IGHDM_MOUSE
ID IGHDM_MOUSE Reviewed; 290 AA.
AC P01882;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Ig delta chain C region membrane-bound form;
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].
RX PubMed=6968091; DOI=10.1126/science.6968091;
RA Tucker P.W., Liu C.-P., Mushinski J.F., Blattner F.R.;
RT "Mouse immunoglobulin D: messenger RNA and genomic DNA sequences.";
RL Science 209:1353-1360(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-290.
RX PubMed=6801528; DOI=10.1038/296410a0;
RA Cheng H.-L., Blattner F.R., Fitzmaurice L., Mushinski J.F., Tucker P.W.;
RT "Structure of genes for membrane and secreted murine IgD heavy chains.";
RL Nature 296:410-415(1982).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Membrane-bound;
CC IsoId=P01882-1; Sequence=Displayed;
CC Name=Secreted;
CC IsoId=P01881-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Cell lines producing IgD contain several mRNA
CC species for Ig delta chains. In plasmacytomas, the secreted form is the
CC major component, and the membrane-bound form is a minor component. In
CC spleen, however, the membrane-bound form is the major component. These
CC two forms differ in their C-terminal segments.
CC -!- MISCELLANEOUS: The sequence of residues 1-237 is assumed to be
CC identical with that of the secreted form.
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DR EMBL; J00447; AAB59654.1; -; Genomic_DNA.
DR EMBL; J00448; AAB59654.1; JOINED; Genomic_DNA.
DR EMBL; J00449; AAB59654.1; JOINED; Genomic_DNA.
DR EMBL; J00450; AAB59654.1; JOINED; Genomic_DNA.
DR PIR; A02177; DHMSM.
DR AlphaFoldDB; P01882; -.
DR SMR; P01882; -.
DR IntAct; P01882; 4.
DR GlyGen; P01882; 5 sites.
DR MaxQB; P01882; -.
DR PRIDE; P01882; -.
DR UCSC; uc007pgq.1; mouse. [P01882-1]
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01882; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR Pfam; PF07654; C1-set; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..290
FT /note="Ig delta chain C region membrane-bound form"
FT /id="PRO_0000153572"
FT TRANSMEM 262..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 5..105
FT /note="Ig-like 1"
FT DOMAIN 133..233
FT /note="Ig-like 2"
FT REGION 89..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 13
FT /note="Interchain (with light chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 26..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 155
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1
SQ SEQUENCE 290 AA; 32353 MW; 037A888CEB7598A0 CRC64;
DKKEPDMFLL SECKAPEENE KINLGCLVIG SQPLKISWEP KKSSIVEHVF PSEMRNGNYT
MVLQVTVLAS ELNLNHTCTI NKPKRKEKPF KFPESWDSQS SKRVTPTLQA KNHSTEATKA
ITTKKDIEGA MAPSNLTVNI LTTSTHPEMS SWLLCEVSGF FPENIHLMWL GVHSKMKSTN
FVTANPTAQP GGTFQTWSVL RLPVALSSSL DTYTCVVEHE ASKTKLNASK SLAISGIVNT
IQHSCIMDEQ SDSYMDLEEE NGLWPTMCTF VALFLLTLLY SGFVTFIKVK
