FCGRN_CAMDR
ID FCGRN_CAMDR Reviewed; 355 AA.
AC Q2KN22;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=IgG receptor FcRn large subunit p51 {ECO:0000305};
DE Short=FcRn {ECO:0000303|PubMed:16690125};
DE AltName: Full=IgG Fc fragment receptor transporter alpha chain {ECO:0000305};
DE AltName: Full=Neonatal Fc receptor {ECO:0000303|PubMed:16690125};
DE Flags: Precursor;
GN Name=FCGRT {ECO:0000305}; Synonyms=Fcrn {ECO:0000303|PubMed:16690125};
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838 {ECO:0000312|EMBL:AAX82484.1};
RN [1] {ECO:0000312|EMBL:AAX82484.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND PHYLOGENETIC ANALYSIS.
RX PubMed=16690125; DOI=10.1016/j.dci.2006.02.006;
RA Kacskovics I., Mayer B., Kis Z., Frenyo L.V., Zhao Y., Muyldermans S.,
RA Hammarstrom L.;
RT "Cloning and characterization of the dromedary (Camelus dromedarius)
RT neonatal Fc receptor (drFcRn).";
RL Dev. Comp. Immunol. 30:1203-1215(2006).
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. IgG
CC in the milk is bound at the apical surface of the intestinal
CC epithelium. The resultant FcRn-IgG complexes are transcytosed across
CC the intestinal epithelium and IgG is released from FcRn into blood or
CC tissue fluids. 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. {ECO:0000250|UniProtKB:P13599,
CC ECO:0000250|UniProtKB:P55899}.
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 (By similarity). Interacts with albumin/ALB; this
CC interaction regulates ALB homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:P13599, 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: Expressed in liver and mammary gland of non-
CC lactating animals. Expressed in hepatocytes and in epithelial cells of
CC portal bile ductuli. Not expressed in the brances of portal veins or
CC hepatic arteries. Expressed in the epithelial cells of the acini and
CC ducti in the mammary gland with expression emphasized at the apical
CC side. Not expressed in blood vessels of mammary gland.
CC {ECO:0000269|PubMed:16690125}.
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; AY894681; AAX82484.1; -; mRNA.
DR RefSeq; NP_001290499.1; NM_001303570.1.
DR AlphaFoldDB; Q2KN22; -.
DR SMR; Q2KN22; -.
DR STRING; 9838.ENSCDRP00005010759; -.
DR GeneID; 105100203; -.
DR KEGG; cdk:105100203; -.
DR CTD; 2217; -.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endosome; Glycoprotein;
KW Immunoglobulin domain; Membrane; Receptor; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..355
FT /note="IgG receptor FcRn large subunit p51"
FT /evidence="ECO:0000255"
FT /id="PRO_5004211833"
FT TOPO_DOM 25..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 203..292
FT /note="Ig-like C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 25..111
FT /note="Alpha-1"
FT /evidence="ECO:0000250|UniProtKB:P13599"
FT REGION 112..201
FT /note="Alpha-2"
FT /evidence="ECO:0000250|UniProtKB:P13599"
FT REGION 202..291
FT /note="Alpha-3"
FT /evidence="ECO:0000250|UniProtKB:P13599"
FT REGION 293..298
FT /note="Connecting peptide"
FT /evidence="ECO:0000305"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 222..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 355 AA; 39398 MW; 98D648D5AEB40922 CRC64;
MRVPRSQPWG LALLLLLLPG TLRAAESHRS LLYHFTAVSN PASGTPAFSL SGWLGPQQYL
SYNNLRAQAE PYGAWVWESQ VSWYWEKETT DLRDKEKLFL EALKVFGDRD SYTLQGLLGC
ELGPDNVSVP MAKYALNGEE FMEFDPKLGI WDGDWPEART IGIKWMKHPE AVNKEKTFLL
YSCPHRLLGH LERGRGNLEW KEPPSMRLKA RPGNPGFSVL TCSAFSFYPP ELQLRFLRNG
LAAGSGEGDV VPNGDGSFYA WSSLTVKSGD EHQYRCWVQH VGPAQPLTVE LESPAKSSVP
VIGISIGFLL LMTVAAGGAL LWRRRKGLPA PWIAFRGDDI GALLPTPGLS KDAES
