位置:首页 > 蛋白库 > HVM49_MOUSE
HVM49_MOUSE
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   03-AUG-2022, entry version 108.
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).
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; 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   PDBsum; 1NGW; -.
DR   AlphaFoldDB; P06328; -.
DR   SMR; P06328; -.
DR   MaxQB; P06328; -.
DR   PeptideAtlas; P06328; -.
DR   PRIDE; P06328; -.
DR   Ensembl; ENSMUST00000103541; ENSMUSP00000100322; ENSMUSG00000096074.
DR   MGI; MGI:4439633; Ighv1-72.
DR   VEuPathDB; HostDB:ENSMUSG00000096074; -.
DR   GeneTree; ENSGT00950000183013; -.
DR   HOGENOM; CLU_077975_5_2_1; -.
DR   OMA; RYYCARN; -.
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 tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
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 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024