ID   HVM46_MOUSE             Reviewed;         137 AA.
AC   P01822;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Ig heavy chain V region MOPC 315;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2497341; DOI=10.1016/0161-5890(89)90133-8;
RA   Rinfret A., Horne C., Dorrington K.J., Klein M.;
RT   "Cloning, sequencing and expression of the rearranged MOPC 315 VH gene
RT   segment.";
RL   Mol. Immunol. 26:431-434(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-31 (PRECURSOR PROTEIN).
RX   PubMed=414225; DOI=10.1073/pnas.74.12.5692;
RA   Jilka R.L., Pestka S.;
RT   "Amino acid sequence of the precursor region of MOPC-315 mouse
RT   immunoglobulin heavy chain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 74:5692-5696(1977).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-21 (PRECURSOR PROTEIN).
RX   PubMed=428562;
RA   Schechter I., Wolf O., Zemell R., Burstein Y.;
RT   "Structure and function of immunoglobulin genes and precursors.";
RL   Fed. Proc. 38:1839-1845(1979).
RN   [4]
RP   PROTEIN SEQUENCE OF 19-136.
RX   PubMed=4524622; DOI=10.1073/pnas.71.4.1123;
RA   Francis S.H., Leslie R.G.Q., Hood L., Eisen H.N.;
RT   "Amino-acid sequence of the variable region of the heavy (alpha) chain of a
RT   mouse myeloma protein with anti-hapten activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 71:1123-1127(1974).
RN   [5]
RP   SEQUENCE REVISION TO 53.
RX   PubMed=268248; DOI=10.1101/sqb.1977.041.01.072;
RA   Padlan E.A., Davies D.R., Pecht I., Givol D., Wright C.;
RT   "Model-building studies of antigen-binding sites: the hapten-binding site
RT   of mopc-315.";
RL   Cold Spring Harb. Symp. Quant. Biol. 41:627-637(1977).
CC   -!- MISCELLANEOUS: This alpha chain was isolated from a myeloma protein
CC       that has anti-dinitrophenyl activity.
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DR   EMBL; M27638; AAA61337.1; -; Genomic_DNA.
DR   EMBL; X07880; CAA30727.1; -; Genomic_DNA.
DR   PIR; PL0102; AVMS35.
DR   AlphaFoldDB; P01822; -.
DR   SMR; P01822; -.
DR   PRIDE; P01822; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P01822; protein.
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; -; 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   Adaptive immunity; Direct protein sequencing; Disulfide bond; Immunity;
KW   Immunoglobulin; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:414225,
FT                   ECO:0000269|PubMed:4524622"
FT   CHAIN           19..137
FT                   /note="Ig heavy chain V region MOPC 315"
FT                   /id="PRO_0000015232"
FT   REGION          19..48
FT                   /note="Framework-1"
FT   REGION          49..54
FT                   /note="Complementarity-determining-1"
FT   REGION          55..68
FT                   /note="Framework-2"
FT   REGION          69..84
FT                   /note="Complementarity-determining-2"
FT   REGION          85..116
FT                   /note="Framework-3"
FT   REGION          117..126
FT                   /note="Complementarity-determining-3"
FT   REGION          127..137
FT                   /note="Framework-4"
FT   DISULFID        40..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        15
FT                   /note="G -> GG (in Ref. 1; CAA30727)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="G -> H (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77..78
FT                   /note="GY -> YG (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="N -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="Missing (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         137
SQ   SEQUENCE   137 AA;  15399 MW;  FB3828304C2B81DC CRC64;
     MKVLSLLYLL TAIPGIMSDV QLQESGPGLV KPSQSLSLTC SVTGYSITSG YFWNWIRQFP
     GNKLEWLGFI KYDGSNGYNP SLKNRVSITR DTSENQFFLK LNSVTTEDTA TYYCAGDNDH
     LYYFDYWGQG TTLTVSS