IGL1_HUMAN
ID IGL1_HUMAN Reviewed; 216 AA.
AC P0DOX8;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Immunoglobulin lambda-1 light chain {ECO:0000305};
DE AltName: Full=Immunoglobulin lambda-1 light chain MCG {ECO:0000305|PubMed:4415202};
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=4415202; DOI=10.1021/bi00717a007;
RA Fett J.W., Deutsch H.F.;
RT "Primary structure of the Mcg lambda chain.";
RL Biochemistry 13:4102-4114(1974).
RN [2]
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 [3]
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 [4]
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 lambda-1 light chain. {ECO:0000305}.
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DR PDB; 1MCD; X-ray; -; A/B=2-216.
DR PDBsum; 1MCD; -.
DR AlphaFoldDB; P0DOX8; -.
DR SMR; P0DOX8; -.
DR IntAct; P0DOX8; 1.
DR GlyConnect; 226; 2 N-Linked glycans (1 site), 2 O-Linked glycans (1 site).
DR jPOST; P0DOX8; -.
DR PRIDE; P0DOX8; -.
DR PathwayCommons; P0DOX8; -.
DR SIGNOR; P0DOX8; -.
DR Pharos; P0DOX8; 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 Pyrrolidone carboxylic acid; Secreted.
FT CHAIN 1..216
FT /note="Immunoglobulin lambda-1 light chain"
FT /id="PRO_0000439289"
FT DOMAIN 1..108
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 117..211
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..111
FT /note="Variable (V) domain, involved in antigen
FT recognition"
FT /evidence="ECO:0000305"
FT REGION 112..216
FT /note="Constant (C) domain"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:4415202"
FT DISULFID 22..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 138..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 215
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:1MCD"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1MCD"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 134..146
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:1MCD"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:1MCD"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:1MCD"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:1MCD"
SQ SEQUENCE 216 AA; 22830 MW; 6B8F588742273FDA CRC64;
QSALTQPPSA SGSLGQSVTI SCTGTSSDVG GYNYVSWYQQ HAGKAPKVII YEVNKRPSGV
PDRFSGSKSG NTASLTVSGL QAEDEADYYC SSYEGSDNFV FGTGTKVTVL GQPKANPTVT
LFPPSSEELQ ANKATLVCLI SDFYPGAVTV AWKADGSPVK AGVETTKPSK QSNNKYAASS
YLSLTPEQWK SHRSYSCQVT HEGSTVEKTV APTECS
