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Protein

IgG receptor FcRn large subunit p51

Gene

FCGRT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the Fc region of monomeric immunoglobulins gamma (PubMed:7964511, PubMed:10933786). Mediates the selective uptake of IgG from milk and helps newborn animals to acquire passive immunity. IgG in the milk is bound at the apical surface of the intestinal epithelium. The resultant FcRn-IgG complexes are transcytosed across the intestinal epithelium and IgG is released from FcRn into blood or tissue fluids (By similarity). Possible role in transfer of immunoglobulin G from mother to fetus (PubMed:7964511).By similarity2 Publications

GO - Molecular functioni

  • beta-2-microglobulin binding Source: GO_Central
  • IgG binding Source: UniProtKB
  • IgG receptor activity Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionIgG-binding protein, Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
IgG receptor FcRn large subunit p51
Short name:
FcRn
Alternative name(s):
IgG Fc fragment receptor transporter alpha chain
Neonatal Fc receptor
Gene namesi
Name:FCGRT
Synonyms:FCRN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000104870.12.
HGNCiHGNC:3621. FCGRT.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 297ExtracellularSequence analysisAdd BLAST274
Transmembranei298 – 321HelicalSequence analysisAdd BLAST24
Topological domaini322 – 365CytoplasmicSequence analysisAdd BLAST44

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2217.
OpenTargetsiENSG00000104870.
PharmGKBiPA28067.

Chemistry databases

ChEMBLiCHEMBL5966.

Polymorphism and mutation databases

BioMutaiFCGRT.
DMDMi2497331.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000001515724 – 365IgG receptor FcRn large subunit p511 PublicationAdd BLAST342

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi119 ↔ 182Combined sources1 Publication
Glycosylationi125N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi221 ↔ 275Combined sources1 Publication
Modified residuei334PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP55899.
MaxQBiP55899.
PaxDbiP55899.
PeptideAtlasiP55899.
PRIDEiP55899.

PTM databases

iPTMnetiP55899.
PhosphoSitePlusiP55899.

Expressioni

Tissue specificityi

Expressed in full-term placenta, heart, lung, liver, muscle, kidney, pancreas, and both fetal and adult small intestine.1 Publication

Gene expression databases

BgeeiENSG00000104870.
CleanExiHS_FCGRT.
ExpressionAtlasiP55899. baseline and differential.
GenevisibleiP55899. HS.

Organism-specific databases

HPAiHPA012122.
HPA015130.

Interactioni

Subunit structurei

FcRn complex consist of two subunits: p51, and p14 which is equivalent to beta-2-microglobulin. It forms an MHC class I-like heterodimer.By similarity

GO - Molecular functioni

  • beta-2-microglobulin binding Source: GO_Central
  • IgG binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108511. 64 interactors.
DIPiDIP-6165N.
IntActiP55899. 4 interactors.
MINTiMINT-5002634.
STRINGi9606.ENSP00000221466.

Chemistry databases

BindingDBiP55899.

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 39Combined sources11
Beta strandi46 – 53Combined sources8
Beta strandi56 – 62Combined sources7
Turni63 – 65Combined sources3
Helixi72 – 76Combined sources5
Helixi83 – 105Combined sources23
Beta strandi107 – 109Combined sources3
Beta strandi112 – 121Combined sources10
Beta strandi123 – 125Combined sources3
Beta strandi127 – 135Combined sources9
Beta strandi138 – 144Combined sources7
Turni145 – 148Combined sources4
Beta strandi149 – 151Combined sources3
Helixi155 – 166Combined sources12
Helixi170 – 179Combined sources10
Helixi181 – 192Combined sources12
Helixi194 – 197Combined sources4
Beta strandi204 – 213Combined sources10
Beta strandi216 – 229Combined sources14
Beta strandi231 – 237Combined sources7
Beta strandi240 – 243Combined sources4
Beta strandi246 – 251Combined sources6
Beta strandi253 – 255Combined sources3
Beta strandi257 – 266Combined sources10
Helixi270 – 272Combined sources3
Beta strandi273 – 279Combined sources7
Beta strandi282 – 284Combined sources3
Beta strandi286 – 288Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EXUX-ray2.70A24-290[»]
3M17X-ray2.60A/C/E/G24-290[»]
3M1BX-ray3.10A/C/E/G24-290[»]
4K71X-ray2.40B/E24-297[»]
4N0FX-ray3.02A/E/H/K27-297[»]
4N0UX-ray3.80A27-290[»]
5BJTX-ray3.20A/C/E/G24-290[»]
5BXFX-ray2.85A/C1-290[»]
ProteinModelPortaliP55899.
SMRiP55899.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55899.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini202 – 289Ig-like C1-typePROSITE-ProRule annotationAdd BLAST88

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 110Alpha-1Combined sources1 PublicationAdd BLAST87
Regioni111 – 200Alpha-2Combined sources1 PublicationAdd BLAST90
Regioni201 – 290Alpha-3Combined sources1 PublicationAdd BLAST90
Regioni291 – 297Connecting peptide7

Sequence similaritiesi

Belongs to the immunoglobulin superfamily.Curated

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPRY. Eukaryota.
ENOG4111C4R. LUCA.
GeneTreeiENSGT00740000114936.
HOGENOMiHOG000112560.
HOVERGENiHBG100415.
InParanoidiP55899.
OMAiPWISLRG.
OrthoDBiEOG091G0KJB.
PhylomeDBiP55899.
TreeFamiTF336617.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.30.500.10. 1 hit.
InterProiView protein in InterPro
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003597. Ig_C1-set.
IPR011161. MHC_I-like_Ag-recog.
IPR011162. MHC_I/II-like_Ag-recog.
PfamiView protein in Pfam
PF07654. C1-set. 1 hit.
PF00129. MHC_I. 1 hit.
SMARTiView protein in SMART
SM00407. IGc1. 1 hit.
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. SSF54452. 1 hit.
PROSITEiView protein in PROSITE
PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55899-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVPRPQPWA LGLLLFLLPG SLGAESHLSL LYHLTAVSSP APGTPAFWVS
60 70 80 90 100
GWLGPQQYLS YNSLRGEAEP CGAWVWENQV SWYWEKETTD LRIKEKLFLE
110 120 130 140 150
AFKALGGKGP YTLQGLLGCE LGPDNTSVPT AKFALNGEEF MNFDLKQGTW
160 170 180 190 200
GGDWPEALAI SQRWQQQDKA ANKELTFLLF SCPHRLREHL ERGRGNLEWK
210 220 230 240 250
EPPSMRLKAR PSSPGFSVLT CSAFSFYPPE LQLRFLRNGL AAGTGQGDFG
260 270 280 290 300
PNSDGSFHAS SSLTVKSGDE HHYCCIVQHA GLAQPLRVEL ESPAKSSVLV
310 320 330 340 350
VGIVIGVLLL TAAAVGGALL WRRMRSGLPA PWISLRGDDT GVLLPTPGEA
360
QDADLKDVNV IPATA
Length:365
Mass (Da):39,743
Last modified:November 1, 1997 - v1
Checksum:iC886C6A1F66A0D89
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti101 – 103Missing in AAG31421 (PubMed:10998088).Curated3
Sequence conflicti201E → G in AAF72596 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12255 mRNA. Translation: AAA58958.1.
AF220542 Genomic DNA. Translation: AAF72596.1.
AF200220, AF200219 Genomic DNA. Translation: AAG31421.1.
BX647163 mRNA. Translation: CAI46032.1.
CH471177 Genomic DNA. Translation: EAW52498.1.
BC008734 mRNA. Translation: AAH08734.1.
CCDSiCCDS12770.1.
PIRiI38720.
RefSeqiNP_001129491.1. NM_001136019.2.
NP_004098.1. NM_004107.4.
UniGeneiHs.111903.

Genome annotation databases

EnsembliENST00000221466; ENSP00000221466; ENSG00000104870.
ENST00000426395; ENSP00000410798; ENSG00000104870.
GeneIDi2217.
KEGGihsa:2217.
UCSCiuc002poe.3. human.

Similar proteinsi

Entry informationi

Entry nameiFCGRN_HUMAN
AccessioniPrimary (citable) accession number: P55899
Secondary accession number(s): Q5HYM5, Q9HBV7, Q9NZ19
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 27, 2017
This is version 152 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families