HVM58_MOUSE
ID HVM58_MOUSE Reviewed; 117 AA.
AC P18529;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Ig heavy chain V region 5-76;
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.
RC STRAIN=BALB/cJ;
RX PubMed=2499654; DOI=10.1084/jem.169.6.2007;
RA Levy N.S., Malipiero U.V., Lebecque S.G., Gearhart P.J.;
RT "Early onset of somatic mutation in immunoglobulin VH genes during the
RT primary immune response.";
RL J. Exp. Med. 169:2007-2019(1989).
CC -!- MISCELLANEOUS: This sequence belongs to the VH7183 subfamily.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; JT0506; HVMS57.
DR PDB; 1BFV; X-ray; 2.10 A; H=21-117.
DR PDB; 1I8I; X-ray; 2.40 A; B=21-117.
DR PDB; 1I8K; X-ray; 1.80 A; B=21-117.
DR PDBsum; 1BFV; -.
DR PDBsum; 1I8I; -.
DR PDBsum; 1I8K; -.
DR AlphaFoldDB; P18529; -.
DR SMR; P18529; -.
DR MaxQB; P18529; -.
DR PRIDE; P18529; -.
DR EvolutionaryTrace; P18529; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P18529; 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; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 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; Disulfide bond; Immunity; Immunoglobulin;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT CHAIN 20..117
FT /note="Ig heavy chain V region 5-76"
FT /id="PRO_0000015239"
FT REGION 20..49
FT /note="Framework-1"
FT REGION 50..54
FT /note="Complementarity-determining-1"
FT REGION 55..68
FT /note="Framework-2"
FT REGION 69..85
FT /note="Complementarity-determining-2"
FT REGION 86..117
FT /note="Framework-3"
FT DISULFID 41..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 117
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1I8K"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1I8K"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1I8K"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1I8K"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1I8K"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1I8K"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1I8K"
FT TURN 81..86
FT /evidence="ECO:0007829|PDB:1I8K"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1I8K"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1I8K"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1I8K"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1I8K"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:1I8K"
SQ SEQUENCE 117 AA; 12991 MW; 93A04782B78B8FA0 CRC64;
MNFVLSLIFL ALILKGVQCE VHLVESGGGL VKPGGSLKLS CVVSGFTFNK YAMSWVRQTP
EKRLEWVATI SSGGLYTYYP DSVKGRFTIS RDNAGNTLYL QMSSLRSEDT AMYYCAR
