ID   FCAMR_PONAB             Reviewed;         544 AA.
AC   Q5R770; Q5REH9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=High affinity immunoglobulin alpha and immunoglobulin mu Fc receptor;
DE   AltName: Full=Fc alpha/mu receptor;
DE   AltName: CD_antigen=CD351;
DE   Flags: Precursor;
GN   Name=FCAMR;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 IgM
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH89828.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAH92390.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR857549; CAH89828.1; ALT_INIT; mRNA.
DR   EMBL; CR860248; CAH92390.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001124847.1; NM_001131375.1.
DR   RefSeq; NP_001128857.1; NM_001135385.2.
DR   AlphaFoldDB; Q5R770; -.
DR   SMR; Q5R770; -.
DR   STRING; 9601.ENSPPYP00000000292; -.
DR   GeneID; 100189781; -.
DR   KEGG; pon:100189781; -.
DR   CTD; 83953; -.
DR   eggNOG; ENOG502SNZE; Eukaryota.
DR   InParanoid; Q5R770; -.
DR   OrthoDB; 593994at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
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.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Membrane; Receptor; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..544
FT                   /note="High affinity immunoglobulin alpha and
FT                   immunoglobulin mu Fc receptor"
FT                   /id="PRO_0000331485"
FT   TOPO_DOM        17..462
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        484..544
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          61..169
FT                   /note="Ig-like V-type"
FT   REGION          75..97
FT                   /note="Mediates immunoglobulin Fc fragment-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          218..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        324
FT                   /note="E -> G (in Ref. 1; CAH89828)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        449
FT                   /note="F -> S (in Ref. 1; CAH89828)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   544 AA;  58458 MW;  4443D4C7304B1568 CRC64;
     MPLFLILCLL QGSSFALPQK RPHPRWLWEG SLPSRTHLRA MGTLTPSSPL CWQEESSFAA
     PNALKGSRLV SGEPGGAVTI QCHYAPSSVN RHQRKYWCRL GPPRWICQTI VSTNHYTHHR
     YRDRVALTDF PQRGLFVVRL SQLSPDDIGC YLCGIGSENN MLFLSMNLTI SAGPSSTLPT
     ATPAAGELTM RSYGTASPVA NRWTPGTTQT LGQGTAWDTV ASTPGTSMTT ASAEGRETPG
     ATRLATPGTG SWAEGSVKAP APIPESPASK APAPIPESPA SKSRSMSNTT EGVWEGTRSL
     VTNRAKASKD RREITTTKAD RPREDTEGVR IALDAAKKVL GTIRPPALVS ETLAWEIFPQ
     ATPVSKQQSL SSIGETTPAA GMWTLGTPAA DVWILGTPTA DVWTSMEAAS GEGSSAGDLD
     AATGDRGPQV TLSQAPAVGP WRPPGKESFV KSTFPEDESS SRTLAPVSTM LALFMLMALV
     LLQRKLRRRR TSQEAERVTL IQMTHFLEVN PQPDQLPHVE RKMLQDDSLP AGASLTAPER
     NPGP