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 24-NOV-2009, entry version 69. DE RecName: Full=Ig heavy chain V region MOPC 315; DE Flags: Precursor; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89238351; 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. RX MEDLINE=78094475; 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. RX MEDLINE=79148758; 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 MEDLINE=74170779; 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 RT of a 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 MEDLINE=77244979; PubMed=268248; RA Padlan E.A., Davies D.R., Pecht I., Givol D., Wright C.; RT "Model-building studies of antigen-binding sites: the hapten-binding RT site of mopc-315."; RL Cold Spring Harb. Symp. Quant. Biol. 41:627-637(1977). CC -!- MISCELLANEOUS: This alpha chain was isolated from a myeloma CC protein that has anti-dinitrophenyl activity. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M27638; AAA61337.1; -; Genomic_DNA. DR EMBL; X07880; CAA30727.1; -; Genomic_DNA. DR IPI; IPI00457481; -. DR PIR; PL0102; AVMS35. DR SMR; P01822; 20-137. DR STRING; P01822; -. DR Ensembl; ENSMUST00000103481; ENSMUSP00000100262; ENSMUSG00000076672; Mus musculus. DR HOVERGEN; P01822; -. DR Genevestigator; P01822; -. DR GO; GO:0003823; F:antigen binding; IEA:UniProtKB-KW. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR003596; Ig_V-set_sub. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00406; IGv; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Immunoglobulin domain; KW Immunoglobulin V region; Signal. FT SIGNAL 1 18 FT CHAIN 19 137 Ig heavy chain V region MOPC 315. FT /FTId=PRO_0000015232. FT REGION 19 48 Framework-1. FT REGION 49 54 Complementarity-determining-1. FT REGION 55 68 Framework-2. FT REGION 69 84 Complementarity-determining-2. FT REGION 85 116 Framework-3. FT REGION 117 126 Complementarity-determining-3. FT REGION 127 137 Framework-4. FT DISULFID 40 114 By similarity. FT CONFLICT 15 15 G -> GG (in Ref. 1; CAA30727). FT CONFLICT 15 15 G -> H (in Ref. 2; AA sequence). FT CONFLICT 77 78 GY -> YG (in Ref. 4; AA sequence). FT CONFLICT 102 102 N -> D (in Ref. 4; AA sequence). FT CONFLICT 123 123 Missing (in Ref. 4; AA sequence). FT NON_TER 137 137 SQ SEQUENCE 137 AA; 15399 MW; FB3828304C2B81DC CRC64; MKVLSLLYLL TAIPGIMSDV QLQESGPGLV KPSQSLSLTC SVTGYSITSG YFWNWIRQFP GNKLEWLGFI KYDGSNGYNP SLKNRVSITR DTSENQFFLK LNSVTTEDTA TYYCAGDNDH LYYFDYWGQG TTLTVSS //