GCAB_MOUSE
ID GCAB_MOUSE Reviewed; 335 AA.
AC P01864;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Ig gamma-2A chain C region secreted form;
DE AltName: Full=B allele;
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].
RC STRAIN=C57BL/6J;
RX PubMed=6170065; DOI=10.1073/pnas.78.7.4495;
RA Schreier P.H., Bothwell A.L.M., Mueller-Hill B., Baltimore D.;
RT "Multiple differences between the nucleic acid sequences of the IgG2aa and
RT IgG2ab alleles of the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4495-4499(1981).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=6794027; DOI=10.1073/pnas.78.7.4031;
RA Dognin M.J., Lauwereys M., Strosberg A.D.;
RT "Multiple amino acid substitutions between murine gamma 2a heavy chain Fc
RT regions of Ig1a and Ig1b allotypic forms.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4031-4035(1981).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185.
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: [Isoform Secreted]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Secreted;
CC IsoId=P01864-1; Sequence=Displayed;
CC Name=Membrane-bound;
CC IsoId=P01865-1; Sequence=External;
CC -!- MISCELLANEOUS: The sequence differs from that of the a allele, from
CC BALB/c mice, at 15% of the positions.
CC -!- MISCELLANEOUS: [Isoform Secreted]: Probably the major isoform.
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DR EMBL; J00479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02153; G2MSAB.
DR PDB; 1BOG; X-ray; 2.60 A; B=1-101.
DR PDB; 1CFN; X-ray; 2.65 A; B=1-101.
DR PDB; 1CFQ; X-ray; 2.80 A; B=1-101.
DR PDB; 1CFS; X-ray; 2.75 A; B=1-101.
DR PDB; 1CFT; X-ray; 2.80 A; B=1-101.
DR PDB; 1HH6; X-ray; 2.60 A; B=1-101.
DR PDB; 1HH9; X-ray; 2.70 A; B=1-101.
DR PDB; 1HI6; X-ray; 2.55 A; B=1-101.
DR PDB; 2IPT; X-ray; 2.00 A; H=1-100.
DR PDB; 2IQ9; X-ray; 2.30 A; H=1-100.
DR PDB; 2IQA; X-ray; 2.00 A; B/H=1-100.
DR PDB; 2VWE; X-ray; 3.40 A; E/L=1-99.
DR PDBsum; 1BOG; -.
DR PDBsum; 1CFN; -.
DR PDBsum; 1CFQ; -.
DR PDBsum; 1CFS; -.
DR PDBsum; 1CFT; -.
DR PDBsum; 1HH6; -.
DR PDBsum; 1HH9; -.
DR PDBsum; 1HI6; -.
DR PDBsum; 2IPT; -.
DR PDBsum; 2IQ9; -.
DR PDBsum; 2IQA; -.
DR PDBsum; 2VWE; -.
DR AlphaFoldDB; P01864; -.
DR SMR; P01864; -.
DR MINT; P01864; -.
DR STRING; 10090.ENSMUSP00000100212; -.
DR GlyGen; P01864; 1 site.
DR iPTMnet; P01864; -.
DR PaxDb; P01864; -.
DR PeptideAtlas; P01864; -.
DR PRIDE; P01864; -.
DR ABCD; P01864; 22 sequenced antibodies.
DR UCSC; uc007pgl.2; mouse. [P01864-1]
DR eggNOG; ENOG502R54U; Eukaryota.
DR PhylomeDB; P01864; -.
DR EvolutionaryTrace; P01864; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01864; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
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; Direct protein sequencing;
KW Glycoprotein; Immunoglobulin domain; Reference proteome; Repeat; Secreted.
FT CHAIN <1..335
FT /note="Ig gamma-2A chain C region secreted form"
FT /id="PRO_0000153585"
FT DOMAIN 6..98
FT /note="Ig-like 1"
FT DOMAIN 126..225
FT /note="Ig-like 2"
FT DOMAIN 234..330
FT /note="Ig-like 3"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT NON_TER 1
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1HI6"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1HI6"
FT STRAND 20..35
FT /evidence="ECO:0007829|PDB:1HI6"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1HI6"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:1HI6"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1HI6"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1HI6"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:1HI6"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1HI6"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1HI6"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1HI6"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1HI6"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1HI6"
SQ SEQUENCE 335 AA; 36596 MW; FA3382792CBB13C6 CRC64;
AKTTAPSVYP LVPVCGGTTG SSVTLGCLVK GYFPEPVTLT WNSGSLSSGV HTFPALLQSG
LYTLSSSVTV TSNTWPSQTI TCNVAHPASS TKVDKKIEPR VPITQNPCPP HQRVPPCAAP
DLLGGPSVFI FPPKIKDVLM ISLSPMVTCV VVDVSEDDPD VQISWFVNNV EVHTAQTQTH
REDYNSTLRV VSALPIQHQD WMSGKEFKCK VNNRALPSPI EKTISKPRGP VRAPQVYVLP
PPAEEMTKKE FSLTCMITGF LPAEIAVDWT SNGRTEQNYK NTATVLDSDG SYFMYSKLRV
QKSTWERGSL FACSVVHEVL HNHLTTKTIS RSLGK
