FCGRN_MOUSE
ID FCGRN_MOUSE Reviewed; 365 AA.
AC Q61559; Q9QUR0; Q9R2A5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=IgG receptor FcRn large subunit p51;
DE Short=FcRn;
DE AltName: Full=IgG Fc fragment receptor transporter alpha chain;
DE AltName: Full=Neonatal Fc receptor;
DE Flags: Precursor;
GN Name=Fcgrt; Synonyms=Fcrn;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=A/J, AKR/J, BALB/cJ, C3H/HeJ, DBA/2J, P/J, and TW75;
RC TISSUE=Small intestine;
RX PubMed=7538537;
RA Kandil E., Noguchi M., Ishibashi T., Kasahara M.;
RT "Structural and phylogenetic analysis of the MHC class I-like Fc receptor
RT gene.";
RL J. Immunol. 154:5907-5918(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=FVB/N; TISSUE=Small intestine;
RX PubMed=7504013;
RA Ahouse J.J., Hagerman C.L., Mittal P., Gilbert D.J., Copeland N.G.,
RA Jenkins N.A., Simister N.E.;
RT "Mouse MHC class I-like Fc receptor encoded outside the MHC.";
RL J. Immunol. 151:6076-6088(1993).
RN [3]
RP PROTEIN SEQUENCE OF 167-173, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cell surface receptor that transfers passive humoral immunity
CC from the mother to the newborn. Binds to the Fc region of monomeric
CC immunoglobulin gamma and mediates its selective uptake from milk
CC (PubMed:7504013). IgG in the milk is bound at the apical surface of the
CC intestinal epithelium. The resultant FcRn-IgG complexes are
CC transcytosed across the intestinal epithelium and IgG is released from
CC FcRn into blood or tissue fluids. Throughout life, contributes to
CC effective humoral immunity by recycling IgG and extending its half-life
CC in the circulation. Mechanistically, monomeric IgG binding to FcRn in
CC acidic endosomes of endothelial and hematopoietic cells recycles IgG to
CC the cell surface where it is released into the circulation. In addition
CC of IgG, regulates homeostasis of the other most abundant circulating
CC protein albumin/ALB. {ECO:0000250|UniProtKB:P55899,
CC ECO:0000269|PubMed:7504013}.
CC -!- SUBUNIT: FcRn complex consists of two subunits: p51, and p14 which is
CC equivalent to beta-2-microglobulin. It forms an MHC class I-like
CC heterodimer. Interacts with albumin/ALB; this interaction regulates ALB
CC homeostasis. {ECO:0000250|UniProtKB:P13599,
CC ECO:0000250|UniProtKB:P55899}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13599};
CC Single-pass type I membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:P55899}.
CC -!- TISSUE SPECIFICITY: Intestinal epithelium of suckling rodents.
CC Expressed in neonatal intestine and fetal yolk sac.
CC {ECO:0000269|PubMed:7504013}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D37874; BAA07111.1; -; mRNA.
DR EMBL; D37873; BAA07110.1; -; Genomic_DNA.
DR EMBL; L17022; AAA16904.1; -; mRNA.
DR EMBL; D37903; BAA07134.1; -; Genomic_DNA.
DR EMBL; D37905; BAA07135.1; -; Genomic_DNA.
DR EMBL; D37907; BAA07136.1; -; Genomic_DNA.
DR EMBL; D37909; BAA07137.1; -; Genomic_DNA.
DR EMBL; D37911; BAA07138.1; -; Genomic_DNA.
DR EMBL; D37913; BAA07139.1; -; Genomic_DNA.
DR CCDS; CCDS52243.1; -.
DR PIR; I56197; I56197.
DR RefSeq; NP_034319.2; NM_010189.3.
DR AlphaFoldDB; Q61559; -.
DR SMR; Q61559; -.
DR STRING; 10090.ENSMUSP00000003512; -.
DR GlyGen; Q61559; 4 sites.
DR PhosphoSitePlus; Q61559; -.
DR jPOST; Q61559; -.
DR MaxQB; Q61559; -.
DR PaxDb; Q61559; -.
DR PeptideAtlas; Q61559; -.
DR PRIDE; Q61559; -.
DR ProteomicsDB; 272976; -.
DR ABCD; Q61559; 6 sequenced antibodies.
DR Antibodypedia; 1522; 314 antibodies from 31 providers.
DR DNASU; 14132; -.
DR Ensembl; ENSMUST00000003512; ENSMUSP00000003512; ENSMUSG00000003420.
DR GeneID; 14132; -.
DR KEGG; mmu:14132; -.
DR UCSC; uc009gtf.2; mouse.
DR CTD; 2217; -.
DR MGI; MGI:103017; Fcgrt.
DR VEuPathDB; HostDB:ENSMUSG00000003420; -.
DR eggNOG; ENOG502RTZ5; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_7_0_1; -.
DR InParanoid; Q61559; -.
DR PhylomeDB; Q61559; -.
DR TreeFam; TF336617; -.
DR BioGRID-ORCS; 14132; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Fcgrt; mouse.
DR PRO; PR:Q61559; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61559; protein.
DR Bgee; ENSMUSG00000003420; Expressed in stroma of bone marrow and 235 other tissues.
DR ExpressionAtlas; Q61559; baseline and differential.
DR Genevisible; Q61559; MM.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030881; F:beta-2-microglobulin binding; ISO:MGI.
DR GO; GO:0019864; F:IgG binding; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Endosome;
KW Glycoprotein; IgG-binding protein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:P55899"
FT CHAIN 22..365
FT /note="IgG receptor FcRn large subunit p51"
FT /evidence="ECO:0000250|UniProtKB:P55899"
FT /id="PRO_0000015159"
FT TOPO_DOM 22..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 202..289
FT /note="Ig-like C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 22..110
FT /note="Alpha-1"
FT /evidence="ECO:0000250|UniProtKB:P13599"
FT REGION 111..200
FT /note="Alpha-2"
FT /evidence="ECO:0000250|UniProtKB:P13599"
FT REGION 201..290
FT /note="Alpha-3"
FT /evidence="ECO:0000250|UniProtKB:P13599"
FT REGION 291..297
FT /note="Connecting peptide"
FT REGION 343..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55899"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 119..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 221..275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 73
FT /note="M -> V (in strain: FVB/N)"
FT VARIANT 111
FT /note="Y -> F (in strain: P/J)"
SQ SEQUENCE 365 AA; 40093 MW; 0A2290A54507E0C4 CRC64;
MGMPLPWALS LLLVLLPQTW GSETRPPLMY HLTAVSNPST GLPSFWATGW LGPQQYLTYN
SLRQEADPCG AWMWENQVSW YWEKETTDLK SKEQLFLEAL KTLEKILNGT YTLQGLLGCE
LASDNSSVPT AVFALNGEEF MKFNPRIGNW TGEWPETEIV ANLWMKQPDA ARKESEFLLN
SCPERLLGHL ERGRRNLEWK EPPSMRLKAR PGNSGSSVLT CAAFSFYPPE LKFRFLRNGL
ASGSGNCSTG PNGDGSFHAW SLLEVKRGDE HHYQCQVEHE GLAQPLTVDL DSSARSSVPV
VGIVLGLLLV VVAIAGGVLL WGRMRSGLPA PWLSLSGDDS GDLLPGGNLP PEAEPQGANA
FPATS
