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Database: UniProt
Entry: P98154
LinkDB: P98154
Original site: P98154 
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   08-MAY-2019, entry version 143.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Kimber W.L., 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
RT   adhesion protein.";
RL   Biochem. Biophys. Res. Commun. 222:144-148(1996).
CC   -!- FUNCTION: Probably plays a role in neural crest cell migration.
CC       May play a role in delivery of extracellular signals.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Ubiquitous in various organs with low
CC       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";
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   SMR; P98154; -.
DR   STRING; 10090.ENSMUSP00000012152; -.
DR   iPTMnet; P98154; -.
DR   PhosphoSitePlus; P98154; -.
DR   MaxQB; P98154; -.
DR   PaxDb; P98154; -.
DR   PRIDE; P98154; -.
DR   GeneID; 13356; -.
DR   KEGG; mmu:13356; -.
DR   CTD; 9993; -.
DR   MGI; MGI:892866; Dgcr2.
DR   eggNOG; ENOG410J28G; Eukaryota.
DR   eggNOG; ENOG4111WJC; LUCA.
DR   HOGENOM; HOG000112997; -.
DR   InParanoid; P98154; -.
DR   OrthoDB; 491327at2759; -.
DR   PhylomeDB; P98154; -.
DR   ChiTaRS; Dgcr2; mouse.
DR   PRO; PR:P98154; -.
DR   Proteomes; UP000000589; Unplaced.
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:0042493; P:response to drug; 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; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001007; VWF_dom.
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; Complete proteome; Disulfide bond; Glycoprotein;
KW   Lectin; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    548       Integral membrane protein DGCR2/IDD.
FT                                /FTId=PRO_0000021485.
FT   TOPO_DOM     25    347       Extracellular. {ECO:0000255}.
FT   TRANSMEM    348    366       Helical. {ECO:0000255}.
FT   TOPO_DOM    367    548       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       28     68       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      113    239       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      268    331       VWFC.
FT   MOD_RES     379    379       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P98153}.
FT   CARBOHYD    147    147       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    194    194       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     30     44       {ECO:0000250}.
FT   DISULFID     37     57       {ECO:0000250}.
FT   DISULFID     51     66       {ECO:0000250}.
FT   DISULFID    143    263       {ECO:0000250}.
FT   DISULFID    236    255       {ECO:0000250}.
FT   CONFLICT     67     67       P -> PE (in Ref. 2; BAA11460).
FT                                {ECO:0000305}.
FT   CONFLICT    108    111       SFLG -> R (in Ref. 2; BAA11460).
FT                                {ECO:0000305}.
FT   CONFLICT    370    370       A -> R (in Ref. 2; BAA11460).
FT                                {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
//
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