FCGRN_RAT
ID FCGRN_RAT Reviewed; 366 AA.
AC P13599;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 177.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-39; 176-185 AND 282-291,
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Epithelium {ECO:0000303|PubMed:2911353};
RX PubMed=2911353; DOI=10.1038/337184a0;
RA Simister N.E., Mostov K.E.;
RT "An Fc receptor structurally related to MHC class I antigens.";
RL Nature 337:184-187(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epithelium;
RX PubMed=2534798; DOI=10.1101/sqb.1989.054.01.068;
RA Simister N.E., Mostov K.E.;
RT "Cloning and expression of the neonatal rat intestinal Fc receptor, a major
RT histocompatibility complex class I antigen homolog.";
RL Cold Spring Harb. Symp. Quant. Biol. 54:571-580(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=7298722; DOI=10.1083/jcb.91.1.270;
RA Abrahamson D.R., Rodewald R.;
RT "Evidence for the sorting of endocytic vesicle contents during the
RT receptor-mediated transport of IgG across the newborn rat intestine.";
RL J. Cell Biol. 91:270-280(1981).
RN [5]
RP FUNCTION.
RX PubMed=18818657; DOI=10.1038/nature07255;
RA He W., Ladinsky M.S., Huey-Tubman K.E., Jensen G.J., McIntosh J.R.,
RA Bjoerkman P.J.;
RT "FcRn-mediated antibody transport across epithelial cells revealed by
RT electron tomography.";
RL Nature 455:542-546(2008).
RN [6] {ECO:0007744|PDB:1FRT}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-291 IN COMPLEX WITH FC AND
RP BETA-2-MICROGLOBULIN, FUNCTION, AND SUBUNIT.
RX PubMed=7969498; DOI=10.1038/372379a0;
RA Burmeister W.P., Huber A.H., Bjorkman P.J.;
RT "Crystal structure of the complex of rat neonatal Fc receptor with Fc.";
RL Nature 372:379-383(1994).
RN [7] {ECO:0007744|PDB:3FRU}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-291 IN COMPLEX WITH
RP BETA-2-MICROGLOBULIN.
RX PubMed=9493268; DOI=10.1016/s0969-2126(98)00008-2;
RA Vaughn D.E., Bjorkman P.J.;
RT "Structural basis of pH-dependent antibody binding by the neonatal Fc
RT receptor.";
RL Structure 6:63-73(1998).
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:18818657, PubMed:7969498). IgG in the milk is bound at the
CC apical surface of the intestinal epithelium. The resultant FcRn-IgG
CC complexes are transcytosed across the intestinal epithelium and IgG is
CC released from FcRn into blood or tissue fluids (PubMed:7298722,
CC PubMed:18818657). Throughout life, contributes to effective humoral
CC immunity by recycling IgG and extending its half-life in the
CC circulation. Mechanistically, monomeric IgG binding to FcRn in acidic
CC endosomes of endothelial and hematopoietic cells recycles IgG to the
CC cell surface where it is released into the circulation. In addition of
CC IgG, regulates homeostasis of the other most abundant circulating
CC protein albumin/ALB (By similarity). {ECO:0000250|UniProtKB:P55899,
CC ECO:0000269|PubMed:18818657, ECO:0000269|PubMed:7298722,
CC ECO:0000269|PubMed:7969498}.
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 (PubMed:2911353, PubMed:7969498, PubMed:9493268). Interacts
CC with albumin/ALB; this interaction regulates ALB homeostasis (By
CC similarity). {ECO:0000250|UniProtKB:P55899, ECO:0000269|PubMed:2911353,
CC ECO:0000269|PubMed:7969498, ECO:0000269|PubMed:9493268}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2911353};
CC Single-pass type I membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:P55899}.
CC -!- TISSUE SPECIFICITY: Intestinal epithelium.
CC {ECO:0000269|PubMed:2911353}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; X14323; CAA32503.1; -; mRNA.
DR EMBL; M35495; AAA41611.1; -; mRNA.
DR EMBL; BC061975; AAH61975.1; -; mRNA.
DR PIR; A37374; A37374.
DR RefSeq; NP_203502.1; NM_033351.2.
DR RefSeq; XP_006229105.1; XM_006229043.2.
DR RefSeq; XP_008757565.1; XM_008759343.2.
DR PDB; 1FRT; X-ray; 4.50 A; A=23-291.
DR PDB; 1I1A; X-ray; 2.80 A; A=23-291.
DR PDB; 3FRU; X-ray; 2.20 A; A/C/E=23-291.
DR PDBsum; 1FRT; -.
DR PDBsum; 1I1A; -.
DR PDBsum; 3FRU; -.
DR AlphaFoldDB; P13599; -.
DR SMR; P13599; -.
DR IntAct; P13599; 1.
DR STRING; 10116.ENSRNOP00000027944; -.
DR GlyGen; P13599; 4 sites.
DR iPTMnet; P13599; -.
DR PhosphoSitePlus; P13599; -.
DR PaxDb; P13599; -.
DR GeneID; 29558; -.
DR KEGG; rno:29558; -.
DR UCSC; RGD:61811; rat.
DR CTD; 2217; -.
DR RGD; 61811; Fcgrt.
DR VEuPathDB; HostDB:ENSRNOG00000020583; -.
DR eggNOG; ENOG502RTZ5; Eukaryota.
DR HOGENOM; CLU_047501_7_0_1; -.
DR InParanoid; P13599; -.
DR OMA; EGGFGPN; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; P13599; -.
DR EvolutionaryTrace; P13599; -.
DR PRO; PR:P13599; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020583; Expressed in spleen and 19 other tissues.
DR Genevisible; P13599; RN.
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; IDA:RGD.
DR GO; GO:0019864; F:IgG binding; ISO:RGD.
DR GO; GO:0019770; F:IgG receptor activity; TAS:RGD.
DR GO; GO:0006959; P:humoral immune response; TAS:RGD.
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 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Endosome; Glycoprotein; IgG-binding protein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:2911353"
FT CHAIN 23..366
FT /note="IgG receptor FcRn large subunit p51"
FT /evidence="ECO:0000269|PubMed:2911353"
FT /id="PRO_0000015160"
FT TOPO_DOM 23..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 203..290
FT /note="Ig-like C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 23..111
FT /note="Alpha-1"
FT /evidence="ECO:0000269|PubMed:7969498,
FT ECO:0000269|PubMed:9493268, ECO:0007744|PDB:1FRT,
FT ECO:0007744|PDB:3FRU"
FT REGION 112..201
FT /note="Alpha-2"
FT /evidence="ECO:0000269|PubMed:7969498,
FT ECO:0000269|PubMed:9493268, ECO:0007744|PDB:1FRT,
FT ECO:0007744|PDB:3FRU"
FT REGION 202..291
FT /note="Alpha-3"
FT /evidence="ECO:0000269|PubMed:7969498,
FT ECO:0000269|PubMed:9493268, ECO:0007744|PDB:1FRT,
FT ECO:0007744|PDB:3FRU"
FT REGION 293..298
FT /note="Connecting peptide"
FT REGION 344..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55899"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 222..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:3FRU"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3FRU"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:3FRU"
FT HELIX 82..107
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1I1A"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:3FRU"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1I1A"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:3FRU"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:3FRU"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:3FRU"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 217..230
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:3FRU"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3FRU"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3FRU"
SQ SEQUENCE 366 AA; 40169 MW; 8A8BF2873A698BB5 CRC64;
MGMSQPGVLL SLLLVLLPQT WGAEPRLPLM YHLAAVSDLS TGLPSFWATG WLGAQQYLTY
NNLRQEADPC GAWIWENQVS WYWEKETTDL KSKEQLFLEA IRTLENQING TFTLQGLLGC
ELAPDNSSLP TAVFALNGEE FMRFNPRTGN WSGEWPETDI VGNLWMKQPE AARKESEFLL
TSCPERLLGH LERGRQNLEW KEPPSMRLKA RPGNSGSSVL TCAAFSFYPP ELKFRFLRNG
LASGSGNCST GPNGDGSFHA WSLLEVKRGD EHHYQCQVEH EGLAQPLTVD LDSPARSSVP
VVGIILGLLL VVVAIAGGVL LWNRMRSGLP APWLSLSGDD SGDLLPGGNL PPEAEPQGVN
AFPATS
