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 27-MAR-2024, entry version 159. 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 EMDB; EMD-0894; -. DR EMDB; EMD-26668; -. DR SMR; P01749; -. DR MaxQB; P01749; -. DR PeptideAtlas; P01749; -. DR ProteomicsDB; 266903; -. DR Ensembl; ENSMUST00000103531.4; ENSMUSP00000100312.4; ENSMUSG00000094087.2. DR AGR; MGI:4439824; -. 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; TSYDIHC; -. 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 cell types or tissues. DR GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW. DR GO; GO:0003823; F:antigen binding; IBA:GO_Central. DR GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central. DR CDD; cd04981; IgV_H; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR23266:SF355; IG HEAVY CHAIN V REGION 3-RELATED; 1. DR PANTHER; PTHR23266; IMMUNOGLOBULIN HEAVY CHAIN; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 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 //