rhodes,G., Mechref,Y., Molitoris,B.A. and
            Wagner,M.C.
  TITLE     Mechanism of how carbamylation reduces albumin binding to FcRn
            contributing to increased vascular clearance
  JOURNAL   Am J Physiol Renal Physiol 320 (1), F114-F129 (2021)
   PUBMED   33283642
  REMARK    GeneRIF: Mechanism of how carbamylation reduces albumin binding to
            FcRn contributing to increased vascular clearance.
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Wagner,M.C., Myslinski,J., Pratap,S., Flores,B., Rhodes,G.,
            Campos-Bilderback,S.B., Sandoval,R.M., Kumar,S., Patel,M., Ashish
            and Molitoris,B.A.
  TITLE     Mechanism of increased clearance of glycated albumin by proximal
            tubule cells
  JOURNAL   Am J Physiol Renal Physiol 310 (10), F1089-F1102 (2016)
   PUBMED   26887834
  REMARK    GeneRIF: significant structural changes occur to albumin with
            glycation, particularly in the FcRn-binding region, which could
            explain the reduced affinity to FcRn
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Abdiche,Y.N., Yeung,Y.A., Chaparro-Riggers,J., Barman,I., Strop,P.,
            Chin,S.M., Pham,A., Bolton,G., McDonough,D., Lindquist,K., Pons,J.
            and Rajpal,A.
  TITLE     The neonatal Fc receptor (FcRn) binds independently to both sites
            of the IgG homodimer with identical affinity
  JOURNAL   MAbs 7 (2), 331-343 (2015)
   PUBMED   25658443
  REMARK    GeneRIF: The neonatal Fc receptor (FcRn) binds independently to
            both sites of the IgG homodimer with identical affinity.
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Neuber,T., Frese,K., Jaehrling,J., Jager,S., Daubert,D.,
            Felderer,K., Linnemann,M., Hohne,A., Kaden,S., Kolln,J., Tiller,T.,
            Brocks,B., Ostendorp,R. and Pabst,S.
  TITLE     Characterization and screening of IgG binding to the neonatal Fc
            receptor
  JOURNAL   MAbs 6 (4), 928-942 (2014)
   PUBMED   24802048
  REMARK    GeneRIF: Characterization and screening of IgG binding to the
            neonatal Fc receptor.
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Kliwinski,C., Cooper,P.R., Perkinson,R., Mabus,J.R., Tam,S.H.,
            Wilkinson,T.M., Giles-Komar,J., Scallon,B., Powers,G.D. and
            Hornby,P.J.
  TITLE     Contribution of FcRn binding to intestinal uptake of IgG in
            suckling rat pups and human FcRn-transgenic mice
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 304 (3), G262-G270 (2013)
   PUBMED   23220220
  REMARK    GeneRIF: The suckling rat pup intestine is a mechanistic model of
            FcRn-IgG-mediated transcytosis
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Vaughn,D.E. and Bjorkman,P.J.
  TITLE     Structural basis of pH-dependent antibody binding by the neonatal
            Fc receptor
  JOURNAL   Structure 6 (1), 63-73 (1998)
   PUBMED   9493268
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Story,C.M., Mikulska,J.E. and Simister,N.E.
  TITLE     A major histocompatibility complex class I-like Fc receptor cloned
            from human placenta: possible role in transfer of immunoglobulin G
            from mother to fetus
  JOURNAL   J Exp Med 180 (6), 2377-2381 (1994)
   PUBMED   7964511
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Burmeister,W.P., Huber,A.H. and Bjorkman,P.J.
  TITLE     Crystal structure of the complex of rat neonatal Fc receptor with
            Fc
  JOURNAL   Nature 372 (6504), 379-383 (1994)
   PUBMED   7969498
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Simister,N.E. and Mostov,K.E.
  TITLE     An Fc receptor structurally related to MHC class I antigens
  JOURNAL   Nature 337 (6203), 184-187 (1989)
   PUBMED   2911353
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Simister,N.E. and Mostov,K.E.
  TITLE     Cloning and expression of the neonatal rat intestinal Fc receptor,
            a major histocompatibility complex class I antigen homolog
  JOURNAL   Cold Spring Harb Symp Quant Biol 54 Pt 1, 571-580 (1989)
   PUBMED   2534798
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M35495.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M35495.1, SRR8487227.114136.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..366
                     /product="IgG receptor FcRn large subunit p51 precursor"
                     /note="neonatal Fc receptor; igG receptor FcRn large
                     subunit p51; igG Fc fragment receptor transporter alpha
                     chain; Fc fragment immunoglobulin G receptor; Fc receptor,
                     IgG, alpha chain transporter; Fc fragment of IgG,
                     receptor, transporter, alpha; Fc fragment of IgG receptor
                     and transporter"
                     /calculated_mol_wt=37833
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2354
     mat_peptide     23..366
                     /product="IgG receptor FcRn large subunit p51"
                     /calculated_mol_wt=37833
     Region          23..111
                     /region_name="Alpha-1.
                     /evidence=ECO:0000269|PubMed:7969498,
                     ECO:0000269|PubMed:9493268, ECO:0007744|PDB:1FRT,
                     ECO:0007744|PDB:3FRU"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Region          25..198
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; pfam00129"
                     /db_xref="CDD:395078"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Region          112..201
                     /region_name="Alpha-2.
                     /evidence=ECO:0000269|PubMed:7969498,
                     ECO:0000269|PubMed:9493268, ECO:0007744|PDB:1FRT,
                     ECO:0007744|PDB:3FRU"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Site            150
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Region          199..291
                     /region_name="IgC1_MHC-like_FcRn"
                     /note="immunoglobulin domain of neonatal Fc receptor,
                     major histocompatibility complex (MHC)-like; member of the
                     C1-set of Ig superfamily (IgSF) domains; cd21011"
                     /db_xref="CDD:409602"
     Region          202..291
                     /region_name="Alpha-3.
                     /evidence=ECO:0000269|PubMed:7969498,
                     ECO:0000269|PubMed:9493268, ECO:0007744|PDB:1FRT,
                     ECO:0007744|PDB:3FRU"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Region          203..211
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409602"
     Site            order(207..210,219,221,223,225,258..261,263,265..266)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409602"
     Region          219..228
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409602"
     Region          232..238
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409602"
     Region          240..243
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409602"
     Region          245..253
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409602"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Region          258..266
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409602"
     Region          273..280
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409602"
     Region          287..290
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409602"
     Region          293..298
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Site            299..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55899; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Region          344..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     CDS             1..366
                     /gene="Fcgrt"
                     /gene_synonym="FcRn"
                     /coded_by="NM_033351.2:203..1303"
                     /db_xref="GeneID:29558"
                     /db_xref="RGD:61811"
ORIGIN      
        1 mgmsqpgvll slllvllpqt wgaeprlplm yhlaavsdls tglpsfwatg wlgaqqylty
       61 nnlrqeadpc gawiwenqvs wywekettdl kskeqlflea irtlenqing tftlqgllgc
      121 elapdnsslp tavfalngee fmrfnprtgn wsgewpetdi vgnlwmkqpe aarkesefll
      181 tscperllgh lergrqnlew keppsmrlka rpgnsgssvl tcaafsfypp elkfrflrng
      241 lasgsgncst gpngdgsfha wsllevkrgd ehhyqcqveh eglaqpltvd ldsparssvp
      301 vvgiilglll vvvaiaggvl lwnrmrsglp apwlslsgdd sgdllpggnl ppeaepqgvn
      361 afpats
//
