FCGRN_MACFA
ID FCGRN_MACFA Reviewed; 365 AA.
AC Q8SPV9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 89.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Namenuk A.K., Hong K., Meng Y.G., Shields R.L., Cromwell M.E.M.,
RA Presta L.G.;
RT "Binding of human IgG to cynomolgus FcR.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AF485818; AAL92101.1; -; mRNA.
DR RefSeq; NP_001271480.1; NM_001284551.1.
DR RefSeq; XP_015296443.1; XM_015440957.1.
DR RefSeq; XP_015296444.1; XM_015440958.1.
DR AlphaFoldDB; Q8SPV9; -.
DR SMR; Q8SPV9; -.
DR STRING; 9541.XP_005589978.1; -.
DR ABCD; Q8SPV9; 1 sequenced antibody.
DR GeneID; 102128913; -.
DR KEGG; mcf:102128913; -.
DR CTD; 2217; -.
DR VEuPathDB; HostDB:ENSMFAG00000038710; -.
DR eggNOG; ENOG502RTZ5; Eukaryota.
DR OMA; EGGFGPN; -.
DR Proteomes; UP000233100; Chromosome 19.
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 GO; GO:0019864; F:IgG binding; IEA:UniProtKB-KW.
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; IgG-binding protein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..365
FT /note="IgG receptor FcRn large subunit p51"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015158"
FT TOPO_DOM 24..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 24..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 MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55899"
FT CARBOHYD 125
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"
SQ SEQUENCE 365 AA; 39877 MW; 809EFF1BD432A5DB CRC64;
MRVPRPQPWA LGLLLFLLPG SLGAESHLSL LYHLTAVSSP APGTPAFWVS GWLGPQQYLS
YDSLRGQAEP CGAWVWENQV SWYWEKETTD LRIKEKLFLE AFKALGGKGP YTLQGLLGCE
LSPDNTSVPT AKFALNGEEF MNFDLKQGTW GGDWPEALAI SQRWQQQDKA ANKELTFLLF
SCPHRLREHL ERGRGNLEWK EPPSMRLKAR PGNPGFSVLT CSAFSFYPPE LQLRFLRNGM
AAGTGQGDFG PNSDGSFHAS SSLTVKSGDE HHYCCIVQHA GLAQPLRVEL ETPAKSSVLV
VGIVIGVLLL TAAAVGGALL WRRMRSGLPA PWISLRGDDT GSLLPTPGEA QDADSKDINV
IPATA
