ID HVM49_MOUSE Reviewed; 117 AA.
AC P06328; A0A075B5X9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 2.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Ig heavy chain V region 1-72 {ECO:0000312|MGI:MGI:4439633};
DE AltName: Full=Ig heavy chain V region VH558 B4 {ECO:0000303|PubMed:2578321};
DE Flags: Precursor;
GN Name=Ighv1-72 {ECO:0000312|MGI:MGI:4439633};
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 [MRNA].
RX PubMed=2578321; DOI=10.1016/0092-8674(85)90141-2;
RA Yancopoulos G.D., Alt F.W.;
RT "Developmentally controlled and tissue-specific expression of unrearranged
RT VH gene segments.";
RL Cell 40:271-281(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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DR EMBL; M13788; AAA38506.1; -; mRNA.
DR EMBL; AC163348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02035; MHMSB4.
DR PDB; 1NGW; X-ray; 2.60 A; B/H=27-117.
DR PDB; 8EMA; EM; 8.20 A; A/B=1-117.
DR PDBsum; 1NGW; -.
DR PDBsum; 8EMA; -.
DR AlphaFoldDB; P06328; -.
DR EMDB; EMD-9633; -.
DR EMDB; EMD-9634; -.
DR SMR; P06328; -.
DR MaxQB; P06328; -.
DR PeptideAtlas; P06328; -.
DR Ensembl; ENSMUST00000103541.3; ENSMUSP00000100322.2; ENSMUSG00000096074.3.
DR AGR; MGI:4439633; -.
DR MGI; MGI:4439633; Ighv1-72.
DR VEuPathDB; HostDB:ENSMUSG00000096074; -.
DR GeneTree; ENSGT00950000183013; -.
DR HOGENOM; CLU_077975_5_2_1; -.
DR InParanoid; P06328; -.
DR OMA; EWMGIIN; -.
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 PRO; PR:P06328; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P06328; Protein.
DR Bgee; ENSMUSG00000096074; Expressed in jejunum and 21 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:SF391; IG HEAVY CHAIN V REGION 1-62-3-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 1-72"
FT /id="PRO_0000015234"
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 CONFLICT 20
FT /note="Q -> P (in Ref. 1; AAA38506)"
FT CONFLICT 69
FT /note="R -> N (in Ref. 1; AAA38506)"
FT CONFLICT 116
FT /note="A -> T (in Ref. 1; AAA38506)"
FT NON_TER 117
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1NGW"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1NGW"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1NGW"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1NGW"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1NGW"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1NGW"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1NGW"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1NGW"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1NGW"
FT TURN 81..86
FT /evidence="ECO:0007829|PDB:1NGW"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1NGW"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1NGW"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1NGW"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1NGW"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:1NGW"
SQ SEQUENCE 117 AA; 12877 MW; 58DBF5088CB162EF CRC64;
MGWSCIMLFL AATATGVHSQ VQLQQPGAEL VKPGASVKLS CKASGYTFTS YWMHWVKQRP
GRGLEWIGRI DPNSGGTKYN EKFKSKATLT VDKPSSTAYM QLSSLTSEDS AVYYCAR
//
