IDD_MOUSE
ID IDD_MOUSE Reviewed; 548 AA.
AC P98154; Q61844;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Integral membrane protein DGCR2/IDD;
DE AltName: Full=Seizure-related membrane-bound adhesion protein;
DE Flags: Precursor;
GN Name=Dgcr2; Synonyms=Dgsc, Idd, Sez-12, Sez12;
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].
RC TISSUE=Embryo;
RX PubMed=9107688; DOI=10.1007/s003359900445;
RA Taylor C., Wadey R., O'Donnell H., Roberts C., Mattei M.-G., Kimber W.L.,
RA Wynshaw-Boris A., Scambler P.J.;
RT "Cloning and mapping of murine Dgcr2 and its homology to the Sez-12
RT seizure-related protein.";
RL Mamm. Genome 8:371-375(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=8630060; DOI=10.1006/bbrc.1996.0712;
RA Kajiwara K., Nagasawa H., Shimizu-Nishikawa K., Ookura T., Kimura M.,
RA Sugaya E.;
RT "Cloning of SEZ-12 encoding seizure-related and membrane-bound adhesion
RT protein.";
RL Biochem. Biophys. Res. Commun. 222:144-148(1996).
CC -!- FUNCTION: Probably plays a role in neural crest cell migration. May
CC play a role in delivery of extracellular signals.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous in various organs with low abundance.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=IDD;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_282";
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DR EMBL; X95480; CAA64749.1; -; mRNA.
DR EMBL; D78641; BAA11460.1; -; mRNA.
DR PIR; JC4798; JC4798.
DR RefSeq; NP_001103220.1; NM_001109750.1.
DR AlphaFoldDB; P98154; -.
DR SMR; P98154; -.
DR BioGRID; 199215; 2.
DR STRING; 10090.ENSMUSP00000012152; -.
DR GlyGen; P98154; 2 sites.
DR iPTMnet; P98154; -.
DR PhosphoSitePlus; P98154; -.
DR MaxQB; P98154; -.
DR PaxDb; P98154; -.
DR PRIDE; P98154; -.
DR ProteomicsDB; 273263; -.
DR DNASU; 13356; -.
DR GeneID; 13356; -.
DR KEGG; mmu:13356; -.
DR CTD; 9993; -.
DR MGI; MGI:892866; Dgcr2.
DR eggNOG; KOG1215; Eukaryota.
DR InParanoid; P98154; -.
DR PhylomeDB; P98154; -.
DR BioGRID-ORCS; 13356; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Dgcr2; mouse.
DR PRO; PR:P98154; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P98154; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:MGI.
DR CDD; cd03599; CLECT_DGCR2_like; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR034010; DGCR2-like_CTLD.
DR InterPro; IPR042378; IDD.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR15256; PTHR15256; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS01208; VWFC_1; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..548
FT /note="Integral membrane protein DGCR2/IDD"
FT /id="PRO_0000021485"
FT TOPO_DOM 25..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..68
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 113..239
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 268..331
FT /note="VWFC"
FT REGION 415..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98153"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..44
FT /evidence="ECO:0000250"
FT DISULFID 37..57
FT /evidence="ECO:0000250"
FT DISULFID 51..66
FT /evidence="ECO:0000250"
FT DISULFID 143..263
FT /evidence="ECO:0000250"
FT DISULFID 236..255
FT /evidence="ECO:0000250"
FT CONFLICT 67
FT /note="P -> PE (in Ref. 2; BAA11460)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..111
FT /note="SFLG -> R (in Ref. 2; BAA11460)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="A -> R (in Ref. 2; BAA11460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 60697 MW; 77AF5CA839F6B817 CRC64;
MVPKADSGAF LLLFLLVLTV TEPLRPELRC NPGQFACHGG TIQCIPLPWQ CDGWPTCEDK
SDEADCPVTG EARPYGKETV DLRQGRARGG DPTHFHTVNV AQPVRFSSFL GKCPSGWHHY
EGTASCYRVY LSGENYWDAA QTCQRVNGSL ATFSTDQELR FVLAQEWDQP ERSFGWKDQR
KLWVGYQYVI TGRNHSLEGR WEVAFKGSPE VFLPPDPIFA SAMSENDNVF CAQLQCFHFP
TLRHHDLHSW HAESCSEKSS FLCKRSQTCV DIKDNVVDEG FYFTPKGDDP CLSCTCHRGE
PEMCVAALCE RPQGCQQYRK DPKECCKFMC LDPDGSSLFD SMASGMRLVV SCISSFLILS
LLLFMVHRLA QRRRERIESL IGANLHHFNL GRRIPGFDYG PDGFGTGLTP LHLSDDGEGG
TFHFHDPPPP YTAYKYPDMD QPDDPPPPYE ASINPDSVFY DPADDDAFEP VEASLPAPRD
GGIEGALPRH LDQPLPPAET SLADLEDSTD SSSALLVPPD PAQSGSTPAT EAPPGGGRLP
RASLNTVV
