FCAMR_MOUSE
ID FCAMR_MOUSE Reviewed; 535 AA.
AC Q2TB54; Q2TB55; Q920L8; Q9EQT7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=High affinity immunoglobulin alpha and immunoglobulin mu Fc receptor;
DE AltName: Full=Fc alpha/mu receptor;
DE Short=mFcamR;
DE AltName: CD_antigen=CD351;
DE Flags: Precursor;
GN Name=Fcamr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-519 AND LEU-520.
RC TISSUE=T-cell;
RX PubMed=11062505; DOI=10.1038/80886;
RA Shibuya A., Sakamoto N., Shimizu Y., Shibuya K., Osawa M., Hiroyama T.,
RA Eyre H.J., Sutherland G.R., Endo Y., Fujita T., Miyabayashi T., Sakano S.,
RA Tsuji T., Nakayama E., Phillips J.H., Lanier L.L., Nakauchi H.;
RT "Fc alpha/mu receptor mediates endocytosis of IgM-coated microbes.";
RL Nat. Immunol. 1:441-446(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-535 (ISOFORM 1).
RX PubMed=11797105; DOI=10.1007/s00251-001-0375-y;
RA Shimizu Y., Honda S., Yotsumoto K., Tahara-Hanaoka S., Eyre H.J.,
RA Sutherland G.R., Endo Y., Shibuya K., Koyama A., Nakauchi H., Shibuya A.;
RT "Fc(alpha)/mu receptor is a single gene-family member closely related to
RT polymeric immunoglobulin receptor encoded on Chromosome 1.";
RL Immunogenetics 53:709-711(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12527391; DOI=10.1016/s0304-3940(02)01312-5;
RA Nakahara J., Seiwa C., Shibuya A., Aiso S., Asou H.;
RT "Expression of Fc receptor for immunoglobulin M in oligodendrocytes and
RT myelin of mouse central nervous system.";
RL Neurosci. Lett. 337:73-76(2003).
RN [5]
RP CHARACTERIZATION.
RX PubMed=16681999; DOI=10.1016/j.bbrc.2006.04.084;
RA Cho Y., Usui K., Honda S., Tahara-Hanaoka S., Shibuya K., Shibuya A.;
RT "Molecular characteristics of IgA and IgM Fc binding to the Fcalpha/muR.";
RL Biochem. Biophys. Res. Commun. 345:474-478(2006).
CC -!- FUNCTION: Functions as a receptor for the Fc fragment of IgA and IgM.
CC Binds IgA and IgM with high affinity and mediates their endocytosis.
CC May function in the immune response to microbes mediated by IgA and
CC IgM. {ECO:0000269|PubMed:11062505}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11062505};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:11062505}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2TB54-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2TB54-2; Sequence=VSP_033233;
CC -!- TISSUE SPECIFICITY: Expressed in several tissues including thymus,
CC spleen, liver, kidney, small and large intestine, testis and placenta.
CC Expressed by oligodendrocytes, B-cells and macrophages but not
CC granulocytes, T-cells or NK cells (at protein level).
CC {ECO:0000269|PubMed:11062505, ECO:0000269|PubMed:12527391}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; AB048834; BAB17312.1; -; mRNA.
DR EMBL; BC110549; AAI10550.1; -; mRNA.
DR EMBL; BC110550; AAI10551.1; -; mRNA.
DR EMBL; AB071978; BAB71750.1; -; Genomic_DNA.
DR CCDS; CCDS15259.1; -. [Q2TB54-1]
DR CCDS; CCDS48353.1; -. [Q2TB54-2]
DR RefSeq; NP_001164103.1; NM_001170632.1. [Q2TB54-2]
DR RefSeq; NP_659209.2; NM_144960.2. [Q2TB54-1]
DR RefSeq; XP_006529850.1; XM_006529787.3. [Q2TB54-1]
DR RefSeq; XP_017177414.1; XM_017321925.1. [Q2TB54-1]
DR AlphaFoldDB; Q2TB54; -.
DR SMR; Q2TB54; -.
DR STRING; 10090.ENSMUSP00000108096; -.
DR GlyGen; Q2TB54; 1 site.
DR iPTMnet; Q2TB54; -.
DR PhosphoSitePlus; Q2TB54; -.
DR PaxDb; Q2TB54; -.
DR PRIDE; Q2TB54; -.
DR ProteomicsDB; 267362; -. [Q2TB54-1]
DR ProteomicsDB; 267363; -. [Q2TB54-2]
DR Antibodypedia; 57057; 51 antibodies from 17 providers.
DR DNASU; 64435; -.
DR Ensembl; ENSMUST00000027670; ENSMUSP00000027670; ENSMUSG00000026415. [Q2TB54-1]
DR Ensembl; ENSMUST00000112477; ENSMUSP00000108096; ENSMUSG00000026415. [Q2TB54-2]
DR GeneID; 64435; -.
DR KEGG; mmu:64435; -.
DR UCSC; uc007cmk.1; mouse. [Q2TB54-1]
DR UCSC; uc007cml.1; mouse. [Q2TB54-2]
DR CTD; 83953; -.
DR MGI; MGI:1927803; Fcamr.
DR VEuPathDB; HostDB:ENSMUSG00000026415; -.
DR eggNOG; ENOG502SNZE; Eukaryota.
DR GeneTree; ENSGT00950000182977; -.
DR HOGENOM; CLU_041432_0_0_1; -.
DR InParanoid; Q2TB54; -.
DR OMA; WEILPQA; -.
DR OrthoDB; 593994at2759; -.
DR PhylomeDB; Q2TB54; -.
DR TreeFam; TF334441; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 64435; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q2TB54; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q2TB54; protein.
DR Bgee; ENSMUSG00000026415; Expressed in right kidney and 30 other tissues.
DR Genevisible; Q2TB54; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019862; F:IgA binding; IDA:MGI.
DR GO; GO:0001791; F:IgM binding; IDA:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; TAS:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..535
FT /note="High affinity immunoglobulin alpha and
FT immunoglobulin mu Fc receptor"
FT /id="PRO_0000331484"
FT TOPO_DOM 36..455
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 95..189
FT /note="Ig-like V-type"
FT REGION 95..117
FT /note="Mediates immunoglobulin Fc fragment-binding"
FT REGION 201..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..173
FT /evidence="ECO:0000250"
FT VAR_SEQ 13
FT /note="K -> KHLTCQDTQFPGPAFRVELPSYWSKLRMHSQSAEPWTPDHSLQLLTS
FT LPLASCLWLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033233"
FT MUTAGEN 519
FT /note="L->A: Prevents receptor internalization."
FT /evidence="ECO:0000269|PubMed:11062505"
FT MUTAGEN 520
FT /note="L->A: Prevents receptor internalization."
FT /evidence="ECO:0000269|PubMed:11062505"
FT CONFLICT 42
FT /note="R -> G (in Ref. 1; BAB17312 and 2; AAI10550)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="N -> T (in Ref. 1; BAB17312 and 2; AAI10550)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="I -> V (in Ref. 1; BAB17312, 2; AAI10550 and 3;
FT BAB71750)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="G -> S (in Ref. 1; BAB17312, 2; AAI10550 and 3;
FT BAB71750)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="I -> V (in Ref. 1; BAB17312, 2; AAI10550 and 3;
FT BAB71750)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="V -> A (in Ref. 1; BAB17312, 2; AAI10550 and 3;
FT BAB71750)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="M -> V (in Ref. 1; BAB17312, 2; AAI10550 and 3;
FT BAB71750)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="P -> L (in Ref. 1; BAB17312, 2; AAI10550 and 3;
FT BAB71750)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="S -> N (in Ref. 1; BAB17312 and 3; BAB71750)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="K -> I (in Ref. 2; AAI10551)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="N -> D (in Ref. 1; BAB17312, 2; AAI10550 and 3;
FT BAB71750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 57823 MW; ABC2C22CB0F0E883 CRC64;
MDQGAPAKPS EQKVPSLRTR WEILLLTLCL LHGSSMTPPH RRSHSRWLQA GSPQFRTHLY
NVEAHTAPTP LCCWKNSLSG TNALRGPRLV TGNTGGAVTI HCHYAPSSVN RHQRKYWCRL
GSPLWICHTV VSTNQYTHPD YRGRAALTDI PQSGLFVVRL LRLSLGDVGL YRCGIGDRND
MLFFSVNLTV SAGPSNTTYA AAPASGEPTT ASPGAASSAG NGWTSGITQI LEGSGSEWDR
TVPTTGTSKT TSSANGRQTL RTARTMVPGT GSREEGSIRA AVPTPEGPSP KSRSMSSTTQ
GVWLWSTRNS VTPSVTTSEG RRQGTTPETD GPRDETDVRV SPEAPRKTTG TTRPSALISE
HVTWETLQDK TEVSKQQMLH SLEELSPAPS AQTLNATCLE VASEEGRSID GSLENTTEES
SPPTPSQLSV AGPVWVSVKG PSMKSALMEG ESHTRILTPV STVLALLLIA ALILLKRSLG
RQRTSQKKER VPRITLIQMT HFLPDKLPDE GKNFQQSNLL PPQASLTVLE NDPRP
