ID GCAM_MOUSE Reviewed; 398 AA. AC P01865; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 3. DT 24-JAN-2024, entry version 164. DE RecName: Full=Ig gamma-2A chain C region, membrane-bound form; GN Name=Igh-1a; 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=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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 329-398. 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 372-398. RX PubMed=2513486; DOI=10.1016/0161-5890(89)90137-5; RA Hall B., Milcarek C.; RT "Sequence and polyadenylation site determination of the murine RT immunoglobulin gamma 2a membrane 3' untranslated region."; RL Mol. Immunol. 26:819-826(1989). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-179. 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: Cell membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Membrane-bound; CC IsoId=P01865-1; Sequence=Displayed; CC Name=Secreted; CC IsoId=P01864-1; Sequence=External; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J00470; AAB59661.1; -; Genomic_DNA. DR EMBL; J00471; AAB59661.1; JOINED; Genomic_DNA. DR EMBL; M35032; AAA37919.1; -; Genomic_DNA. DR PIR; A02154; G2MSAM. DR PDB; 1AXT; X-ray; 2.15 A; H=1-99. DR PDB; 1DQJ; X-ray; 2.00 A; B=1-96. DR PDB; 1E4W; X-ray; 1.95 A; H=1-98. DR PDB; 1EGJ; X-ray; 2.80 A; H=1-96. DR PDB; 1FLR; X-ray; 1.85 A; H=1-100. DR PDB; 1FPT; X-ray; 3.00 A; H=1-99. DR PDB; 1GGB; X-ray; 2.80 A; H=1-99. DR PDB; 1GGC; X-ray; 2.80 A; H=1-99. DR PDB; 1KB5; X-ray; 2.50 A; H=1-99. DR PDB; 1LO0; X-ray; 2.00 A; H/Y=1-101. DR PDB; 1NBY; X-ray; 1.80 A; B=1-96. DR PDB; 1NCA; X-ray; 2.50 A; H=1-100. DR PDB; 1NCB; X-ray; 2.50 A; H=1-100. DR PDB; 1NCC; X-ray; 2.50 A; H=1-100. DR PDB; 1NCD; X-ray; 2.90 A; H=1-100. DR PDB; 1NCW; X-ray; 1.30 A; H=1-102. DR PDB; 1ND0; X-ray; 2.45 A; B/D/F/H=1-102. DR PDB; 1NDG; X-ray; 1.90 A; B=1-96. DR PDB; 1NDM; X-ray; 2.10 A; B=1-96. DR PDB; 1ORQ; X-ray; 3.20 A; B=1-99. DR PDB; 1PLG; X-ray; 2.80 A; H=1-97. DR PDB; 1RU9; X-ray; 2.50 A; H=1-102. DR PDB; 1RUA; X-ray; 1.75 A; H=1-102. DR PDB; 1RUK; X-ray; 1.40 A; H=1-102. DR PDB; 1RUL; X-ray; 1.88 A; H=1-102. DR PDB; 1RUM; X-ray; 1.48 A; H=1-102. DR PDB; 1RUP; X-ray; 1.40 A; H=1-102. DR PDB; 1YEE; X-ray; 2.20 A; H=1-98. DR PDB; 3FO9; X-ray; 1.90 A; B/H=1-99. DR PDB; 3J3P; EM; 9.10 A; H=1-99. DR PDB; 4FAB; X-ray; 2.70 A; H=1-97. DR PDB; 4ZXB; X-ray; 3.30 A; C=1-106. DR PDB; 6UQC; X-ray; 1.87 A; C/D/E/F=119-325. DR PDB; 8AQT; EM; 4.40 A; A=97-328. DR PDB; 8AQU; EM; 3.22 A; A=97-328. DR PDB; 8AQV; EM; 2.96 A; A=97-328. DR PDBsum; 1AXT; -. DR PDBsum; 1DQJ; -. DR PDBsum; 1E4W; -. DR PDBsum; 1EGJ; -. DR PDBsum; 1FLR; -. DR PDBsum; 1FPT; -. DR PDBsum; 1GGB; -. DR PDBsum; 1GGC; -. DR PDBsum; 1KB5; -. DR PDBsum; 1LO0; -. DR PDBsum; 1NBY; -. DR PDBsum; 1NCA; -. DR PDBsum; 1NCB; -. DR PDBsum; 1NCC; -. DR PDBsum; 1NCD; -. DR PDBsum; 1NCW; -. DR PDBsum; 1ND0; -. DR PDBsum; 1NDG; -. DR PDBsum; 1NDM; -. DR PDBsum; 1ORQ; -. DR PDBsum; 1PLG; -. DR PDBsum; 1RU9; -. DR PDBsum; 1RUA; -. DR PDBsum; 1RUK; -. DR PDBsum; 1RUL; -. DR PDBsum; 1RUM; -. DR PDBsum; 1RUP; -. DR PDBsum; 1YEE; -. DR PDBsum; 3FO9; -. DR PDBsum; 3J3P; -. DR PDBsum; 4FAB; -. DR PDBsum; 4ZXB; -. DR PDBsum; 6UQC; -. DR PDBsum; 8AQT; -. DR PDBsum; 8AQU; -. DR PDBsum; 8AQV; -. DR AlphaFoldDB; P01865; -. DR PCDDB; P01865; -. DR SMR; P01865; -. DR IntAct; P01865; 2. DR MINT; P01865; -. DR GlyCosmos; P01865; 1 site, No reported glycans. DR GlyGen; P01865; 1 site. DR iPTMnet; P01865; -. DR MaxQB; P01865; -. DR ProteomicsDB; 266787; -. [P01865-1] DR AGR; MGI:96443; -. DR MGI; MGI:96443; Igh-1a. DR InParanoid; P01865; -. DR EvolutionaryTrace; P01865; -. DR PRO; PR:P01865; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P01865; Protein. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0005615; C:extracellular space; ISO:MGI. DR GO; GO:0071735; C:IgG immunoglobulin complex; ISO:MGI. DR GO; GO:0042571; C:immunoglobulin complex, circulating; IDA:MGI. DR GO; GO:0005771; C:multivesicular body; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO: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; IBA:GO_Central. DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IDA:MGI. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0006958; P:complement activation, classical pathway; IDA:MGI. DR GO; GO:0045022; P:early endosome to late endosome transport; IDA:MGI. DR GO; GO:0008333; P:endosome to lysosome transport; 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:0050871; P:positive regulation of B cell activation; IDA:MGI. DR GO; GO:0045807; P:positive regulation of endocytosis; 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 GO; GO:0030162; P:regulation of proteolysis; IDA:MGI. DR GO; GO:0009617; P:response to bacterium; IEP:MGI. DR CDD; cd21817; IgC1_CH1_IgEG; 1. DR CDD; cd05768; IgC1_CH3_IgAGD_CH4_IgAEM; 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 PANTHER; PTHR23411:SF28; IG GAMMA-2A CHAIN C REGION SECRETED FORM-RELATED; 1. 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. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix. FT CHAIN <1..398 FT /note="Ig gamma-2A chain C region, membrane-bound form" FT /id="PRO_0000153586" FT TRANSMEM 345..362 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 363..398 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 5..97 FT /note="Ig-like 1" FT DOMAIN 120..219 FT /note="Ig-like 2" FT DOMAIN 228..324 FT /note="Ig-like 3" FT CARBOHYD 179 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:17330941" FT DISULFID 14 FT /note="Interchain (with a light chain)" FT DISULFID 26..81 FT DISULFID 106 FT /note="Interchain (with a heavy chain)" FT DISULFID 109 FT /note="Interchain (with a heavy chain)" FT DISULFID 111 FT /note="Interchain (with a heavy chain)" FT DISULFID 143..203 FT DISULFID 249..307 FT NON_TER 1 FT STRAND 6..10 FT /evidence="ECO:0007829|PDB:1NCW" FT HELIX 14..16 FT /evidence="ECO:0007829|PDB:1NCW" FT STRAND 17..34 FT /evidence="ECO:0007829|PDB:1NCW" FT STRAND 37..40 FT /evidence="ECO:0007829|PDB:1NCW" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:1NCW" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:1NCW" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:1NCW" FT STRAND 60..70 FT /evidence="ECO:0007829|PDB:1NCW" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:1NCW" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:1NCW" FT STRAND 80..85 FT /evidence="ECO:0007829|PDB:1NCW" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:1NCW" FT STRAND 90..95 FT /evidence="ECO:0007829|PDB:1NCW" SQ SEQUENCE 398 AA; 43949 MW; B9CE2EE11224D13B CRC64; KTTAPSVYPL APVCGDTTGS SVTLGCLVKG YFPEPVTLTW NSGSLSSGVH TFPAVLQSDL YTLSSSVTVT SSTWPSQSIT CNVAHPASST KVDKKIEPRG PTIKPCPPCK CPAPNLLGGP SVFIFPPKIK DVLMISLSPI VTCVVVDVSE DDPDVQISWF VNNVEVHTAQ TQTHREDYNS TLRVVSALPI QHQDWMSGKE FKCKVNNKDL PAPIERTISK PKGSVRAPQV YVLPPPEEEM TKKQVTLTCM VTDFMPEDIY VEWTNNGKTE LNYKNTEPVL DSDGSYFMYS KLRVEKKNWV ERNSYSCSVV HEGLHNHHTT KSFSRTPGLD LDDVCAEAQD GELDGLWTTI TIFISLFLLS VCYSASVTLF KVKWIFSSVV ELKQTISPDY RNMIGQGA //