ID IGHG3_HUMAN Reviewed; 377 AA. AC P01860; A2NU35; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 2. DT 03-APR-2013, entry version 116. DE RecName: Full=Ig gamma-3 chain C region; DE AltName: Full=HDC; DE AltName: Full=Heavy chain disease protein; GN Name=IGHG3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3081877; DOI=10.1093/nar/14.4.1779; RA Huck S., Fort P., Crawford D.H., Lefranc M.-P., Lefranc G.; RT "Sequence of a human immunoglobulin gamma 3 heavy chain constant RT region gene: comparison with the other human C gamma genes."; RL Nucleic Acids Res. 14:1779-1789(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., RA Quetier F., Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [3] RP PROTEIN SEQUENCE (VARIANT WIS), AND SUBUNIT. RX PubMed=6774747; DOI=10.1021/bi00559a024; RA Frangione B., Rosenwasser E., Prelli F., Franklin E.C.; RT "Primary structure of human gamma 3 immunoglobulin deletion mutant: RT gamma 3 heavy-chain disease protein Wis."; RL Biochemistry 19:4304-4308(1980). RN [4] RP SEQUENCE REVISION TO 146-376 (VARIANT WIS/VARIANT ZUC). RX PubMed=402363; RA Michaelsen T.E., Frangione B., Franklin E.C.; RT "Primary structure of the 'hinge' region of human IgG3. Probable RT quadruplication of a 15-amino acid residue basic unit."; RL J. Biol. Chem. 252:883-889(1977). RN [5] RP SEQUENCE REVISION TO 59-289 (VARIANT WIS/VARIANT ZUC). RX PubMed=823945; DOI=10.1016/0006-291X(76)90741-5; RA Wolfenstein-Todel C., Frangione B., Prelli F., Franklin E.C.; RT "The amino acid sequence of 'heavy chain disease' protein ZUC. RT Structure of the Fc fragment of immunoglobulin G3."; RL Biochem. Biophys. Res. Commun. 71:907-914(1976). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-377 (VARIANT OMM). RX PubMed=6808505; DOI=10.1073/pnas.79.10.3260; RA Alexander A., Steinmetz M., Barritault D., Frangione B., RA Franklin E.C., Hood L., Buxbaum J.N.; RT "Gamma heavy chain disease in man: cDNA sequence supports partial gene RT deletion model."; RL Proc. Natl. Acad. Sci. U.S.A. 79:3260-3264(1982). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-59. RX PubMed=6811139; DOI=10.1016/0092-8674(82)90183-0; RA Takahashi N., Ueda S., Obata M., Nikaido T., Nakai S., Honjo T.; RT "Structure of human immunoglobulin gamma genes: implications for RT evolution of a gene family."; RL Cell 29:671-679(1982). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227 AND ASN-322, AND MASS RP SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- POLYMORPHISM: The IGHG3 gene shows a structural polymorphism CC characterized by different hinge lengths. Variant WIS is lacking CC most of the V region and all of the CH1 region. It has an extra CC interchain disulfide bond at position 7 in addition to the 11 CC normally present in the hinge region. Variant ZUC lackS most of CC the V region, all of the CH1 region, and part of the hinge. CC Variant OMM may represent an allelic form or another gamma chain CC subclass. CC -!- MISCELLANEOUS: The hinge region in gamma-3 chains is about four CC times as long as in other gamma chains and contains three CC identical 15-residue segments preceded by a similar 17-residue CC segment (12-28). CC -!- WEB RESOURCE: Name=IMGT/GENE-DB; CC URL="http://www.imgt.org/IMGT_GENE-DB/GENElect?query=2+IGHG3&species=Homo+sapiens"; 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; X03604; CAA27268.1; -; Genomic_DNA. DR EMBL; AL122127; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; J00231; AAA52805.1; ALT_SEQ; mRNA. DR IPI; IPI00973474; -. DR PIR; A23511; A23511. DR PIR; A90442; G3HUWI. DR UniGene; Hs.510635; -. DR ProteinModelPortal; P01860; -. DR SMR; P01860; 1-377. DR MINT; MINT-1135282; -. DR STRING; 9606.ENSP00000374992; -. DR DMDM; 193806361; -. DR UCD-2DPAGE; P01860; -. DR PaxDb; P01860; -. DR PRIDE; P01860; -. DR GeneCards; GC14M106231; -. DR HGNC; HGNC:5527; IGHG3. DR MIM; 147120; gene. DR neXtProt; NX_P01860; -. DR eggNOG; NOG313034; -. DR HOVERGEN; HBG005814; -. DR Pathway_Interaction_DB; il4_2pathway; IL4-mediated signaling events. DR Reactome; REACT_6900; Immune System. DR Genevestigator; P01860; -. DR GermOnline; ENSG00000130076; Homo sapiens. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0003823; F:antigen binding; IEA:UniProtKB-KW. DR GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR Pfam; PF07654; C1-set; 3. DR SMART; SM00407; IGc1; 2. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00290; IG_MHC; 2. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Immunoglobulin C region; Immunoglobulin domain; KW Polymorphism; Reference proteome; Repeat; Secreted. FT CHAIN 1 377 Ig gamma-3 chain C region. FT /FTId=PRO_0000153580. FT REPEAT 116 130 FT REPEAT 131 145 FT REPEAT 146 160 FT REGION 1 98 CH1. FT REGION 99 160 Hinge. FT REGION 161 270 CH2. FT REGION 271 376 CH3. FT CARBOHYD 227 227 N-linked (GlcNAc...). FT CARBOHYD 322 322 N-linked (GlcNAc...). FT DISULFID 27 83 FT DISULFID 111 111 Interchain (with heavy chain dimer). FT DISULFID 114 114 Interchain (with heavy chain dimer). FT DISULFID 120 120 Interchain (with heavy chain dimer). FT DISULFID 126 126 Interchain (with heavy chain dimer). FT DISULFID 129 129 Interchain (with heavy chain dimer). FT DISULFID 135 135 Interchain (with heavy chain dimer). FT DISULFID 141 141 Interchain (with heavy chain dimer). FT DISULFID 144 144 Interchain (with heavy chain dimer). FT DISULFID 150 150 Interchain (with heavy chain dimer). FT DISULFID 156 156 Interchain (with heavy chain dimer). FT DISULFID 159 159 Interchain (with heavy chain dimer). FT VARIANT 1 76 Missing (in variant WIS). FT /FTId=VAR_068695. FT VARIANT 77 98 GTQTYTCNVNHKPSNTKVDKRV -> QMQGVNCTVSS (in FT variant WIS). FT /FTId=VAR_068696. FT VARIANT 213 213 E -> Q (in variant WIS). FT /FTId=VAR_068697. FT VARIANT 214 214 V -> B (in variant ZUC). FT /FTId=VAR_003890. FT VARIANT 221 221 P -> L (in variant OMM). FT /FTId=VAR_003891. FT VARIANT 224 224 E -> Q (in variant WIS). FT /FTId=VAR_068698. FT VARIANT 226 226 Y -> F (in variant ZUC and WIS). FT /FTId=VAR_003892. FT VARIANT 242 242 D -> N (in variant WIS). FT /FTId=VAR_068699. FT VARIANT 245 245 N -> D (in variant WIS). FT /FTId=VAR_068700. FT VARIANT 269 269 T -> A (in variant OMM). FT /FTId=VAR_003893. FT VARIANT 314 314 S -> N (in variant OMM). FT /FTId=VAR_003894. FT VARIANT 314 314 Missing (in variant ZUC). FT /FTId=VAR_003895. FT VARIANT 366 366 F -> Y (in variant OMM). FT /FTId=VAR_003896. SQ SEQUENCE 377 AA; 41287 MW; FEB7F537953F807F CRC64; ASTKGPSVFP LAPCSRSTSG GTAALGCLVK DYFPEPVTVS WNSGALTSGV HTFPAVLQSS GLYSLSSVVT VPSSSLGTQT YTCNVNHKPS NTKVDKRVEL KTPLGDTTHT CPRCPEPKSC DTPPPCPRCP EPKSCDTPPP CPRCPEPKSC DTPPPCPRCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVQFKWYVD GVEVHNAKTK PREEQYNSTF RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKTK GQPREPQVYT LPPSREEMTK NQVSLTCLVK GFYPSDIAVE WESSGQPENN YNTTPPMLDS DGSFFLYSKL TVDKSRWQQG NIFSCSVMHE ALHNRFTQKS LSLSPGK //