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   27-MAR-2024, entry version 159.
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   GlyCosmos; P98154; 2 sites, No reported glycans.
DR   GlyGen; P98154; 2 sites.
DR   iPTMnet; P98154; -.
DR   PhosphoSitePlus; P98154; -.
DR   MaxQB; P98154; -.
DR   PaxDb; 10090-ENSMUSP00000012152; -.
DR   ProteomicsDB; 273263; -.
DR   DNASU; 13356; -.
DR   GeneID; 13356; -.
DR   KEGG; mmu:13356; -.
DR   AGR; MGI:892866; -.
DR   CTD; 9993; -.
DR   MGI; MGI:892866; Dgcr2.
DR   eggNOG; KOG1215; Eukaryota.
DR   InParanoid; P98154; -.
DR   OrthoDB; 3145217at2759; -.
DR   PhylomeDB; P98154; -.
DR   BioGRID-ORCS; 13356; 1 hit in 75 CRISPR screens.
DR   ChiTaRS; Dgcr2; mouse.
DR   PRO; PR:P98154; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P98154; Protein.
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; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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; INTEGRAL MEMBRANE PROTEIN DGCR2/IDD; 1.
DR   PANTHER; PTHR15256:SF6; INTEGRAL MEMBRANE PROTEIN DGCR2_IDD; 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; C-type lectin-like; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 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
//