[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Placenta; DOI=10.1084/jem.180.6.2377; PubMed=7964511 [NCBI, ExPASy, EBI, Israel, Japan] Story C.M., Mikulska J., Simister N.E.; "A major histocompatibility complex class I-like Fc receptor cloned from human placenta: possible role in transfer of immunoglobulin G from mother to fetus."; J. Exp. Med. 180:2377-2381(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tiwari B., Junghans R.P.; "Partial sequence of the human fcgrt gene and its 5' upstream region."; Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1046/j.1365-2370.2000.00225.x; PubMed=10998088 [NCBI, ExPASy, EBI, Israel, Japan] Mikulska J.E., Pablo L., Canel J., Simister N.E.; "Cloning and analysis of the gene encoding the human neonatal Fc receptor."; Eur. J. Immunogenet. 27:231-240(2000).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	PROTEIN SEQUENCE OF 24-38. DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Z., Henzel W.J.; "Signal peptide prediction based on analysis of experimentally verified cleavage sites."; Protein Sci. 13:2819-2824(2004).
[6]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-290. DOI=10.1021/bi000749m; PubMed=10933786 [NCBI, ExPASy, EBI, Israel, Japan] West A.P. Jr., Bjorkman P.J.; "Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor."; Biochemistry 39:9698-9708(2000).

Comments

FUNCTION: Binds to the Fc region of monomeric immunoglobulins gamma. Mediates the uptake of IgG from milk. Possible role in transfer of immunoglobulin G from mother to fetus.
SUBUNIT: 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).
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein (By similarity).
SIMILARITY: Belongs to the immunoglobulin superfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U12255; AAA58958.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF220542; AAF72596.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF200220; AAG31421.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF200219; AAG31421.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008734; AAH08734.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I38720; I38720.

NP_004098.1; -.

3D structure databases

PDB

1EXU; X-ray; 2.70 A; A=24-290.

[ExPASy / RCSB / EBI]

PDBsum

1EXU; -.

ModBase

P55899.

Protein-protein interaction databases

DIP

DIP:6165N; -.

Organism-specific databases

HIX0015331; -.

HGNC:3621; FCGRT.

HPA012122; -.
HPA015130; -.

MIM

601437; gene. [NCBI / EBI]

PharmGKB

PA28067; -.

GeneCards

P55899.

Gene expression databases

ArrayExpress

P55899; -.

CleanEx

HS_FCGRT; -.

GermOnline

ENSG00000104870; Homo sapiens.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0042612;	Cellular component: MHC class I protein complex (inferred from electronic annotation from InterPro).
GO:0019864;	Molecular function: IgG binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004872;	Molecular function: receptor activity (traceable author statement from ProtInc).
GO:0019882;	Biological process: antigen processing and presentation (inferred from electronic annotation from InterPro).
GO:0007565;	Biological process: female pregnancy (traceable author statement from ProtInc).
GO:0006955;	Biological process: immune response (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR003006; Ig/MHC_CS.
IPR003597; Ig_C1-set.
IPR011161; MHC_I-like_Ag-recog.
IPR001039; MHC_I_a_a1/a2.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.10; Ig-like_fold; 1.
G3DSA:3.30.500.10; MHC_I-like_Ag-recog; 1.

Pfam

PF07654; C1-set; 1.
PF00129; MHC_I; 1.
Pfam graphical view of domain structure.

SMART

SM00407; IGc1; 1.
SMART graphical view of domain structure.

PROSITE

PS50835; IG_LIKE; 1.
PS00290; IG_MHC; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSG00000104870; Homo sapiens. [Contig view]

GeneID

2217; -.

KEGG

hsa:2217; -.

Phylogenomic databases

HOGENOM

P55899; -.

HOVERGEN

P55899; -.

Other

NextBio

8991; -.

SOURCE

FCGRT; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell membrane; Direct protein sequencing; Glycoprotein; IgG-binding protein; Immunoglobulin domain; Membrane; Receptor; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 365`	`342`	`IgG receptor FcRn large subunit p51.`	`PRO_0000015157`
`TOPO_DOM`	`24 297`	`274`	`Extracellular (Potential).`
`TRANSMEM`	`298 321`	`24`	`Potential.`
`TOPO_DOM`	`322 365`	`44`	`Cytoplasmic (Potential).`
`REGION`	`24 110`	`87`	`Alpha-1.`
`REGION`	`111 200`	`90`	`Alpha-2.`
`REGION`	`201 290`	`90`	`Alpha-3.`
`REGION`	`291 297`	`7`	`Connecting peptide.`
`CARBOHYD`	`125 125`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`119 182`
`DISULFID`	`221 275`
`CONFLICT`	`101 103`		`Missing (in Ref. 3; AAG31421).`
`CONFLICT`	`201 201`		`E -> G (in Ref. 2; AAF72596).`
`STRAND`	`29 39`	`11`
`STRAND`	`46 53`	`8`
`STRAND`	`56 62`	`7`
`TURN`	`63 65`	`3`
`HELIX`	`85 103`	`19`
`STRAND`	`112 121`	`10`
`STRAND`	`127 135`	`9`
`STRAND`	`138 144`	`7`
`TURN`	`145 148`	`4`
`STRAND`	`149 151`	`3`
`HELIX`	`155 165`	`11`
`HELIX`	`170 179`	`10`
`HELIX`	`181 191`	`11`
`HELIX`	`194 197`	`4`
`STRAND`	`204 211`	`8`
`STRAND`	`216 229`	`14`
`STRAND`	`231 237`	`7`
`STRAND`	`249 251`	`3`
`STRAND`	`257 266`	`10`
`HELIX`	`270 272`	`3`
`STRAND`	`273 279`	`7`
`STRAND`	`282 284`	`3`
`STRAND`	`286 289`	`4`

Sequence information

Length: 365 AA [This is the length of the unprocessed precursor]

Molecular weight: 39743 Da [This is the MW of the unprocessed precursor]

CRC64: C886C6A1F66A0D89 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGVPRPQPWA LGLLLFLLPG SLGAESHLSL LYHLTAVSSP APGTPAFWVS GWLGPQQYLS 

        70         80         90        100        110        120 
YNSLRGEAEP CGAWVWENQV SWYWEKETTD LRIKEKLFLE AFKALGGKGP YTLQGLLGCE 

       130        140        150        160        170        180 
LGPDNTSVPT AKFALNGEEF MNFDLKQGTW GGDWPEALAI SQRWQQQDKA ANKELTFLLF 

       190        200        210        220        230        240 
SCPHRLREHL ERGRGNLEWK EPPSMRLKAR PSSPGFSVLT CSAFSFYPPE LQLRFLRNGL 

       250        260        270        280        290        300 
AAGTGQGDFG PNSDGSFHAS SSLTVKSGDE HHYCCIVQHA GLAQPLRVEL ESPAKSSVLV 

       310        320        330        340        350        360 
VGIVIGVLLL TAAAVGGALL WRRMRSGLPA PWISLRGDDT GVLLPTPGEA QDADLKDVNV 


IPATA

P55899 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools