HVM05_MOUSE
ID HVM05_MOUSE Reviewed; 117 AA.
AC P01749;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ig heavy chain V region 3;
DE Flags: Precursor;
GN Name=Ighv1-61; Synonyms=Igh-VJ558;
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].
RC STRAIN=C57BL/6J;
RX PubMed=6788376; DOI=10.1016/0092-8674(81)90089-1;
RA Bothwell A.L.M., Paskind M., Reth M., Imanishi-Kari T., Rajewsky K.,
RA Baltimore D.;
RT "Heavy chain variable region contribution to the NPb family of antibodies:
RT somatic mutation evident in a gamma 2a variable region.";
RL Cell 24:625-637(1981).
CC -!- MISCELLANEOUS: This germline gene belongs to a set of closely related
CC genes that could encode V regions of NPb antibodies.
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 EMBL; J00536; AAA38605.1; -; Genomic_DNA.
DR PIR; A02031; HVMS3.
DR PIR; PH1163; PH1163.
DR PIR; PH1164; PH1164.
DR PDB; 1A14; X-ray; 2.50 A; H=20-117.
DR PDBsum; 1A14; -.
DR AlphaFoldDB; P01749; -.
DR SMR; P01749; -.
DR MaxQB; P01749; -.
DR PeptideAtlas; P01749; -.
DR PRIDE; P01749; -.
DR ProteomicsDB; 266903; -.
DR Ensembl; ENSMUST00000103531; ENSMUSP00000100312; ENSMUSG00000094087.
DR MGI; MGI:4439824; Ighv1-61.
DR VEuPathDB; HostDB:ENSMUSG00000094087; -.
DR GeneTree; ENSGT00950000183013; -.
DR HOGENOM; CLU_077975_5_2_1; -.
DR InParanoid; P01749; -.
DR OMA; MGWICII; -.
DR PhylomeDB; P01749; -.
DR TreeFam; TF352061; -.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-173623; Classical antibody-mediated complement activation.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-2029481; FCGR activation.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR Reactome; R-MMU-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-5690714; CD22 mediated BCR regulation.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR EvolutionaryTrace; P01749; -.
DR PRO; PR:P01749; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P01749; protein.
DR Bgee; ENSMUSG00000094087; Expressed in jejunum and 24 other tissues.
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 3"
FT /id="PRO_0000015218"
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..25
FT /evidence="ECO:0007829|PDB:1A14"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:1A14"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1A14"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1A14"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1A14"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1A14"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1A14"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1A14"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1A14"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1A14"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1A14"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1A14"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1A14"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1A14"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:1A14"
SQ SEQUENCE 117 AA; 13016 MW; 427C861C53975EDC CRC64;
MGWSCIILFL VATATGVHSQ VQLQQPGAEL VRPGSSVKLS CKASGYTFTS YWMDWVKQRP
GQGLEWIGNI YPSDSETHYN QKFKDKATLT VDKSSSTAYM QLSSLTSEDS AVYYCAR
