IGLC2_HUMAN
ID IGLC2_HUMAN Reviewed; 106 AA.
AC P0DOY2; A0A075B6K9; A0M8Q4; P0CG05; P0CG06; P80423;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Immunoglobulin lambda constant 2 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.11};
DE AltName: Full=Ig lambda chain C region Kern {ECO:0000305|PubMed:5549568};
DE AltName: Full=Ig lambda chain C region NIG-64 {ECO:0000305|PubMed:6404900};
DE AltName: Full=Ig lambda chain C region SH {ECO:0000305|PubMed:4909564};
DE AltName: Full=Ig lambda chain C region X {ECO:0000305|PubMed:4883841};
DE AltName: Full=Ig lambda-2 chain C region {ECO:0000305};
GN Name=IGLC2 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.11};
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 DISULFIDE BONDS.
RX PubMed=4883841; DOI=10.1042/bj1100631;
RA Milstein C., Clegg J.B., Jarvis J.M.;
RT "Immunoglobulin lambda-chains. The complete amino acid sequence of a Bence-
RT Jones protein.";
RL Biochem. J. 110:631-652(1968).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=4909564; DOI=10.1016/s0021-9258(18)63220-x;
RA Titani K., Wikler M., Shinoda T., Putnam F.W.;
RT "The amino acid sequence of a lambda type Bence-Jones protein. 3. The
RT complete amino acid sequence and the location of the disulfide bridges.";
RL J. Biol. Chem. 245:2171-2176(1970).
RN [3]
RP PROTEIN SEQUENCE.
RX PubMed=5549568;
RA Ponstingl H., Hess M., Hilschmann N.;
RT "Structural rule of antibodies. Primary structure of a monoclonal
RT immunoglobulin-L-chain of the lambda type, subgroup IV (Bence-Jones-protein
RT Kern). V. The complete amino acid sequence and its genetic
RT interpretation.";
RL Hoppe-Seyler's Z. Physiol. Chem. 352:247-266(1971).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC2*01).
RX PubMed=6273747; DOI=10.1038/294536a0;
RA Hieter P.A., Hollis G.F., Korsmeyer S.J., Waldmann T.A., Leder P.;
RT "Clustered arrangement of immunoglobulin lambda constant region genes in
RT man.";
RL Nature 294:536-540(1981).
RN [5]
RP PROTEIN SEQUENCE.
RX PubMed=6404900; DOI=10.1093/oxfordjournals.jbchem.a134196;
RA Kametani F., Takayasu T., Suzuki S., Shinoda T., Okuyama T., Shimizu A.;
RT "Comparative studies on the structure of the light chains of human
RT immunoglobulins. IV. Assignment of a subsubgroup.";
RL J. Biochem. 93:421-429(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC2*02).
RX PubMed=2115572; DOI=10.1084/jem.172.2.609;
RA Vasicek T.J., Leder P.;
RT "Structure and expression of the human immunoglobulin lambda genes.";
RL J. Exp. Med. 172:609-620(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGLC2*02).
RX PubMed=9074928; DOI=10.1101/gr.7.3.250;
RA Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A.,
RA Schmeits J.L., Wang J., Shimizu N.;
RT "One-megabase sequence analysis of the human immunoglobulin lambda gene
RT locus.";
RL Genome Res. 7:250-261(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC2*02).
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGLC2*02).
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NOMENCLATURE.
RX PubMed=11872955; DOI=10.1159/000049203;
RA Lefranc M.P.;
RT "Nomenclature of the human immunoglobulin lambda (IGL) genes.";
RL Exp. Clin. Immunogenet. 18:242-254(2001).
RN [11]
RP NOMENCLATURE.
RA Lefranc M.P., Lefranc G.;
RT "The Immunoglobulin FactsBook.";
RL (In) Lefranc M.P., Lefranc G. (eds.);
RL The Immunoglobulin FactsBook., pp.1-458, Academic Press, London. (2001).
RN [12]
RP SEROLOGICAL ISOTYPE.
RA Lefranc M.-P., Lefranc G.;
RT "Immunoglobulin lambda (IGL) genes of human and mouse.";
RL (In) Honjo T., Alt F.W., Neuberger M. (eds.);
RL Molecular Biology of B Cells, pp.37-59, Elsevier Academic Press, London
RL (2004).
RN [13]
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 [14]
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 [15]
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: Constant region of immunoglobulin light chains.
CC Immunoglobulins, also known as antibodies, are membrane-bound or
CC 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:17576170, PubMed:20176268).
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 -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele IGLC2*02. {ECO:0000305}.
CC -!- MISCELLANEOUS: Displays the following serological isotype: Mcg-,
CC Kern- and Oz-. The Mcg- isotype marker is characterized by Ala-6, Ser-8
CC and Thr-57; the Ke- marker by Ser-46 and the Oz- marker by Arg-83.
CC {ECO:0000303|Ref.12}.
CC -!- CAUTION: For an example of a full-length immunoglobulin lambda light
CC chain see AC P0DOX8. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA59107.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA20026.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA36049.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB38569.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW59547.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW59549.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J00253; AAA59107.1; ALT_INIT; Genomic_DNA.
DR EMBL; X51754; CAB38569.1; ALT_INIT; Genomic_DNA.
DR EMBL; X51755; CAA36049.1; ALT_INIT; Genomic_DNA.
DR EMBL; D87023; BAA20026.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC245028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59547.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471095; EAW59549.1; ALT_INIT; Genomic_DNA.
DR PIR; A92057; L2HU.
DR PDB; 1JVK; X-ray; 1.94 A; B=1-105.
DR PDB; 1LIL; X-ray; 2.65 A; A/B=1-106.
DR PDB; 1ZVO; X-ray; -; A/B=2-106.
DR PDB; 2JB5; X-ray; 2.80 A; L=1-104.
DR PDB; 2JB6; X-ray; 2.85 A; A/L=1-104.
DR PDB; 3C2A; X-ray; 2.10 A; L/M=2-105.
DR PDB; 3TV3; X-ray; 1.29 A; L=1-106.
DR PDB; 3TWC; X-ray; 1.65 A; L=1-106.
DR PDB; 3TYG; X-ray; 3.25 A; L=1-106.
DR PDB; 4EOW; X-ray; 1.97 A; L=1-106.
DR PDB; 4LLD; X-ray; 1.19 A; B=1-105.
DR PDB; 4LLM; X-ray; 1.75 A; B=1-105.
DR PDB; 4LLQ; X-ray; 1.42 A; B=1-105.
DR PDB; 4LLU; X-ray; 2.16 A; B/D=1-105.
DR PDB; 4LLW; X-ray; 1.95 A; B/D=1-105.
DR PDB; 4LLY; X-ray; 1.60 A; B/D=1-105.
DR PDB; 4O58; X-ray; 2.75 A; L=1-106.
DR PDB; 4O5I; X-ray; 6.50 A; N/P/R/T/V/X=1-106.
DR PDB; 5IQ7; X-ray; 3.29 A; L=1-104.
DR PDB; 5IQ9; X-ray; 2.40 A; B/L=1-102.
DR PDB; 6DE7; X-ray; 4.12 A; L=1-106.
DR PDB; 6UMX; X-ray; 2.79 A; L/l=1-106.
DR PDBsum; 1JVK; -.
DR PDBsum; 1LIL; -.
DR PDBsum; 1ZVO; -.
DR PDBsum; 2JB5; -.
DR PDBsum; 2JB6; -.
DR PDBsum; 3C2A; -.
DR PDBsum; 3TV3; -.
DR PDBsum; 3TWC; -.
DR PDBsum; 3TYG; -.
DR PDBsum; 4EOW; -.
DR PDBsum; 4LLD; -.
DR PDBsum; 4LLM; -.
DR PDBsum; 4LLQ; -.
DR PDBsum; 4LLU; -.
DR PDBsum; 4LLW; -.
DR PDBsum; 4LLY; -.
DR PDBsum; 4O58; -.
DR PDBsum; 4O5I; -.
DR PDBsum; 5IQ7; -.
DR PDBsum; 5IQ9; -.
DR PDBsum; 6DE7; -.
DR PDBsum; 6UMX; -.
DR AlphaFoldDB; P0DOY2; -.
DR SMR; P0DOY2; -.
DR IMGT_GENE-DB; IGLC2; -.
DR CarbonylDB; P0DOY2; -.
DR BioMuta; IGLC2; -.
DR jPOST; P0DOY2; -.
DR MassIVE; P0DOY2; -.
DR MaxQB; P0DOY2; -.
DR PeptideAtlas; P0DOY2; -.
DR PRIDE; P0DOY2; -.
DR Ensembl; ENST00000390323.2; ENSP00000374856.2; ENSG00000211677.2.
DR GeneCards; IGLC2; -.
DR HGNC; HGNC:5856; IGLC2.
DR HPA; ENSG00000211677; Tissue enhanced (intestine, lymphoid tissue, stomach).
DR neXtProt; NX_P0DOY2; -.
DR VEuPathDB; HostDB:ENSG00000211677; -.
DR PathwayCommons; P0DOY2; -.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-2029481; FCGR activation.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR ChiTaRS; IGLC2; human.
DR Pharos; P0DOY2; Tdark.
DR PRO; PR:P0DOY2; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P0DOY2; protein.
DR Bgee; ENSG00000211677; Expressed in duodenum and 93 other tissues.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; -; 1.
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 Pfam; PF07654; C1-set; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Bence-Jones protein; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Reference proteome; Secreted.
FT CHAIN <1..106
FT /note="Immunoglobulin lambda constant 2"
FT /id="PRO_0000394665"
FT DOMAIN 7..101
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 28..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 105
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:4883841"
FT NON_TER 1
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4LLD"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 24..36
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4LLY"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:4LLD"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:4LLD"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4LLD"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3C2A"
SQ SEQUENCE 106 AA; 11294 MW; E5DB72BBE65F4577 CRC64;
GQPKAAPSVT LFPPSSEELQ ANKATLVCLI SDFYPGAVTV AWKADSSPVK AGVETTTPSK
QSNNKYAASS YLSLTPEQWK SHRSYSCQVT HEGSTVEKTV APTECS
