GCAM_MOUSE
ID GCAM_MOUSE Reviewed; 398 AA.
AC P01865;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ig gamma-2A chain C region, membrane-bound form;
GN Name=Igh-1a;
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 [GENOMIC DNA].
RX PubMed=6262729; DOI=10.1093/nar/9.6.1365;
RA Yamawaki-Kataoka Y., Miyata T., Honjo T.;
RT "The complete nucleotide sequence of mouse immunoglobin gamma 2a gene and
RT evolution of heavy chain genes: further evidence for intervening sequence-
RT mediated domain transfer.";
RL Nucleic Acids Res. 9:1365-1381(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 329-398.
RX PubMed=6283537; DOI=10.1073/pnas.79.8.2623;
RA Yamawaki-Kataoka Y., Nakai S., Miyata T., Honjo T.;
RT "Nucleotide sequences of gene segments encoding membrane domains of
RT immunoglobulin gamma chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2623-2627(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 372-398.
RX PubMed=2513486; DOI=10.1016/0161-5890(89)90137-5;
RA Hall B., Milcarek C.;
RT "Sequence and polyadenylation site determination of the murine
RT immunoglobulin gamma 2a membrane 3' untranslated region.";
RL Mol. Immunol. 26:819-826(1989).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-179.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Membrane-bound;
CC IsoId=P01865-1; Sequence=Displayed;
CC Name=Secreted;
CC IsoId=P01864-1; Sequence=External;
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DR EMBL; J00470; AAB59661.1; -; Genomic_DNA.
DR EMBL; J00471; AAB59661.1; JOINED; Genomic_DNA.
DR EMBL; M35032; AAA37919.1; -; Genomic_DNA.
DR PIR; A02154; G2MSAM.
DR PDB; 1AXT; X-ray; 2.15 A; H=1-99.
DR PDB; 1DQJ; X-ray; 2.00 A; B=1-96.
DR PDB; 1E4W; X-ray; 1.95 A; H=1-98.
DR PDB; 1EGJ; X-ray; 2.80 A; H=1-96.
DR PDB; 1FLR; X-ray; 1.85 A; H=1-100.
DR PDB; 1FPT; X-ray; 3.00 A; H=1-99.
DR PDB; 1GGB; X-ray; 2.80 A; H=1-99.
DR PDB; 1GGC; X-ray; 2.80 A; H=1-99.
DR PDB; 1KB5; X-ray; 2.50 A; H=1-99.
DR PDB; 1LO0; X-ray; 2.00 A; H/Y=1-101.
DR PDB; 1NBY; X-ray; 1.80 A; B=1-96.
DR PDB; 1NCA; X-ray; 2.50 A; H=1-100.
DR PDB; 1NCB; X-ray; 2.50 A; H=1-100.
DR PDB; 1NCC; X-ray; 2.50 A; H=1-100.
DR PDB; 1NCD; X-ray; 2.90 A; H=1-100.
DR PDB; 1NCW; X-ray; 1.30 A; H=1-102.
DR PDB; 1ND0; X-ray; 2.45 A; B/D/F/H=1-102.
DR PDB; 1NDG; X-ray; 1.90 A; B=1-96.
DR PDB; 1NDM; X-ray; 2.10 A; B=1-96.
DR PDB; 1ORQ; X-ray; 3.20 A; B=1-99.
DR PDB; 1PLG; X-ray; 2.80 A; H=1-97.
DR PDB; 1RU9; X-ray; 2.50 A; H=1-102.
DR PDB; 1RUA; X-ray; 1.75 A; H=1-102.
DR PDB; 1RUK; X-ray; 1.40 A; H=1-102.
DR PDB; 1RUL; X-ray; 1.88 A; H=1-102.
DR PDB; 1RUM; X-ray; 1.48 A; H=1-102.
DR PDB; 1RUP; X-ray; 1.40 A; H=1-102.
DR PDB; 1YEE; X-ray; 2.20 A; H=1-98.
DR PDB; 3FO9; X-ray; 1.90 A; B/H=1-99.
DR PDB; 3J3P; EM; 9.10 A; H=1-99.
DR PDB; 4FAB; X-ray; 2.70 A; H=1-97.
DR PDB; 4ZXB; X-ray; 3.30 A; C=1-106.
DR PDB; 6UQC; X-ray; 1.87 A; C/D/E/F=119-325.
DR PDBsum; 1AXT; -.
DR PDBsum; 1DQJ; -.
DR PDBsum; 1E4W; -.
DR PDBsum; 1EGJ; -.
DR PDBsum; 1FLR; -.
DR PDBsum; 1FPT; -.
DR PDBsum; 1GGB; -.
DR PDBsum; 1GGC; -.
DR PDBsum; 1KB5; -.
DR PDBsum; 1LO0; -.
DR PDBsum; 1NBY; -.
DR PDBsum; 1NCA; -.
DR PDBsum; 1NCB; -.
DR PDBsum; 1NCC; -.
DR PDBsum; 1NCD; -.
DR PDBsum; 1NCW; -.
DR PDBsum; 1ND0; -.
DR PDBsum; 1NDG; -.
DR PDBsum; 1NDM; -.
DR PDBsum; 1ORQ; -.
DR PDBsum; 1PLG; -.
DR PDBsum; 1RU9; -.
DR PDBsum; 1RUA; -.
DR PDBsum; 1RUK; -.
DR PDBsum; 1RUL; -.
DR PDBsum; 1RUM; -.
DR PDBsum; 1RUP; -.
DR PDBsum; 1YEE; -.
DR PDBsum; 3FO9; -.
DR PDBsum; 3J3P; -.
DR PDBsum; 4FAB; -.
DR PDBsum; 4ZXB; -.
DR PDBsum; 6UQC; -.
DR AlphaFoldDB; P01865; -.
DR PCDDB; P01865; -.
DR SMR; P01865; -.
DR IntAct; P01865; 2.
DR MINT; P01865; -.
DR GlyGen; P01865; 1 site.
DR iPTMnet; P01865; -.
DR MaxQB; P01865; -.
DR PRIDE; P01865; -.
DR ProteomicsDB; 266787; -. [P01865-1]
DR MGI; MGI:96443; Igh-1a.
DR InParanoid; P01865; -.
DR EvolutionaryTrace; P01865; -.
DR PRO; PR:P01865; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01865; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0071735; C:IgG immunoglobulin complex; ISO:MGI.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005771; C:multivesicular body; IDA:MGI.
DR GO; GO:0003823; F:antigen binding; IDA:MGI.
DR GO; GO:0034988; F:Fc-gamma receptor I complex binding; ISO:MGI.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IDA:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IDA:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0045022; P:early endosome to late endosome transport; IDA:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:MGI.
DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IDA:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IDA:MGI.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IDA:MGI.
DR GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
DR GO; GO:0050871; P:positive regulation of B cell activation; IDA:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; IDA:MGI.
DR GO; GO:0050778; P:positive regulation of immune response; IDA:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
DR GO; GO:0001812; P:positive regulation of type I hypersensitivity; IDA:MGI.
DR GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; IDA:MGI.
DR GO; GO:0030162; P:regulation of proteolysis; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 3.
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 Pfam; PF07654; C1-set; 3.
DR SMART; SM00407; IGc1; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN <1..398
FT /note="Ig gamma-2A chain C region, membrane-bound form"
FT /id="PRO_0000153586"
FT TRANSMEM 345..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 5..97
FT /note="Ig-like 1"
FT DOMAIN 120..219
FT /note="Ig-like 2"
FT DOMAIN 228..324
FT /note="Ig-like 3"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT DISULFID 14
FT /note="Interchain (with a light chain)"
FT DISULFID 26..81
FT DISULFID 106
FT /note="Interchain (with a heavy chain)"
FT DISULFID 109
FT /note="Interchain (with a heavy chain)"
FT DISULFID 111
FT /note="Interchain (with a heavy chain)"
FT DISULFID 143..203
FT DISULFID 249..307
FT NON_TER 1
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1NCW"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1NCW"
FT STRAND 17..34
FT /evidence="ECO:0007829|PDB:1NCW"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1NCW"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1NCW"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1NCW"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1NCW"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:1NCW"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1NCW"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1NCW"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1NCW"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1NCW"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1NCW"
SQ SEQUENCE 398 AA; 43949 MW; B9CE2EE11224D13B CRC64;
KTTAPSVYPL APVCGDTTGS SVTLGCLVKG YFPEPVTLTW NSGSLSSGVH TFPAVLQSDL
YTLSSSVTVT SSTWPSQSIT CNVAHPASST KVDKKIEPRG PTIKPCPPCK CPAPNLLGGP
SVFIFPPKIK DVLMISLSPI VTCVVVDVSE DDPDVQISWF VNNVEVHTAQ TQTHREDYNS
TLRVVSALPI QHQDWMSGKE FKCKVNNKDL PAPIERTISK PKGSVRAPQV YVLPPPEEEM
TKKQVTLTCM VTDFMPEDIY VEWTNNGKTE LNYKNTEPVL DSDGSYFMYS KLRVEKKNWV
ERNSYSCSVV HEGLHNHHTT KSFSRTPGLD LDDVCAEAQD GELDGLWTTI TIFISLFLLS
VCYSASVTLF KVKWIFSSVV ELKQTISPDY RNMIGQGA
