IGHG1_MOUSE
ID IGHG1_MOUSE Reviewed; 324 AA.
AC P01868;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ig gamma-1 chain C region secreted form;
GN Name=Ighg1; Synonyms=Igh-4;
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=115593; DOI=10.1016/0092-8674(79)90072-2;
RA Honjo T., Obata M., Yamawaki-Kataoka Y., Kataoka T., Kawakami T.,
RA Takahashi N., Mano Y.;
RT "Cloning and complete nucleotide sequence of mouse immunoglobulin gamma 1
RT chain gene.";
RL Cell 18:559-568(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-324 (MYELOMA PROTEIN MOPC 31C).
RX PubMed=6769752; DOI=10.1016/0378-1119(80)90168-7;
RA Obata M., Yamawaki-Kataoka Y., Takahashi N., Kataoka T., Shimizu A.,
RA Mano Y., Seidman J.G., Peterlin B.M., Leder P., Honjo T.;
RT "Immunoglobulin gamma 1 heavy chain gene: structural gene sequences cloned
RT in a bacterial plasmid.";
RL Gene 9:87-97(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 70-322 (MYELOMA PROTEIN MOPC
RP 21).
RX PubMed=113776; DOI=10.1093/nar/6.10.3305;
RA Rogers J., Clarke P., Salser W.;
RT "Sequence analysis of cloned cDNA encoding part of an immunoglobulin heavy
RT chain.";
RL Nucleic Acids Res. 6:3305-3321(1979).
RN [4]
RP PROTEIN SEQUENCE (MYELOMA PROTEIN MOPC 21).
RX PubMed=98524; DOI=10.1016/s0021-9258(17)34580-5;
RA Adetugbo K.;
RT "Evolution of immunoglobulin subclasses. Primary structure of a murine
RT myeloma gamma1 chain.";
RL J. Biol. Chem. 253:6068-6075(1978).
RN [5]
RP DISULFIDE BONDS (MOPC 21).
RX PubMed=5073237; DOI=10.1042/bj1260837;
RA Svasti J., Milstein C.;
RT "The disulphide bridges of a mouse immunoglobulin G1 protein.";
RL Biochem. J. 126:837-850(1972).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: [Isoform Secreted]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Secreted;
CC IsoId=P01868-1; Sequence=Displayed;
CC Name=Membrane-bound;
CC IsoId=P01869-1; Sequence=External;
CC -!- MISCELLANEOUS: [Isoform Secreted]: May be the major isoform.
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DR EMBL; J00453; AAB59656.1; -; Genomic_DNA.
DR EMBL; V00795; CAA24176.1; -; mRNA.
DR PIR; A02159; G1MS.
DR PDB; 1AHW; X-ray; 3.00 A; B/E=-.
DR PDB; 1AI1; X-ray; 2.80 A; H=1-100.
DR PDB; 1BM3; X-ray; 2.00 A; H=1-102.
DR PDB; 1CLO; X-ray; 2.10 A; H=1-101.
DR PDB; 1CT8; X-ray; 2.20 A; B/D=1-102.
DR PDB; 1DBA; X-ray; 2.80 A; H=1-100.
DR PDB; 1DBB; X-ray; 2.70 A; H=1-100.
DR PDB; 1DBJ; X-ray; 2.70 A; H=1-100.
DR PDB; 1DBK; X-ray; 3.00 A; H=1-100.
DR PDB; 1DBM; X-ray; 2.70 A; H=1-100.
DR PDB; 1EMT; X-ray; 2.25 A; H=1-100.
DR PDB; 1FBI; X-ray; 3.00 A; H/Q=1-99.
DR PDB; 1FDL; X-ray; 2.50 A; H=1-102.
DR PDB; 1FNS; X-ray; 2.00 A; H=1-103.
DR PDB; 1GPO; X-ray; 1.95 A; H/I=1-102.
DR PDB; 1K4D; X-ray; 2.30 A; A=1-101.
DR PDB; 1KEL; X-ray; 1.90 A; H=1-99.
DR PDB; 1KEM; X-ray; 2.20 A; H=1-99.
DR PDB; 1MF2; X-ray; 2.60 A; H/N=1-101.
DR PDB; 1MLC; X-ray; 2.50 A; B/D=1-102.
DR PDB; 1N5Y; X-ray; 3.10 A; H=1-102.
DR PDB; 1N6Q; X-ray; 3.00 A; H=1-102.
DR PDB; 1NTL; X-ray; 30.00 A; A/B=98-324.
DR PDB; 1OAK; X-ray; 2.20 A; H=1-101.
DR PDB; 1OPG; X-ray; 2.00 A; H=1-102.
DR PDB; 1P2C; X-ray; 2.00 A; B/E=1-102.
DR PDB; 1P7K; X-ray; 1.75 A; B/H=1-102.
DR PDB; 1R0A; X-ray; 2.80 A; H=1-102.
DR PDB; 1R3I; X-ray; 2.40 A; H=1-101.
DR PDB; 1R3J; X-ray; 1.90 A; B=1-101.
DR PDB; 1R3K; X-ray; 2.80 A; B=1-101.
DR PDB; 1R3L; X-ray; 2.41 A; B=1-101.
DR PDB; 1RIH; X-ray; 2.50 A; H=1-106.
DR PDB; 1SEQ; X-ray; 1.78 A; H=3-102.
DR PDB; 1YED; X-ray; 3.10 A; B/H=1-102.
DR PDB; 2ATY; X-ray; -; A/B=98-324.
DR PDB; 2B2X; X-ray; 2.20 A; H/I=1-102.
DR PDB; 2DBL; X-ray; 2.90 A; H=1-100.
DR PDB; 3ZO0; X-ray; 1.99 A; A=114-320.
DR PDBsum; 1AHW; -.
DR PDBsum; 1AI1; -.
DR PDBsum; 1BM3; -.
DR PDBsum; 1CLO; -.
DR PDBsum; 1CT8; -.
DR PDBsum; 1DBA; -.
DR PDBsum; 1DBB; -.
DR PDBsum; 1DBJ; -.
DR PDBsum; 1DBK; -.
DR PDBsum; 1DBM; -.
DR PDBsum; 1EMT; -.
DR PDBsum; 1FBI; -.
DR PDBsum; 1FDL; -.
DR PDBsum; 1FNS; -.
DR PDBsum; 1GPO; -.
DR PDBsum; 1K4D; -.
DR PDBsum; 1KEL; -.
DR PDBsum; 1KEM; -.
DR PDBsum; 1MF2; -.
DR PDBsum; 1MLC; -.
DR PDBsum; 1N5Y; -.
DR PDBsum; 1N6Q; -.
DR PDBsum; 1NTL; -.
DR PDBsum; 1OAK; -.
DR PDBsum; 1OPG; -.
DR PDBsum; 1P2C; -.
DR PDBsum; 1P7K; -.
DR PDBsum; 1R0A; -.
DR PDBsum; 1R3I; -.
DR PDBsum; 1R3J; -.
DR PDBsum; 1R3K; -.
DR PDBsum; 1R3L; -.
DR PDBsum; 1RIH; -.
DR PDBsum; 1SEQ; -.
DR PDBsum; 1YED; -.
DR PDBsum; 2ATY; -.
DR PDBsum; 2B2X; -.
DR PDBsum; 2DBL; -.
DR PDBsum; 3ZO0; -.
DR AlphaFoldDB; P01868; -.
DR SMR; P01868; -.
DR IntAct; P01868; 2.
DR MINT; P01868; -.
DR GlyConnect; 248; 4 N-Linked glycans (1 site).
DR SwissPalm; P01868; -.
DR PeptideAtlas; P01868; -.
DR PRIDE; P01868; -.
DR ProteomicsDB; 269541; -. [P01868-1]
DR ABCD; P01868; 18 sequenced antibodies.
DR MGI; MGI:96446; Ighg1.
DR ChiTaRS; Ighg1; mouse.
DR EvolutionaryTrace; P01868; -.
DR Proteomes; UP000000589; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0071735; C:IgG immunoglobulin complex; ISO:MGI.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; 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:0019731; P:antibacterial humoral response; IDA:MGI.
DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IDA:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP: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; 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; IBA:GO_Central.
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 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; IPR003597; Ig_C1-set.
DR Pfam; PF07654; C1-set; 3.
DR SMART; SM00407; IGc1; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW Secreted.
FT CHAIN <1..324
FT /note="Ig gamma-1 chain C region secreted form"
FT /id="PRO_0000153582"
FT REGION 1..97
FT /note="CH1"
FT REGION 98..110
FT /note="Hinge"
FT REGION 111..217
FT /note="CH2"
FT REGION 218..324
FT /note="CH3"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000055"
FT DISULFID 27..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:5073237"
FT DISULFID 102
FT /note="Interchain (with a light chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:5073237"
FT DISULFID 104
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:5073237"
FT DISULFID 107
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:5073237"
FT DISULFID 109
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:5073237"
FT DISULFID 138..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:5073237"
FT DISULFID 244..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:5073237"
FT CONFLICT 276
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1P7K"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1MLC"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1CLO"
FT STRAND 22..35
FT /evidence="ECO:0007829|PDB:1P7K"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1P7K"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1P7K"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1P7K"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1P7K"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:1P7K"
FT TURN 72..77
FT /evidence="ECO:0007829|PDB:1P7K"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1P7K"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1P7K"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1P7K"
SQ SEQUENCE 324 AA; 35705 MW; A338812F3D1F2C93 CRC64;
AKTTPPSVYP LAPGSAAQTN SMVTLGCLVK GYFPEPVTVT WNSGSLSSGV HTFPAVLQSD
LYTLSSSVTV PSSPRPSETV TCNVAHPASS TKVDKKIVPR DCGCKPCICT VPEVSSVFIF
PPKPKDVLTI TLTPKVTCVV VDISKDDPEV QFSWFVDDVE VHTAQTQPRE EQFNSTFRSV
SELPIMHQDW LNGKEFKCRV NSAAFPAPIE KTISKTKGRP KAPQVYTIPP PKEQMAKDKV
SLTCMITDFF PEDITVEWQW NGQPAENYKN TQPIMNTNGS YFVYSKLNVQ KSNWEAGNTF
TCSVLHEGLH NHHTEKSLSH SPGK
