ID IGH1M_MOUSE Reviewed; 393 AA. AC P01869; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 2. DT 12-AUG-2020, entry version 142. DE RecName: Full=Ig gamma-1 chain C region, membrane-bound 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 323-393. RX PubMed=6804950; DOI=10.1073/pnas.79.6.2008; RA Tyler B.M., Cowman A.F., Gerondakis S.D., Adams J.M., Bernard O.; RT "mRNA for surface immunoglobulin gamma chains encodes a highly conserved RT transmembrane sequence and a 28-residue intracellular domain."; RL Proc. Natl. Acad. Sci. U.S.A. 79:2008-2012(1982). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 323-366. 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44. 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 [5] 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: 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=P01869-1; Sequence=Displayed; CC Name=Secreted; CC IsoId=P01868-1; 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; J00453; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; B02159; G1MSM. DR PDB; 15C8; X-ray; 2.50 A; H=1-98. DR PDB; 1A0Q; X-ray; 2.30 A; H=1-97. DR PDB; 1A3L; X-ray; 1.95 A; H=1-99. DR PDB; 1ACY; X-ray; 3.00 A; H=1-100. DR PDB; 1AE6; X-ray; 3.00 A; H=1-98. DR PDB; 1C12; X-ray; 2.60 A; B=1-99. DR PDB; 1CIC; X-ray; 2.50 A; D=1-102. DR PDB; 1CK0; X-ray; 2.50 A; H=1-98. DR PDB; 1CL7; X-ray; 3.00 A; I=21-102. DR PDB; 1F11; X-ray; 3.00 A; B/D=1-102. DR PDB; 1F58; X-ray; 2.00 A; H=1-102. DR PDB; 1IGY; X-ray; 3.20 A; B/D=1-320. DR PDB; 1JRH; X-ray; 2.80 A; H=1-97. DR PDB; 1KC5; X-ray; 2.50 A; H=1-101. DR PDB; 1KCR; X-ray; 2.90 A; H=1-102. DR PDB; 1KCU; X-ray; 2.20 A; H=1-101. DR PDB; 1KEN; X-ray; 3.50 A; H/T=1-101. DR PDB; 1ORS; X-ray; 1.90 A; B=1-103. DR PDB; 1QFU; X-ray; 2.80 A; H=1-101. DR PDB; 1S5I; X-ray; 2.70 A; H=1-102. DR PDB; 25C8; X-ray; 2.00 A; H=1-98. DR PDB; 2AJS; X-ray; 1.70 A; H=1-100. DR PDB; 2AJU; X-ray; 1.50 A; H=1-100. DR PDB; 2AJV; X-ray; 1.50 A; H=1-100. DR PDB; 2AJX; X-ray; 1.85 A; H=1-100. DR PDB; 2AJY; X-ray; 2.10 A; H=1-100. DR PDB; 2AJZ; X-ray; 2.30 A; B/H=1-100. DR PDB; 2AK1; X-ray; 1.85 A; H=1-100. DR PDBsum; 15C8; -. DR PDBsum; 1A0Q; -. DR PDBsum; 1A3L; -. DR PDBsum; 1ACY; -. DR PDBsum; 1AE6; -. DR PDBsum; 1C12; -. DR PDBsum; 1CIC; -. DR PDBsum; 1CK0; -. DR PDBsum; 1CL7; -. DR PDBsum; 1F11; -. DR PDBsum; 1F58; -. DR PDBsum; 1IGY; -. DR PDBsum; 1JRH; -. DR PDBsum; 1KC5; -. DR PDBsum; 1KCR; -. DR PDBsum; 1KCU; -. DR PDBsum; 1KEN; -. DR PDBsum; 1ORS; -. DR PDBsum; 1QFU; -. DR PDBsum; 1S5I; -. DR PDBsum; 25C8; -. DR PDBsum; 2AJS; -. DR PDBsum; 2AJU; -. DR PDBsum; 2AJV; -. DR PDBsum; 2AJX; -. DR PDBsum; 2AJY; -. DR PDBsum; 2AJZ; -. DR PDBsum; 2AK1; -. DR SMR; P01869; -. DR IntAct; P01869; 1. DR MINT; P01869; -. DR GlyGen; P01869; 1 site, 4 N-linked glycans (1 site). DR CPTAC; non-CPTAC-3532; -. DR CPTAC; non-CPTAC-3533; -. DR MaxQB; P01869; -. DR PRIDE; P01869; -. DR MGI; MGI:96446; Ighg1. DR InParanoid; P01869; -. 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; Ighg1; mouse. DR EvolutionaryTrace; P01869; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P01869; protein. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005615; C:extracellular space; IDA: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:0034987; F:immunoglobulin receptor binding; IPI:AgBase. DR GO; GO:0019731; P:antibacterial humoral response; IDA:MGI. DR GO; GO:0001788; P:antibody-dependent cellular cytotoxicity; IDA: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; Cell membrane; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN <1..393 FT /note="Ig gamma-1 chain C region, membrane-bound form" FT /id="PRO_0000153583" FT TRANSMEM 340..357 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 358..393 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" 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 DISULFID 27..82 FT DISULFID 102 FT /note="Interchain (with a light chain)" FT DISULFID 104 FT /note="Interchain (with a heavy chain)" FT DISULFID 107 FT /note="Interchain (with a heavy chain)" FT DISULFID 109 FT /note="Interchain (with a heavy chain)" FT DISULFID 138..198 FT DISULFID 244..302 FT NON_TER 1 FT STRAND 7..11 FT /evidence="ECO:0000244|PDB:1ORS" FT HELIX 15..19 FT /evidence="ECO:0000244|PDB:1CIC" FT STRAND 20..35 FT /evidence="ECO:0000244|PDB:1ORS" FT STRAND 38..41 FT /evidence="ECO:0000244|PDB:1ORS" FT HELIX 42..44 FT /evidence="ECO:0000244|PDB:1ORS" FT STRAND 50..52 FT /evidence="ECO:0000244|PDB:1ORS" FT STRAND 56..71 FT /evidence="ECO:0000244|PDB:1ORS" FT TURN 72..77 FT /evidence="ECO:0000244|PDB:1ORS" FT STRAND 81..86 FT /evidence="ECO:0000244|PDB:1ORS" FT HELIX 87..89 FT /evidence="ECO:0000244|PDB:1ORS" FT STRAND 91..96 FT /evidence="ECO:0000244|PDB:1ORS" FT STRAND 112..114 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 117..120 FT /evidence="ECO:0000244|PDB:1IGY" FT HELIX 124..128 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 135..140 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 154..158 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 174..176 FT /evidence="ECO:0000244|PDB:1IGY" FT HELIX 187..192 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 226..228 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 232..250 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 254..260 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 277..279 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 281..290 FT /evidence="ECO:0000244|PDB:1IGY" FT HELIX 291..295 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 300..306 FT /evidence="ECO:0000244|PDB:1IGY" FT HELIX 310..312 FT /evidence="ECO:0000244|PDB:1IGY" FT STRAND 314..318 FT /evidence="ECO:0000244|PDB:1IGY" SQ SEQUENCE 393 AA; 43387 MW; 4CC88343B7A1CE27 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 SPGLQLDETC AEAQDGELDG LWTTITIFIS LFLLSVCYSA AVTLFKVKWI FSSVVELKQT LVPEYKNMIG QAP //