KV3A9_MOUSE
ID KV3A9_MOUSE Reviewed; 131 AA.
AC P01661;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Ig kappa chain V-III region MOPC 63;
DE Flags: Precursor;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP PROTEIN SEQUENCE OF 1-35 (PRECURSOR PROTEIN).
RX PubMed=98179; DOI=10.1021/bi00605a022;
RA Burstein Y., Schechter I.;
RT "Primary structures of N-terminal extra peptide segments linked to the
RT variable and constant regions of immunoglobulin light chain precursors:
RT implications on the organization and controlled expression of
RT immunoglobulin genes.";
RL Biochemistry 17:2392-2400(1978).
RN [2]
RP PROTEIN SEQUENCE OF 21-131.
RX PubMed=4691517; DOI=10.1021/bi00728a028;
RA McKean D.J., Potter M., Hood L.E.;
RT "Mouse immunoglobulin chains. Pattern of sequence variation among kappa
RT chains with limited sequence differences.";
RL Biochemistry 12:760-771(1973).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=99744; DOI=10.1073/pnas.75.8.3913;
RA McKean D.J., Bell M., Potter M.;
RT "Mechanisms of antibody diversity: multiple genes encode structurally
RT related mouse kappa variable regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:3913-3917(1978).
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DR PIR; B90412; KVMSM6.
DR PIR; D45722; D45722.
DR PDB; 1EGJ; X-ray; 2.80 A; L=21-131.
DR PDBsum; 1EGJ; -.
DR AlphaFoldDB; P01661; -.
DR SMR; P01661; -.
DR MaxQB; P01661; -.
DR PeptideAtlas; P01661; -.
DR PRIDE; P01661; -.
DR PhylomeDB; P01661; -.
DR EvolutionaryTrace; P01661; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01661; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; 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; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Direct protein sequencing; Disulfide bond;
KW Immunity; Immunoglobulin; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:4691517"
FT CHAIN 21..131
FT /note="Ig kappa chain V-III region MOPC 63"
FT /id="PRO_0000015187"
FT REGION 21..43
FT /note="Framework-1"
FT REGION 44..58
FT /note="Complementarity-determining-1"
FT REGION 59..73
FT /note="Framework-2"
FT REGION 74..80
FT /note="Complementarity-determining-2"
FT REGION 81..112
FT /note="Framework-3"
FT REGION 113..121
FT /note="Complementarity-determining-3"
FT REGION 122..131
FT /note="Framework-4"
FT DISULFID 43..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 131
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1EGJ"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1EGJ"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1EGJ"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1EGJ"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1EGJ"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1EGJ"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1EGJ"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:1EGJ"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:1EGJ"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1EGJ"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1EGJ"
SQ SEQUENCE 131 AA; 14291 MW; D212EC9F08DC880A CRC64;
METDTLLLWV LLLWVPGSTG NIVLTQSPAS LAVSLGQRAT ISCRASESVD SYGNSFMHWY
QQKPGQPPKL LIYLASNLES GVPARFSGSG SRTDFTLTID PVEADDAATY YCQQNNEDPW
TFGGGTKLEI K