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 16-JAN-2019, entry version 137. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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 RT gamma 1 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 RT conserved transmembrane sequence and a 28-residue intracellular RT 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., RA Eisenberg D., Wall R.; RT "Gene segments encoding transmembrane carboxyl termini of RT immunoglobulin 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane 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 Note=May be the major isoform.; 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 UniGene; Mm.342177; -. DR PDB; 15C8; X-ray; 2.50 A; H=2-217. 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=1-218. 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=2-217. 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 ProteinModelPortal; P01869; -. DR SMR; P01869; -. DR IntAct; P01869; 1. DR MINT; P01869; -. DR jPOST; P01869; -. DR MaxQB; P01869; -. DR PRIDE; P01869; -. DR MGI; MGI:96446; Ighg1. DR HOVERGEN; HBG005814; -. DR InParanoid; P01869; -. DR ChiTaRS; Ighg1; mouse. DR EvolutionaryTrace; P01869; -. DR Proteomes; UP000000589; Unplaced. 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; Complete proteome; KW Disulfide bond; Glycoprotein; Immunoglobulin C region; KW Immunoglobulin domain; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN <1 393 Ig gamma-1 chain C region, membrane-bound FT form. FT /FTId=PRO_0000153583. FT TRANSMEM 340 357 Helical. {ECO:0000255}. FT TOPO_DOM 358 393 Cytoplasmic. {ECO:0000255}. FT REGION 1 97 CH1. FT REGION 98 110 Hinge. FT REGION 111 217 CH2. FT REGION 218 324 CH3. FT CARBOHYD 174 174 N-linked (GlcNAc...) asparagine. FT DISULFID 27 82 FT DISULFID 102 102 Interchain (with a light chain). FT DISULFID 104 104 Interchain (with a heavy chain). FT DISULFID 107 107 Interchain (with a heavy chain). FT DISULFID 109 109 Interchain (with a heavy chain). FT DISULFID 138 198 FT DISULFID 244 302 FT NON_TER 1 1 FT STRAND 7 11 {ECO:0000244|PDB:1ORS}. FT HELIX 15 19 {ECO:0000244|PDB:1CIC}. FT STRAND 20 35 {ECO:0000244|PDB:1ORS}. FT STRAND 38 41 {ECO:0000244|PDB:1ORS}. FT HELIX 42 44 {ECO:0000244|PDB:1ORS}. FT STRAND 50 52 {ECO:0000244|PDB:1ORS}. FT STRAND 56 71 {ECO:0000244|PDB:1ORS}. FT TURN 72 77 {ECO:0000244|PDB:1ORS}. FT STRAND 81 86 {ECO:0000244|PDB:1ORS}. FT HELIX 87 89 {ECO:0000244|PDB:1ORS}. FT STRAND 91 96 {ECO:0000244|PDB:1ORS}. FT STRAND 112 114 {ECO:0000244|PDB:1IGY}. FT STRAND 117 120 {ECO:0000244|PDB:1IGY}. FT HELIX 124 128 {ECO:0000244|PDB:1IGY}. FT STRAND 135 140 {ECO:0000244|PDB:1IGY}. FT STRAND 154 158 {ECO:0000244|PDB:1IGY}. FT STRAND 174 176 {ECO:0000244|PDB:1IGY}. FT HELIX 187 192 {ECO:0000244|PDB:1IGY}. FT STRAND 226 228 {ECO:0000244|PDB:1IGY}. FT STRAND 232 250 {ECO:0000244|PDB:1IGY}. FT STRAND 254 260 {ECO:0000244|PDB:1IGY}. FT STRAND 277 279 {ECO:0000244|PDB:1IGY}. FT STRAND 281 290 {ECO:0000244|PDB:1IGY}. FT HELIX 291 295 {ECO:0000244|PDB:1IGY}. FT STRAND 300 306 {ECO:0000244|PDB:1IGY}. FT HELIX 310 312 {ECO:0000244|PDB:1IGY}. FT STRAND 314 318 {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 //