IGK_HUMAN
ID IGK_HUMAN Reviewed; 214 AA.
AC P0DOX7;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Immunoglobulin kappa light chain {ECO:0000305};
DE AltName: Full=Immunoglobulin kappa light chain EU {ECO:0000305|PubMed:5489770};
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.
RX PubMed=5489770; DOI=10.1021/bi00818a007;
RA Gottlieb P.D., Cunningham B.A., Rutishauser U., Edelman G.M.;
RT "The covalent structure of a human gamma G-immunoglobulin. VI. Amino acid
RT sequence of the light chain.";
RL Biochemistry 9:3155-3161(1970).
RN [2]
RP DISULFIDE BONDS.
RX PubMed=4923144; DOI=10.1021/bi00818a011;
RA Gall W.E., Edelman G.M.;
RT "The covalent structure of a human gamma G-immunoglobulin. X. Intrachain
RT disulfide bonds.";
RL Biochemistry 9:3188-3196(1970).
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 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 [5]
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 kappa light chain. {ECO:0000305}.
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DR PDB; 5VIC; X-ray; 3.00 A; L=1-214.
DR PDB; 5VIG; X-ray; 3.00 A; B/L=1-214.
DR PDB; 5W1K; X-ray; 3.99 A; A/F/K/S=2-212.
DR PDB; 6BF7; EM; 6.50 A; D/F=1-211.
DR PDB; 6BF9; EM; 7.20 A; D/F=1-211.
DR PDB; 6MSY; X-ray; 2.00 A; L=1-213.
DR PDB; 6MU3; X-ray; 2.33 A; K/L=1-213.
DR PDB; 6MUB; X-ray; 2.50 A; K/L=1-213.
DR PDB; 6N2X; X-ray; 3.00 A; K/L=1-213.
DR PDB; 6N32; X-ray; 2.20 A; L/M=1-213.
DR PDB; 6N35; X-ray; 1.75 A; K/L=1-213.
DR PDB; 6NQD; EM; 3.90 A; D/H/L=1-214.
DR PDB; 6UOE; X-ray; 1.80 A; L=1-214.
DR PDB; 6UTA; X-ray; 3.10 A; B/L=1-214.
DR PDB; 6UTE; X-ray; 2.90 A; B/D/F/H/J=1-214.
DR PDBsum; 5VIC; -.
DR PDBsum; 5VIG; -.
DR PDBsum; 5W1K; -.
DR PDBsum; 6BF7; -.
DR PDBsum; 6BF9; -.
DR PDBsum; 6MSY; -.
DR PDBsum; 6MU3; -.
DR PDBsum; 6MUB; -.
DR PDBsum; 6N2X; -.
DR PDBsum; 6N32; -.
DR PDBsum; 6N35; -.
DR PDBsum; 6NQD; -.
DR PDBsum; 6UOE; -.
DR PDBsum; 6UTA; -.
DR PDBsum; 6UTE; -.
DR AlphaFoldDB; P0DOX7; -.
DR SMR; P0DOX7; -.
DR CarbonylDB; P0DOX7; -.
DR jPOST; P0DOX7; -.
DR PRIDE; P0DOX7; -.
DR SIGNOR; P0DOX7; -.
DR Pharos; P0DOX7; 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; -; 2.
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; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Repeat; Secreted.
FT CHAIN 1..214
FT /note="Immunoglobulin kappa light chain"
FT /id="PRO_0000439288"
FT DOMAIN 2..99
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 113..210
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..108
FT /note="Variable (V) domain, involved in antigen
FT recognition"
FT /evidence="ECO:0000305"
FT REGION 109..214
FT /note="Constant (C) domain"
FT /evidence="ECO:0000305"
FT DISULFID 23..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4923144"
FT DISULFID 134..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:4923144"
FT DISULFID 214
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000269|PubMed:4923144"
FT NON_TER 1
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6N35"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:6N35"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:6UTE"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:6N35"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 129..142
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:6N35"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:6N35"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:6N35"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6UOE"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6N35"
SQ SEQUENCE 214 AA; 23379 MW; 8DF29E176EFE0BB4 CRC64;
DIQMTQSPST LSASVGDRVT ITCRASQSIN TWLAWYQQKP GKAPKLLMYK ASSLESGVPS
RFIGSGSGTE FTLTISSLQP DDFATYYCQQ YNSDSKMFGQ GTKVEVKGTV AAPSVFIFPP
SDEQLKSGTA SVVCLLNNFY PREAKVQWKV DNALQSGNSQ ESVTEQDSKD STYSLSSTLT
LSKADYEKHK VYACEVTHQG LSSPVTKSFN RGEC
