IGG2B_MOUSE
ID IGG2B_MOUSE Reviewed; 404 AA.
AC P01867; P01866;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Immunoglobulin heavy constant gamma 2B {ECO:0000312|MGI:MGI:96445};
DE AltName: Full=Ig gamma-2B chain C region {ECO:0000305};
GN Name=Ighg2b {ECO:0000312|MGI:MGI:96445}; Synonyms=Igh-3 {ECO:0000305};
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=6766534; DOI=10.1038/283786a0;
RA Yamawaki-Kataoka Y., Kataoka T., Takahashi N., Obata M., Honjo T.;
RT "Complete nucleotide sequence of immunoglobulin gamma2b chain gene cloned
RT from newborn nouse DNA.";
RL Nature 283:786-789(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE (MPC 11).
RX PubMed=117548; DOI=10.1126/science.117548;
RA Tucker P.W., Marcu K.B., Slightom J.L., Blattner F.R.;
RT "Structure of the constant and 3' untranslated regions of the murine gamma
RT 2b heavy chain messenger RNA.";
RL Science 206:1299-1303(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=117549; DOI=10.1126/science.117549;
RA Tucker P.W., Marcu K.B., Newell N., Richards J., Blattner F.R.;
RT "Sequence of the cloned gene for the constant region of murine gamma 2b
RT immunoglobulin heavy chain.";
RL Science 206:1303-1306(1979).
RN [4]
RP NUCLEOTIDE SEQUENCE (ALLELE B).
RX PubMed=6803173; DOI=10.1038/296761a0;
RA Ollo R., Rougeon F.;
RT "Mouse immunoglobulin allotypes: post-duplication divergence of gamma 2a
RT and gamma 2b chain genes.";
RL Nature 296:761-763(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-402.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-377.
RX PubMed=6799207; DOI=10.1016/0092-8674(81)90029-5;
RA Rogers J., Choi E., Souza L., Carter C., Word C.J., Kuehl M., Eisenberg D.,
RA Wall R.;
RT "Gene segments encoding transmembrane carboxyl termini of immunoglobulin
RT gamma chains.";
RL Cell 26:19-27(1981).
RN [7]
RP GLYCOSYLATION AT THR-104.
RX PubMed=7512967; DOI=10.1016/s0021-9258(17)32722-9;
RA Kim H., Yamaguchi Y., Masuda K., Matsunaga C., Yamamoto K., Irimura T.,
RA Takahashi N., Kato K., Arata Y.;
RT "O-glycosylation in hinge region of mouse immunoglobulin G2b.";
RL J. Biol. Chem. 269:12345-12350(1994).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 1]: Cell membrane {ECO:0000305}; Single-
CC pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Membrane-bound;
CC IsoId=P01867-1; Sequence=Displayed;
CC Name=2; Synonyms=Secreted;
CC IsoId=P01867-2; Sequence=VSP_034614, VSP_034615;
CC -!- PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is
CC modified with 2 sialic acid residues. {ECO:0000269|PubMed:7512967}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be the major isoform. {ECO:0000305}.
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DR EMBL; J00461; AAB59659.1; -; Genomic_DNA.
DR EMBL; J00462; AAB59659.1; JOINED; Genomic_DNA.
DR PIR; C02154; G2MSBM.
DR PIR; S25057; G2MS11.
DR PDB; 1CBV; X-ray; 2.66 A; H=1-97.
DR PDB; 1CF8; X-ray; 2.70 A; H=1-98.
DR PDB; 1CIC; X-ray; 2.50 A; B=2-99.
DR PDB; 1ETZ; X-ray; 2.60 A; B/H=1-101.
DR PDB; 1FJ1; X-ray; 2.68 A; B/D=1-99.
DR PDB; 1FL3; X-ray; 2.45 A; A/H=1-97.
DR PDB; 1HQ4; X-ray; 2.70 A; B/D=1-98.
DR PDB; 1MAM; X-ray; 2.45 A; H=1-97.
DR PDB; 1NBV; X-ray; 2.00 A; H=1-97.
DR PDB; 1OSP; X-ray; 1.95 A; H=1-97.
DR PDB; 1UB5; X-ray; 2.00 A; A/H=1-97.
DR PDB; 1UB6; X-ray; 2.12 A; A/H=1-97.
DR PDB; 1YNK; X-ray; 2.10 A; H=1-102.
DR PDB; 1YNL; X-ray; 1.70 A; H=1-102.
DR PDB; 1ZTX; X-ray; 2.50 A; H=1-99.
DR PDB; 2GJZ; X-ray; 2.65 A; B/H=1-98.
DR PDB; 2GK0; X-ray; 2.45 A; B/H=1-98.
DR PDB; 2Q8A; X-ray; 2.40 A; H=1-97.
DR PDB; 2Q8B; X-ray; 2.30 A; H=1-97.
DR PDB; 2RGS; X-ray; 2.13 A; A/B=117-334.
DR PDB; 3CFD; X-ray; 2.50 A; B/H=1-99.
DR PDB; 3CFE; X-ray; 2.99 A; B/H=1-99.
DR PDB; 5UBX; X-ray; 2.70 A; A/B=108-334.
DR PDB; 6KRU; X-ray; 2.30 A; A/B/C/D/E/F=117-334.
DR PDB; 6KRV; X-ray; 3.30 A; A/B/C=117-334.
DR PDBsum; 1CBV; -.
DR PDBsum; 1CF8; -.
DR PDBsum; 1CIC; -.
DR PDBsum; 1ETZ; -.
DR PDBsum; 1FJ1; -.
DR PDBsum; 1FL3; -.
DR PDBsum; 1HQ4; -.
DR PDBsum; 1MAM; -.
DR PDBsum; 1NBV; -.
DR PDBsum; 1OSP; -.
DR PDBsum; 1UB5; -.
DR PDBsum; 1UB6; -.
DR PDBsum; 1YNK; -.
DR PDBsum; 1YNL; -.
DR PDBsum; 1ZTX; -.
DR PDBsum; 2GJZ; -.
DR PDBsum; 2GK0; -.
DR PDBsum; 2Q8A; -.
DR PDBsum; 2Q8B; -.
DR PDBsum; 2RGS; -.
DR PDBsum; 3CFD; -.
DR PDBsum; 3CFE; -.
DR PDBsum; 5UBX; -.
DR PDBsum; 6KRU; -.
DR PDBsum; 6KRV; -.
DR AlphaFoldDB; P01867; -.
DR SMR; P01867; -.
DR MINT; P01867; -.
DR GlyConnect; 684; 3 N-Linked glycans (1 site).
DR GlyGen; P01867; 2 sites, 4 N-linked glycans (1 site).
DR iPTMnet; P01867; -.
DR PhosphoSitePlus; P01867; -.
DR CPTAC; non-CPTAC-3524; -.
DR CPTAC; non-CPTAC-3525; -.
DR MaxQB; P01867; -.
DR PeptideAtlas; P01867; -.
DR PRIDE; P01867; -.
DR ProteomicsDB; 269537; -. [P01867-1]
DR ProteomicsDB; 269538; -. [P01867-2]
DR ABCD; P01867; 4 sequenced antibodies.
DR MGI; MGI:96445; Ighg2b.
DR InParanoid; P01867; -.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-173623; Classical antibody-mediated complement activation.
DR Reactome; R-MMU-2029481; FCGR activation.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR ChiTaRS; Ighg2b; mouse.
DR EvolutionaryTrace; P01867; -.
DR PRO; PR:P01867; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01867; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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: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; 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 Secreted; Transmembrane; Transmembrane helix.
FT CHAIN <1..404
FT /note="Immunoglobulin heavy constant gamma 2B"
FT /id="PRO_0000153588"
FT TRANSMEM 351..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 5..97
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 104
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7512967"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 14
FT /note="Interchain (with a light chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 26..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 108
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 111
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 114
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 117
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 149..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 255..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 335
FT /note="L -> K (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034614"
FT VAR_SEQ 336..404
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034615"
FT VARIANT 162
FT /note="Q -> R (in allele B)"
FT VARIANT 193
FT /note="T -> A (in allele B)"
FT VARIANT 299
FT /note="N -> D (in allele B)"
FT VARIANT 300
FT /note="M -> I (in allele B)"
FT CONFLICT 24
FT /note="L -> S (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="S -> P (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="I -> T (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1OSP"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1OSP"
FT STRAND 20..31
FT /evidence="ECO:0007829|PDB:1OSP"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1ETZ"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1OSP"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1MAM"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:1OSP"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:1OSP"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1OSP"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1OSP"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1OSP"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1OSP"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1OSP"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2RGS"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6KRV"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5UBX"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:2RGS"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:2RGS"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2RGS"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 248..263
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:6KRV"
FT STRAND 292..301
FT /evidence="ECO:0007829|PDB:2RGS"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:2RGS"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2RGS"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:2RGS"
SQ SEQUENCE 404 AA; 44259 MW; AE17A03221F6EC0C CRC64;
KTTPPSVYPL APGCGDTTGS SVTLGCLVKG YFPESVTVTW NSGSLSSSVH TFPALLQSGL
YTMSSSVTVP SSTWPSQTVT CSVAHPASST TVDKKLEPSG PISTINPCPP CKECHKCPAP
NLEGGPSVFI FPPNIKDVLM ISLTPKVTCV VVDVSEDDPD VQISWFVNNV EVHTAQTQTH
REDYNSTIRV VSTLPIQHQD WMSGKEFKCK VNNKDLPSPI ERTISKIKGL VRAPQVYILP
PPAEQLSRKD VSLTCLVVGF NPGDISVEWT SNGHTEENYK DTAPVLDSDG SYFIYSKLNM
KTSKWEKTDS FSCNVRHEGL KNYYLKKTIS RSPGLDLDDI CAEAKDGELD GLWTTITIFI
SLFLLSVCYS ASVTLFKVKW IFSSVVELKQ KISPDYRNMI GQGA
