IGHG1_RAT
ID IGHG1_RAT Reviewed; 326 AA.
AC P20759;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ig gamma-1 chain C region;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3149946; DOI=10.1016/0378-1119(88)90180-1;
RA Brueggemann M.;
RT "Evolution of the rat immunoglobulin gamma heavy-chain gene family.";
RL Gene 74:473-482(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 220-326.
RX PubMed=3016742; DOI=10.1073/pnas.83.16.6075;
RA Bruggemann M., Free J., Diamond A., Howard J., Cobbold S., Waldmann H.;
RT "Immunoglobulin heavy chain locus of the rat: striking homology to mouse
RT antibody genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6075-6079(1986).
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DR PIR; PS0017; PS0017.
DR PDB; 1LK3; X-ray; 1.91 A; H/I=1-100.
DR PDBsum; 1LK3; -.
DR AlphaFoldDB; P20759; -.
DR SMR; P20759; -.
DR MINT; P20759; -.
DR STRING; 10116.ENSRNOP00000006975; -.
DR GlyGen; P20759; 1 site.
DR PaxDb; P20759; -.
DR PRIDE; P20759; -.
DR ABCD; P20759; 6 sequenced antibodies.
DR Ensembl; ENSRNOT00000006975; ENSRNOP00000006975; ENSRNOG00000030332.
DR eggNOG; ENOG502R54U; Eukaryota.
DR GeneTree; ENSGT00940000163307; -.
DR HOGENOM; CLU_030625_0_2_1; -.
DR InParanoid; P20759; -.
DR PhylomeDB; P20759; -.
DR Reactome; R-RNO-166663; Initial triggering of complement.
DR Reactome; R-RNO-173623; Classical antibody-mediated complement activation.
DR Reactome; R-RNO-2029481; FCGR activation.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR EvolutionaryTrace; P20759; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000030332; Expressed in spleen and 8 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
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; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Reference proteome.
FT CHAIN <1..326
FT /note="Ig gamma-1 chain C region"
FT /id="PRO_0000153591"
FT REGION 1..97
FT /note="CH1"
FT REGION 98..112
FT /note="Hinge"
FT REGION 113..219
FT /note="CH2"
FT REGION 220..326
FT /note="CH3"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 102
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 106
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 109
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 111
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 140..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 246..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1LK3"
FT STRAND 21..35
FT /evidence="ECO:0007829|PDB:1LK3"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1LK3"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1LK3"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1LK3"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1LK3"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:1LK3"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1LK3"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1LK3"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1LK3"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1LK3"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1LK3"
SQ SEQUENCE 326 AA; 35946 MW; 013BAB45EF49B9DA CRC64;
AETTAPSVYP LAPGTALKSN SMVTLGCLVK GYFPEPVTVT WNSGALSSGV HTFPAVLQSG
LYTLTSSVTV PSSTWPSQTV TCNVAHPASS TKVDKKIVPR NCGGDCKPCI CTGSEVSSVF
IFPPKPKDVL TITLTPKVTC VVVDISQDDP EVHFSWFVDD VEVHTAQTRP PEEQFNSTFR
SVSELPILHQ DWLNGRTFRC KVTSAAFPSP IEKTISKPEG RTQVPHVYTM SPTKEEMTQN
EVSITCMVKG FYPPDIYVEW QMNGQPQENY KNTPPTMDTD GSYFLYSKLN VKKEKWQQGN
TFTCSVLHEG LHNHHTEKSL SHSPGK
