IGH1M_MOUSE
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 03-AUG-2022, entry version 148.
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;
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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 AlphaFoldDB; P01869; -.
DR SMR; P01869; -.
DR GlyGen; P01869; 1 site, 7 N-linked glycans (1 site).
DR CPTAC; non-CPTAC-3532; -.
DR CPTAC; non-CPTAC-3533; -.
DR MaxQB; P01869; -.
DR PRIDE; P01869; -.
DR ProteomicsDB; 269383; -. [P01869-1]
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:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
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; 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:0030183; P:B cell differentiation; IMP: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:0007829|PDB:1ORS"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:1CIC"
FT STRAND 20..35
FT /evidence="ECO:0007829|PDB:1ORS"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1ORS"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1ORS"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1ORS"
FT STRAND 56..71
FT /evidence="ECO:0007829|PDB:1ORS"
FT TURN 72..77
FT /evidence="ECO:0007829|PDB:1ORS"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1ORS"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1ORS"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1ORS"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1IGY"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1IGY"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 232..250
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:1IGY"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:1IGY"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:1IGY"
FT STRAND 314..318
FT /evidence="ECO:0007829|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
