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   02-SEP-2026, entry version 170.
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   AlphaFoldDB; P01867; -.
DR   EMDB; EMD-12746; -.
DR   EMDB; EMD-20487; -.
DR   EMDB; EMD-20488; -.
DR   EMDB; EMD-21368; -.
DR   EMDB; EMD-21369; -.
DR   EMDB; EMD-21370; -.
DR   EMDB; EMD-29350; -.
DR   EMDB; EMD-29727; -.
DR   EMDB; EMD-29728; -.
DR   EMDB; EMD-29733; -.
DR   EMDB; EMD-29741; -.
DR   EMDB; EMD-29742; -.
DR   EMDB; EMD-29743; -.
DR   EMDB; EMD-30786; -.
DR   EMDB; EMD-31056; -.
DR   EMDB; EMD-31838; -.
DR   EMDB; EMD-31839; -.
DR   EMDB; EMD-31840; -.
DR   EMDB; EMD-32759; -.
DR   EMDB; EMD-40456; -.
DR   EMDB; EMD-40457; -.
DR   EMDB; EMD-40467; -.
DR   EMDB; EMD-4598; -.
DR   EMDB; EMD-62748; -.
DR   EMDB; EMD-70872; -.
DR   EMDB; EMD-70873; -.
DR   EMDB; EMD-70874; -.
DR   EMDB; EMD-70875; -.
DR   EMDB; EMD-70876; -.
DR   EMDB; EMD-70877; -.
DR   EMDB; EMD-70889; -.
DR   MDposit; P01867; -.
DR   MDRepo; P01867; -.
DR   SMR; P01867; -.
DR   FunCoup; P01867; 82.
DR   MINT; P01867; -.
DR   GlyConnect; P01867; 3 N-Linked glycans (1 site).
DR   GlyCosmos; P01867; 2 sites, 5 glycans.
DR   GlyGen; P01867; 4 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P01867; -.
DR   PhosphoSitePlus; P01867; -.
DR   SwissPalm; P01867; -.
DR   CPTAC; non-CPTAC-3524; -.
DR   CPTAC; non-CPTAC-3525; -.
DR   jPOST; P01867; -.
DR   PeptideAtlas; P01867; -.
DR   ProteomicsDB; 269537; -. [P01867-1]
DR   ProteomicsDB; 269538; -. [P01867-2]
DR   ABCD; P01867; 4 sequenced antibodies.
DR   AGR; MGI:96445; -.
DR   MGI; MGI:96445; Ighg2b.
DR   InParanoid; P01867; -.
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   EvolutionaryTrace; P01867; -.
DR   PRO; PR:P01867; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P01867; protein.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0071735; C:IgG immunoglobulin complex; ISO:GO_Central.
DR   GO; GO:0042571; C:immunoglobulin complex, circulating; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003823; F:antigen binding; IDA:MGI.
DR   GO; GO:0034988; F:Fc-gamma receptor I complex binding; ISO:GO_Central.
DR   GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR   GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR   GO; GO:0006958; P:complement activation, classical pathway; 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:0006911; P:phagocytosis, engulfment; IDA:MGI.
DR   GO; GO:0006910; P:phagocytosis, recognition; 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   CDD; cd21817; IgC1_CH1_IgEG; 1.
DR   CDD; cd05768; IgC1_CH3_IgAGD_CH4_IgAEM; 1.
DR   FunFam; 2.60.40.10:FF:001739; Ig gamma-2A chain C region; 1.
DR   FunFam; 2.60.40.10:FF:000463; Immunoglobulin heavy constant gamma 1; 1.
DR   FunFam; 2.60.40.10:FF:001129; Immunoglobulin heavy constant gamma 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   InterPro; IPR050380; Immune_Resp_Modulators.
DR   PANTHER; PTHR23411; TAPASIN; 1.
DR   Pfam; PF07654; C1-set; 3.
DR   SMART; SM00407; IGc1; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00290; IG_MHC; 1.
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; -.
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:1YNL"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:1HQ4"
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   STRAND          20..34
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:1YNK"
FT   STRAND          49..57
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   STRAND          60..70
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   TURN            71..76
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:1YNL"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:2RGS"
FT   HELIX           132..134
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   HELIX           226..228
FT                   /evidence="ECO:0007829|PDB:2RGS"
FT   STRAND          235..239
FT                   /evidence="ECO:0007829|PDB:2RGS"
FT   HELIX           240..242
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   HELIX           282..284
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
//