GCAA_MOUSE
ID GCAA_MOUSE Reviewed; 330 AA.
AC P01863;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Ig gamma-2A chain C region, A allele;
DE AltName: Full=Immunoglobulin heavy chain gamma polypeptide;
GN Name=Ighg;
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].
RX PubMed=6777755; DOI=10.1093/nar/8.14.3143;
RA Sikorav J.-L., Auffray C., Rougeon F.;
RT "Structure of the constant and 3' untranslated regions of the murine Balb/c
RT gamma 2a heavy chain messenger RNA.";
RL Nucleic Acids Res. 8:3143-3155(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6787604; DOI=10.1073/pnas.78.4.2442;
RA Ollo R., Auffray C., Morchamps C., Rougeon F.;
RT "Comparison of mouse immunoglobulin gamma 2a and gamma 2b chain genes
RT suggests that exons can be exchanged between genes in a multigenic
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:2442-2446(1981).
RN [4]
RP MYELOMA PROTEIN MOPC 173.
RX PubMed=4831970; DOI=10.1111/j.1432-1033.1974.tb03428.x;
RA Bourgois A., Fougereau M., Rocca-Serra J.;
RT "Determination of the primary structure of a mouse IgG2a immunoglobulin:
RT amino-acid sequence of the Fc fragment. Implications for the evolution of
RT immunoglobulin structure and function.";
RL Eur. J. Biochem. 43:423-435(1974).
RN [5]
RP DISULFIDE BONDS.
RX PubMed=4565406; DOI=10.1111/j.1432-1033.1972.tb02117.x;
RA de Preval C., Fougereau M.;
RT "Determination of the primary structure of a mouse gamma G2a
RT immunoglobulin. Identification of the disulfide bridges.";
RL Eur. J. Biochem. 30:452-462(1972).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-180.
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).
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DR EMBL; V00798; CAA24178.1; -; mRNA.
DR PIR; A02152; G2MSA.
DR PDB; 1DQM; X-ray; 2.10 A; H=1-97.
DR PDB; 1DQQ; X-ray; 1.80 A; B/D=1-97.
DR PDB; 1EHL; X-ray; 2.40 A; H=1-99.
DR PDB; 1FE8; X-ray; 2.03 A; H/I/J=1-101.
DR PDB; 1GGI; X-ray; 2.80 A; H/J=1-107.
DR PDB; 1IGT; X-ray; 2.80 A; B/D=2-326.
DR PDB; 1KEG; X-ray; 2.40 A; H=1-100.
DR PDB; 1KN2; X-ray; 1.90 A; H=1-99.
DR PDB; 1KN4; X-ray; 1.90 A; H=1-99.
DR PDB; 1KNO; X-ray; 3.20 A; B/D/F=1-101.
DR PDB; 1MH5; X-ray; 2.10 A; B/H=1-111.
DR PDB; 1MNU; X-ray; 2.50 A; H=1-104.
DR PDB; 1MPA; X-ray; 2.60 A; H=1-104.
DR PDB; 1OB1; X-ray; 2.90 A; B/E=1-99.
DR PDB; 1PG7; X-ray; 2.50 A; X/Z=1-100.
DR PDB; 1UYW; X-ray; 2.00 A; H/M=1-100.
DR PDB; 1YEC; X-ray; 1.90 A; H=1-99.
DR PDB; 1YEF; X-ray; 2.00 A; H=1-99.
DR PDB; 1YEG; X-ray; 2.00 A; H=1-99.
DR PDB; 1YEH; X-ray; 2.55 A; H=1-99.
DR PDB; 1YEI; X-ray; 1.90 A; H=1-99.
DR PDB; 1YEJ; X-ray; 1.85 A; H=1-99.
DR PDB; 1YEK; X-ray; 2.10 A; H=1-99.
DR PDB; 2IPU; X-ray; 1.65 A; G/H=1-103.
DR PDB; 2MPA; X-ray; 2.60 A; H=1-104.
DR PDB; 2R0W; X-ray; 2.50 A; H=1-100.
DR PDB; 2R0Z; X-ray; 2.10 A; H=1-100.
DR PDB; 2R29; X-ray; 3.00 A; H=1-100.
DR PDB; 2R69; X-ray; 3.80 A; H=1-100.
DR PDB; 2R6P; EM; 24.00 A; D/F=1-100.
DR PDB; 2VL5; X-ray; 2.10 A; A/C=1-99.
DR PDB; 2ZCH; X-ray; 2.83 A; H=1-107.
DR PDB; 2ZCK; X-ray; 3.10 A; H=1-107.
DR PDB; 2ZCL; X-ray; 3.25 A; H=1-107.
DR PDB; 3BGF; X-ray; 3.00 A; B/H=1-99.
DR PDB; 3OZ9; X-ray; 1.60 A; H=1-100.
DR PDB; 3ZO0; X-ray; 1.99 A; A=120-326.
DR PDB; 4F37; X-ray; 2.57 A; F/H=1-100.
DR PDB; 4KVC; X-ray; 2.31 A; H=1-100.
DR PDB; 5VAA; X-ray; 1.55 A; A/B=107-330.
DR PDBsum; 1DQM; -.
DR PDBsum; 1DQQ; -.
DR PDBsum; 1EHL; -.
DR PDBsum; 1FE8; -.
DR PDBsum; 1GGI; -.
DR PDBsum; 1IGT; -.
DR PDBsum; 1KEG; -.
DR PDBsum; 1KN2; -.
DR PDBsum; 1KN4; -.
DR PDBsum; 1KNO; -.
DR PDBsum; 1MH5; -.
DR PDBsum; 1MNU; -.
DR PDBsum; 1MPA; -.
DR PDBsum; 1OB1; -.
DR PDBsum; 1PG7; -.
DR PDBsum; 1UYW; -.
DR PDBsum; 1YEC; -.
DR PDBsum; 1YEF; -.
DR PDBsum; 1YEG; -.
DR PDBsum; 1YEH; -.
DR PDBsum; 1YEI; -.
DR PDBsum; 1YEJ; -.
DR PDBsum; 1YEK; -.
DR PDBsum; 2IPU; -.
DR PDBsum; 2MPA; -.
DR PDBsum; 2R0W; -.
DR PDBsum; 2R0Z; -.
DR PDBsum; 2R29; -.
DR PDBsum; 2R69; -.
DR PDBsum; 2R6P; -.
DR PDBsum; 2VL5; -.
DR PDBsum; 2ZCH; -.
DR PDBsum; 2ZCK; -.
DR PDBsum; 2ZCL; -.
DR PDBsum; 3BGF; -.
DR PDBsum; 3OZ9; -.
DR PDBsum; 3ZO0; -.
DR PDBsum; 4F37; -.
DR PDBsum; 4KVC; -.
DR PDBsum; 5VAA; -.
DR AlphaFoldDB; P01863; -.
DR SMR; P01863; -.
DR GlyGen; P01863; 1 site.
DR iPTMnet; P01863; -.
DR MaxQB; P01863; -.
DR PeptideAtlas; P01863; -.
DR PRIDE; P01863; -.
DR ABCD; P01863; 12 sequenced antibodies.
DR MGI; MGI:2144967; Ighg.
DR InParanoid; P01863; -.
DR EvolutionaryTrace; P01863; -.
DR PRO; PR:P01863; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01863; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IPI:AgBase.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP: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; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Reference proteome; Repeat.
FT CHAIN <1..330
FT /note="Ig gamma-2A chain C region, A allele"
FT /id="PRO_0000153584"
FT DOMAIN 6..98
FT /note="Ig-like 1"
FT DOMAIN 121..220
FT /note="Ig-like 2"
FT DOMAIN 229..325
FT /note="Ig-like 3"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT DISULFID 15
FT /note="Interchain (with a light chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4565406"
FT DISULFID 27..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4565406"
FT DISULFID 107
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4565406"
FT DISULFID 110
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4565406"
FT DISULFID 112
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4565406"
FT DISULFID 144..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4565406"
FT DISULFID 250..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4565406"
FT NON_TER 1
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:3OZ9"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1DQQ"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1YEC"
FT STRAND 22..35
FT /evidence="ECO:0007829|PDB:3OZ9"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3OZ9"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3OZ9"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:3OZ9"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:3OZ9"
FT TURN 72..77
FT /evidence="ECO:0007829|PDB:3OZ9"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3OZ9"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3OZ9"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3OZ9"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:5VAA"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:5VAA"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:5VAA"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5VAA"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 243..258
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:5VAA"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:5VAA"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:5VAA"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:5VAA"
SQ SEQUENCE 330 AA; 36389 MW; B84361C5445A6864 CRC64;
AKTTAPSVYP LAPVCGDTTG SSVTLGCLVK GYFPEPVTLT WNSGSLSSGV HTFPAVLQSD
LYTLSSSVTV TSSTWPSQSI TCNVAHPASS TKVDKKIEPR GPTIKPCPPC KCPAPNLLGG
PSVFIFPPKI KDVLMISLSP IVTCVVVDVS EDDPDVQISW FVNNVEVHTA QTQTHREDYN
STLRVVSALP IQHQDWMSGK EFKCKVNNKD LPAPIERTIS KPKGSVRAPQ VYVLPPPEEE
MTKKQVTLTC MVTDFMPEDI YVEWTNNGKT ELNYKNTEPV LDSDGSYFMY SKLRVEKKNW
VERNSYSCSV VHEGLHNHHT TKSFSRTPGK
