IGG1_HUMAN
ID IGG1_HUMAN Reviewed; 449 AA.
AC P0DOX5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Immunoglobulin gamma-1 heavy chain {ECO:0000305};
DE AltName: Full=Immunoglobulin gamma-1 heavy chain NIE {ECO:0000305|PubMed:826475};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RX PubMed=826475;
RA Ponstingl H., Hilschmann N.;
RT "The rule of antibody structure. The primary structure of a monoclonal IgG1
RT immunoglobulin (myeloma protein Nie). III. The chymotryptic peptides of the
RT H-chain, alignment of the tryptic peptides and discussion of the complete
RT structure.";
RL Hoppe-Seyler's Z. Physiol. Chem. 357:1571-1604(1976).
RN [2]
RP DISULFIDE BOND.
RX PubMed=1002129;
RA Dreker L., Schwarz J., Reichel W., Hilschmann N.;
RT "Rule of antibody structure. The primary structure of a monoclonal IgG1
RT immunoglobulin (myeloma protein Nie), I: purification and characterization
RT of the protein, the L- and H-chains, the cyanogen bromide cleavage
RT products, and the disulfide bridges.";
RL Hoppe-Seyler's Z. Physiol. Chem. 357:1515-1540(1976).
RN [3]
RP REVIEW ON SOMATIC HYPERMUTATION.
RX PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
RA Teng G., Papavasiliou F.N.;
RT "Immunoglobulin somatic hypermutation.";
RL Annu. Rev. Genet. 41:107-120(2007).
RN [4]
RP GLYCOSYLATION AT ASN-299.
RX PubMed=19358553; DOI=10.1021/ac900231w;
RA Thaysen-Andersen M., Mysling S., Hojrup P.;
RT "Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS:
RT strong correlation between signal strength and glycoform quantities.";
RL Anal. Chem. 81:3933-3943(2009).
RN [5]
RP REVIEW ON IMMUNOGLOBULINS.
RX PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
RA Schroeder H.W. Jr., Cavacini L.;
RT "Structure and function of immunoglobulins.";
RL J. Allergy Clin. Immunol. 125:S41-S52(2010).
RN [6]
RP REVIEW ON FUNCTION.
RX PubMed=22158414; DOI=10.1038/nri3128;
RA McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
RT "Molecular programming of B cell memory.";
RL Nat. Rev. Immunol. 12:24-34(2012).
CC -!- FUNCTION: Immunoglobulins, also known as antibodies, are membrane-bound
CC or secreted glycoproteins produced by B lymphocytes. In the recognition
CC phase of humoral immunity, the membrane-bound immunoglobulins serve as
CC receptors which, upon binding of a specific antigen, trigger the clonal
CC expansion and differentiation of B lymphocytes into immunoglobulins-
CC secreting plasma cells. Secreted immunoglobulins mediate the effector
CC phase of humoral immunity, which results in the elimination of bound
CC antigens (PubMed:22158414, PubMed:20176268). The antigen binding site
CC is formed by the variable domain of one heavy chain, together with that
CC of its associated light chain. Thus, each immunoglobulin has two
CC antigen binding sites with remarkable affinity for a particular
CC antigen. The variable domains are assembled by a process called V-(D)-J
CC rearrangement and can then be subjected to somatic hypermutations
CC which, after exposure to antigen and selection, allow affinity
CC maturation for a particular antigen (PubMed:20176268, PubMed:17576170).
CC {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked.
CC {ECO:0000303|PubMed:20176268}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:22158414}. Cell membrane
CC {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
CC -!- CAUTION: This sequence is an example of a full-length immunoglobulin
CC gamma-1 heavy chain. {ECO:0000305}.
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DR PDB; 1N0X; X-ray; 1.80 A; H/K=1-222.
DR PDB; 3PGF; X-ray; 2.10 A; H=1-227.
DR PDB; 4R2G; X-ray; 3.28 A; D/J/N/Q=1-223.
DR PDB; 5O4E; X-ray; 2.15 A; A=227-449, C=227-448.
DR PDB; 5VJ6; EM; 11.50 A; H=3-224.
DR PDB; 5VU0; X-ray; 2.26 A; A/B=230-446.
DR PDB; 5VZX; X-ray; 2.50 A; E/H=1-227.
DR PDB; 5VZY; X-ray; 2.32 A; H=1-227.
DR PDB; 5W5L; X-ray; 1.90 A; A/B=227-449.
DR PDB; 5WAV; X-ray; 2.60 A; A/B=228-448.
DR PDB; 5XJE; X-ray; 2.40 A; A/B=227-449.
DR PDB; 5XJF; X-ray; 2.50 A; A/B=227-449.
DR PDB; 5XMH; X-ray; 2.80 A; A/B=239-446.
DR PDB; 5Y56; X-ray; 2.65 A; A/B=238-445.
DR PDB; 5YC5; X-ray; 2.71 A; A/B=226-448.
DR PDB; 6APD; X-ray; 4.10 A; J/K/N=109-223.
DR PDB; 6ARP; X-ray; 1.70 A; B/D=1-222.
DR PDB; 6ARU; X-ray; 3.20 A; C=1-222.
DR PDB; 6B70; EM; 3.70 A; C/E=1-219.
DR PDB; 6B7Z; EM; 6.50 A; C/E=1-219.
DR PDB; 6BF7; EM; 6.50 A; C/E=1-219.
DR PDB; 6BF9; EM; 7.20 A; C/E=1-219.
DR PDB; 6BFT; X-ray; 2.55 A; A/H=1-227.
DR PDB; 6BGT; X-ray; 2.70 A; B=1-222.
DR PDB; 6BKB; X-ray; 2.80 A; H=2-222.
DR PDB; 6BKC; X-ray; 2.60 A; H=4-222.
DR PDB; 6BZ4; X-ray; 2.40 A; A/B=239-446.
DR PDB; 6DKJ; X-ray; 1.95 A; A/H=1-222.
DR PDB; 6EAQ; X-ray; 2.22 A; A/B=227-446.
DR PDB; 6FCZ; EM; 10.00 A; H/K=234-449.
DR PDB; 6FGO; X-ray; 2.50 A; A/B/C/D=239-448.
DR PDB; 6G1E; X-ray; 1.88 A; B=223-449.
DR PDB; 6IFJ; X-ray; 2.40 A; A/B=218-449.
DR PDB; 6IQG; X-ray; 3.00 A; A/B=238-447.
DR PDB; 6IQH; X-ray; 3.00 A; A/B=238-447.
DR PDB; 6KA7; X-ray; 3.00 A; C/D=240-447.
DR PDB; 6MB3; EM; 3.37 A; A/B/C/D/F/G/H/I/J=1-223.
DR PDB; 6MSY; X-ray; 2.00 A; H=1-221.
DR PDB; 6MU3; X-ray; 2.33 A; H/M=1-221.
DR PDB; 6MUB; X-ray; 2.50 A; H/M=1-222.
DR PDB; 6N2X; X-ray; 3.00 A; H/M=1-220.
DR PDB; 6N32; X-ray; 2.20 A; H/K=1-221.
DR PDB; 6N35; X-ray; 1.75 A; H/M=1-220.
DR PDB; 6OGE; EM; 4.36 A; C=1-222.
DR PDB; 6OKQ; X-ray; 3.20 A; A/D/F=1-226.
DR PDB; 6P6D; X-ray; 2.31 A; A/B=223-449.
DR PDB; 6UBI; X-ray; 1.90 A; A/D=4-226.
DR PDB; 6UGW; X-ray; 2.00 A; A=211-449.
DR PDB; 6UGX; X-ray; 2.10 A; A/B=211-449.
DR PDB; 6UGY; X-ray; 2.10 A; A=211-449.
DR PDB; 6UOE; X-ray; 1.80 A; H=1-223.
DR PDB; 6V8Z; EM; 2.90 A; C/I/O=1-220.
DR PDB; 6VSL; X-ray; 2.10 A; A/B=236-446.
DR PDB; 6VSZ; X-ray; 2.60 A; A/B=236-446.
DR PDB; 6X3I; X-ray; 2.27 A; A=227-449.
DR PDB; 6YSC; X-ray; 2.05 A; A/B=223-449.
DR PDB; 6YT7; X-ray; 1.55 A; A=223-449.
DR PDB; 6YTB; X-ray; 1.65 A; A/B=223-449.
DR PDB; 7CZT; EM; 2.70 A; H/I=99-449.
DR PDB; 7CZU; EM; 3.40 A; H/J=1-5, H/J=99-449.
DR PDB; 7CZV; EM; 3.30 A; H/I/J=1-5, H/I/J=99-449.
DR PDBsum; 1N0X; -.
DR PDBsum; 3PGF; -.
DR PDBsum; 4R2G; -.
DR PDBsum; 5O4E; -.
DR PDBsum; 5VJ6; -.
DR PDBsum; 5VU0; -.
DR PDBsum; 5VZX; -.
DR PDBsum; 5VZY; -.
DR PDBsum; 5W5L; -.
DR PDBsum; 5WAV; -.
DR PDBsum; 5XJE; -.
DR PDBsum; 5XJF; -.
DR PDBsum; 5XMH; -.
DR PDBsum; 5Y56; -.
DR PDBsum; 5YC5; -.
DR PDBsum; 6APD; -.
DR PDBsum; 6ARP; -.
DR PDBsum; 6ARU; -.
DR PDBsum; 6B70; -.
DR PDBsum; 6B7Z; -.
DR PDBsum; 6BF7; -.
DR PDBsum; 6BF9; -.
DR PDBsum; 6BFT; -.
DR PDBsum; 6BGT; -.
DR PDBsum; 6BKB; -.
DR PDBsum; 6BKC; -.
DR PDBsum; 6BZ4; -.
DR PDBsum; 6DKJ; -.
DR PDBsum; 6EAQ; -.
DR PDBsum; 6FCZ; -.
DR PDBsum; 6FGO; -.
DR PDBsum; 6G1E; -.
DR PDBsum; 6IFJ; -.
DR PDBsum; 6IQG; -.
DR PDBsum; 6IQH; -.
DR PDBsum; 6KA7; -.
DR PDBsum; 6MB3; -.
DR PDBsum; 6MSY; -.
DR PDBsum; 6MU3; -.
DR PDBsum; 6MUB; -.
DR PDBsum; 6N2X; -.
DR PDBsum; 6N32; -.
DR PDBsum; 6N35; -.
DR PDBsum; 6OGE; -.
DR PDBsum; 6OKQ; -.
DR PDBsum; 6P6D; -.
DR PDBsum; 6UBI; -.
DR PDBsum; 6UGW; -.
DR PDBsum; 6UGX; -.
DR PDBsum; 6UGY; -.
DR PDBsum; 6UOE; -.
DR PDBsum; 6V8Z; -.
DR PDBsum; 6VSL; -.
DR PDBsum; 6VSZ; -.
DR PDBsum; 6X3I; -.
DR PDBsum; 6YSC; -.
DR PDBsum; 6YT7; -.
DR PDBsum; 6YTB; -.
DR PDBsum; 7CZT; -.
DR PDBsum; 7CZU; -.
DR PDBsum; 7CZV; -.
DR AlphaFoldDB; P0DOX5; -.
DR SMR; P0DOX5; -.
DR CarbonylDB; P0DOX5; -.
DR GlyConnect; 2964; 48 N-Linked glycans.
DR iPTMnet; P0DOX5; -.
DR PhosphoSitePlus; P0DOX5; -.
DR EPD; P0DOX5; -.
DR jPOST; P0DOX5; -.
DR PRIDE; P0DOX5; -.
DR Pharos; P0DOX5; Tdark.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 4.
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; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07654; C1-set; 3.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00407; IGc1; 3.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS00290; IG_MHC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Pyrrolidone carboxylic acid; Repeat;
KW Secreted.
FT CHAIN 1..449
FT /note="Immunoglobulin gamma-1 heavy chain"
FT /id="PRO_0000439287"
FT DOMAIN 1..96
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 125..218
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 240..339
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 348..444
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..119
FT /note="Variable (V) domain, involved in antigen
FT recognition"
FT /evidence="ECO:0000305"
FT REGION 120..449
FT /note="Constant (C) domain"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:826475"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19358553"
FT DISULFID 22..96
FT /evidence="ECO:0000269|PubMed:1002129"
FT DISULFID 146..202
FT /evidence="ECO:0000269|PubMed:1002129"
FT DISULFID 222
FT /note="Interchain (with light chain)"
FT /evidence="ECO:0000269|PubMed:1002129"
FT DISULFID 228
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:1002129"
FT DISULFID 231
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:1002129"
FT DISULFID 263..323
FT /evidence="ECO:0000269|PubMed:1002129"
FT DISULFID 369..427
FT /evidence="ECO:0000269|PubMed:1002129"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:6ARP"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:6ARP"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6V8Z"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:6ARP"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:6ARP"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6ARP"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:6ARP"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:6ARP"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7CZV"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:6ARP"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6UOE"
FT STRAND 141..154
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:6ARP"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:6V8Z"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:6ARP"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6ARP"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:6ARP"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:6ARP"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:6G1E"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:5W5L"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:5O4E"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:6G1E"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:6G1E"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:6G1E"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 362..377
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:6UGW"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:6IQH"
FT STRAND 406..415
FT /evidence="ECO:0007829|PDB:6G1E"
FT HELIX 416..420
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:6G1E"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:6G1E"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:6G1E"
SQ SEQUENCE 449 AA; 49329 MW; A7943E4D7C559ACE CRC64;
QVQLVQSGGG VVQPGRSLRL SCAASGFTFS RYTIHWVRQA PGKGLEWVAV MSYNGNNKHY
ADSVNGRFTI SRNDSKNTLY LNMNSLRPED TAVYYCARIR DTAMFFAHWG QGTLVTVSSA
STKGPSVFPL APSSKSTSGG TAALGCLVKD YFPEPVTVSW NSGALTSGVH TFPAVLQSSG
LYSLSSVVTV PSSSLGTQTY ICNVNHKPSN TKVDKKVEPK SCDKTHTCPP CPAPELLGGP
SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS
TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL
TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ
QGNVFSCSVM HEALHNHYTQ KSLSLSPGK
