Full text data of DSCAML1
DSCAML1
(DSCAM2, KIAA1132)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Down syndrome cell adhesion molecule-like protein 1 (Down syndrome cell adhesion molecule 2; Flags: Precursor)
Down syndrome cell adhesion molecule-like protein 1 (Down syndrome cell adhesion molecule 2; Flags: Precursor)
hRBCD
IPI00154755
IPI00154755 Down syndrome cell adhesion molecule 2 Down syndrome cell adhesion molecule 2 membrane n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a Type I membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00154755 Down syndrome cell adhesion molecule 2 Down syndrome cell adhesion molecule 2 membrane n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a Type I membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
Q8TD84
ID DSCL1_HUMAN Reviewed; 2053 AA.
AC Q8TD84; Q76MU9; Q8IZY3; Q8IZY4; Q8WXU7; Q9ULT7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2005, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Down syndrome cell adhesion molecule-like protein 1;
DE AltName: Full=Down syndrome cell adhesion molecule 2;
DE Flags: Precursor;
GN Name=DSCAML1; Synonyms=DSCAM2, KIAA1132;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11453658; DOI=10.1006/bbrc.2001.5214;
RA Agarwala K.L., Ganesh S., Tsutsumi Y., Suzuki T., Amano K.,
RA Yamakawa K.;
RT "Cloning and functional characterization of DSCAML1, a novel DSCAM-
RT like cell adhesion molecule that mediates homophilic intercellular
RT adhesion.";
RL Biochem. Biophys. Res. Commun. 285:760-772(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RX PubMed=12051741; DOI=10.1016/S0006-291X(02)00307-8;
RA Barlow G.M., Micales B., Chen X.-N., Lyons G.E., Korenberg J.R.;
RT "Mammalian DSCAMs: roles in the development of the spinal cord,
RT cortex, and cerebellum?";
RL Biochem. Biophys. Res. Commun. 293:881-891(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Fetal brain;
RA Lin S., Wang Z., Ying K., Xie Y., Mao Y.;
RT "DSCAML1, a novel member of the immunoglobulin superfamily.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis
RT from size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP STRUCTURE BY NMR OF 979-1087.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second FNIII domain of DSCAML1 protein.";
RL Submitted (FEB-2005) to the PDB data bank.
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-659 AND ILE-1702.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cell adhesion molecule that plays a role in neuronal
CC self-avoidance. Promotes repulsion between specific neuronal
CC processes of either the same cell or the same subtype of cells.
CC Promotes both isoneuronal self-avoidance for creating an orderly
CC neurite arborization in retinal rod bipolar cells and
CC heteroneuronal self-avoidance to maintain mosaic spacing between
CC AII amacrine cells (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=1a;
CC IsoId=Q8TD84-1; Sequence=Displayed;
CC Name=2; Synonyms=1b;
CC IsoId=Q8TD84-2; Sequence=VSP_014978;
CC -!- TISSUE SPECIFICITY: Detected in heart, liver, pancreas, skeletal
CC muscle, kidney and in brain, in particular in the amygdala,
CC caudate nucleus, corpus callosum, hippocampus, substantia nigra,
CC thalamus and subthalamus.
CC -!- SIMILARITY: Contains 6 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 10 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM09558.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAA86446.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AF334384; AAL57166.1; -; mRNA.
DR EMBL; AF491813; AAM09558.1; ALT_INIT; mRNA.
DR EMBL; AF304304; AAN32613.1; -; mRNA.
DR EMBL; AF304305; AAN32614.1; -; mRNA.
DR EMBL; AB032958; BAA86446.2; ALT_INIT; mRNA.
DR EMBL; AP000711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_065744.2; NM_020693.2.
DR UniGene; Hs.659513; -.
DR PDB; 1VA9; NMR; -; A=979-1087.
DR PDBsum; 1VA9; -.
DR ProteinModelPortal; Q8TD84; -.
DR SMR; Q8TD84; 27-1563.
DR IntAct; Q8TD84; 3.
DR STRING; 9606.ENSP00000315465; -.
DR DMDM; 73620825; -.
DR PaxDb; Q8TD84; -.
DR PRIDE; Q8TD84; -.
DR Ensembl; ENST00000321322; ENSP00000315465; ENSG00000177103.
DR GeneID; 57453; -.
DR KEGG; hsa:57453; -.
DR UCSC; uc001prh.1; human.
DR CTD; 57453; -.
DR GeneCards; GC11M117332; -.
DR HGNC; HGNC:14656; DSCAML1.
DR HPA; CAB025540; -.
DR MIM; 611782; gene.
DR neXtProt; NX_Q8TD84; -.
DR PharmGKB; PA38384; -.
DR eggNOG; NOG12793; -.
DR HOGENOM; HOG000112277; -.
DR HOVERGEN; HBG051409; -.
DR InParanoid; Q8TD84; -.
DR KO; K06768; -.
DR Reactome; REACT_111155; Cell-Cell communication.
DR ChiTaRS; DSCAML1; human.
DR EvolutionaryTrace; Q8TD84; -.
DR GenomeRNAi; 57453; -.
DR NextBio; 63628; -.
DR PRO; PR:Q8TD84; -.
DR ArrayExpress; Q8TD84; -.
DR Bgee; Q8TD84; -.
DR CleanEx; HS_DSCAML1; -.
DR Genevestigator; Q8TD84; -.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
DR GO; GO:0070593; P:dendrite self-avoidance; IEA:Ensembl.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; NAS:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IDA:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion; IDA:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 16.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 8.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 7.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Complete proteome; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Polymorphism;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 18 Potential.
FT CHAIN 19 2053 Down syndrome cell adhesion molecule-like
FT protein 1.
FT /FTId=PRO_0000014748.
FT TOPO_DOM 19 1591 Extracellular (Potential).
FT TRANSMEM 1592 1612 Helical; (Potential).
FT TOPO_DOM 1613 2053 Cytoplasmic (Potential).
FT DOMAIN 19 119 Ig-like C2-type 1.
FT DOMAIN 115 217 Ig-like C2-type 2.
FT DOMAIN 226 306 Ig-like C2-type 3.
FT DOMAIN 314 402 Ig-like C2-type 4.
FT DOMAIN 408 501 Ig-like C2-type 5.
FT DOMAIN 506 586 Ig-like C2-type 6.
FT DOMAIN 596 685 Ig-like C2-type 7.
FT DOMAIN 690 784 Ig-like C2-type 8.
FT DOMAIN 788 885 Ig-like C2-type 9.
FT DOMAIN 887 984 Fibronectin type-III 1.
FT DOMAIN 989 1088 Fibronectin type-III 2.
FT DOMAIN 1093 1189 Fibronectin type-III 3.
FT DOMAIN 1193 1288 Fibronectin type-III 4.
FT DOMAIN 1278 1377 Ig-like C2-type 10.
FT DOMAIN 1383 1477 Fibronectin type-III 5.
FT DOMAIN 1478 1578 Fibronectin type-III 6.
FT COMPBIAS 1956 2016 Pro-rich.
FT CARBOHYD 29 29 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 79 79 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 368 368 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 471 471 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 513 513 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 556 556 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 666 666 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 710 710 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 749 749 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 796 796 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 809 809 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 926 926 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1082 1082 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1144 1144 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1162 1162 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1275 1275 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1345 1345 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1492 1492 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1531 1531 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1561 1561 N-linked (GlcNAc...) (Potential).
FT DISULFID 47 103 By similarity.
FT DISULFID 146 198 By similarity.
FT DISULFID 247 294 By similarity.
FT DISULFID 336 386 By similarity.
FT DISULFID 429 485 By similarity.
FT DISULFID 526 575 By similarity.
FT DISULFID 617 669 By similarity.
FT DISULFID 711 767 By similarity.
FT DISULFID 810 867 By similarity.
FT DISULFID 1311 1363 By similarity.
FT VAR_SEQ 34 244 Missing (in isoform 2).
FT /FTId=VSP_014978.
FT VARIANT 659 659 V -> I (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035512.
FT VARIANT 1702 1702 V -> I (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035513.
FT CONFLICT 4 4 V -> L (in Ref. 3; AAN32613/AAN32614).
FT CONFLICT 150 152 SSV -> FLG (in Ref. 3; AAN32613).
FT CONFLICT 172 172 H -> N (in Ref. 1; AAL57166 and 4;
FT BAA86446).
FT CONFLICT 250 250 S -> P (in Ref. 3; AAN32614).
FT CONFLICT 469 469 H -> Y (in Ref. 3; AAN32613).
FT CONFLICT 667 667 Y -> D (in Ref. 3; AAN32613/AAN32614).
FT STRAND 991 997
FT STRAND 999 1008
FT STRAND 1021 1030
FT STRAND 1046 1055
FT STRAND 1062 1070
SQ SEQUENCE 2053 AA; 224463 MW; 9CC9644214FF19C4 CRC64;
MWLVTFLLLL DSLHKARPED VGTSLYFVND SLQQVTFSSS VGVVVPCPAA GSPSAALRWY
LATGDDIYDV PHIRHVHANG TLQLYPFSPS AFNSFIHDND YFCTAENAAG KIRSPNIRVK
AVFREPYTVR VEDQRSMRGN VAVFKCLIPS SVQEYVSVVS WEKDTVSIIP EHRFFITYHG
GLYISDVQKE DALSTYRCIT KHKYSGETRQ SNGARLSVTD PAESIPTILD GFHSQEVWAG
HTVELPCTAS GYPIPAIRWL KDGRPLPADS RWTKRITGLT ISDLRTEDSG TYICEVTNTF
GSAEATGILM VIDPLHVTLT PKKLKTGIGS TVILSCALTG SPEFTIRWYR NTELVLPDEA
ISIRGLSNET LLITSAQKSH SGAYQCFATR KAQTAQDFAI IALEDGTPRI VSSFSEKVVN
PGEQFSLMCA AKGAPPPTVT WALDDEPIVR DGSHRTNQYT MSDGTTISHM NVTGPQIRDG
GVYRCTARNL VGSAEYQARI NVRGPPSIRA MRNITAVAGR DTLINCRVIG YPYYSIKWYK
DALLLPDNHR QVVFENGTLK LTDVQKGMDE GEYLCSVLIQ PQLSISQSVH VAVKVPPLIQ
PFEFPPASIG QLLYIPCVVS SGDMPIRITW RKDGQVIISG SGVTIESKEF MSSLQISSVS
LKHNGNYTCI ASNAAATVSR ERQLIVRVPP RFVVQPNNQD GIYGKAGVLN CSVDGYPPPK
VMWKHAKGSG NPQQYHPVPL TGRIQILPNS SLLIRHVLEE DIGYYLCQAS NGVGTDISKS
MFLTVKIPAM ITSHPNTTIA IKGHAKELNC TARGERPIII RWEKGDTVID PDRVMRYAIA
TKDNGDEVVS TLKLKPADRG DSVFFSCHAI NSYGEDRGLI QLTVQEPPDP PELEIREVKA
RSMNLRWTQR FDGNSIITGF DIEYKNKSDS WDFKQSTRNI SPTINQANIV DLHPASVYSI
RMYSFNKIGR SEPSKELTIS TEEAAPDGPP MDVTLQPVTS QSIQVTWKAP KKELQNGVIR
GYQIGYRENS PGSNGQYSIV EMKATGDSEV YTLDNLKKFA QYGVVVQAFN RAGTGPSSSE
INATTLEDVP SQPPENVRAL SITSDVAVIS WSEPPRSTLN GVLKGYRVIF WSLYVDGEWG
EMQNITTTRE RVELRGMEKF TNYSVQVLAY TQAGDGVRSS VLYIQTKEDV PGPPAGIKAV
PSSASSVVVS WLPPTKPNGV IRKYTIFCSS PGSGQPAPSE YETSPEQLFY RIAHLNRGQQ
YLLWVAAVTS AGRGNSSEKV TIEPAGKAPA KIISFGGTVT TPWMKDVRLP CNSVGDPAPA
VKWTKDSEDS AIPVSMDGHR LIHTNGTLLL RAVKAEDSGY YTCTATNTGG FDTIIVNLLV
QVPPDQPRLT VSKTSASSIT LTWIPGDNGG SSIRGFVLQY SVDNSEEWKD VFISSSERSF
KLDSLKCGTW YKVKLAAKNS VGSGRISEII EAKTHGREPS FSKDQHLFTH INSTHARLNL
QGWNNGGCPI TAIVLEYRPK GTWAWQGLRA NSSGEVFLTE LREATWYELR MRACNSAGCG
NETAQFATLD YDGSTIPPIK SAQGEGDDVK KLFTIGCPVI LATLGVALLF IVRKKRKEKR
LKRLRDAKSL AEMLISKNNR SFDTPVKGPP QGPRLHIDIP RVQLLIEDKE GIKQLGDDKA
TIPVTDAEFS QAVNPQSFCT GVSLHHPTLI QSTGPLIDMS DIRPGTNPVS RKNVKSAHST
RNRYSSQWTL TKCQASTPAR TLTSDWRTVG SQHGVTVTES DSYSASLSQD TDKGRNSMVS
TESASSTYEE LARAYEHAKL EEQLQHAKFE ITECFISDSS SDQMTTGTNE NADSMTSMST
PSEPGICRFT ASPPKPQDAD RGKNVAVPIP HRANKSDYCN LPLYAKSEAF FRKADGREPC
PVVPPREASI RNLARTYHTQ ARHLTLDPAS KSLGLPHPGA PAAASTATLP QRTLAMPAPP
AGTAPPAPGP TPAEPPTAPS AAPPAPSTEP PRAGGPHTKM GGSRDSLLEM STSGVGRSQK
QGAGAYSKSY TLV
//
ID DSCL1_HUMAN Reviewed; 2053 AA.
AC Q8TD84; Q76MU9; Q8IZY3; Q8IZY4; Q8WXU7; Q9ULT7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2005, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Down syndrome cell adhesion molecule-like protein 1;
DE AltName: Full=Down syndrome cell adhesion molecule 2;
DE Flags: Precursor;
GN Name=DSCAML1; Synonyms=DSCAM2, KIAA1132;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11453658; DOI=10.1006/bbrc.2001.5214;
RA Agarwala K.L., Ganesh S., Tsutsumi Y., Suzuki T., Amano K.,
RA Yamakawa K.;
RT "Cloning and functional characterization of DSCAML1, a novel DSCAM-
RT like cell adhesion molecule that mediates homophilic intercellular
RT adhesion.";
RL Biochem. Biophys. Res. Commun. 285:760-772(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RX PubMed=12051741; DOI=10.1016/S0006-291X(02)00307-8;
RA Barlow G.M., Micales B., Chen X.-N., Lyons G.E., Korenberg J.R.;
RT "Mammalian DSCAMs: roles in the development of the spinal cord,
RT cortex, and cerebellum?";
RL Biochem. Biophys. Res. Commun. 293:881-891(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Fetal brain;
RA Lin S., Wang Z., Ying K., Xie Y., Mao Y.;
RT "DSCAML1, a novel member of the immunoglobulin superfamily.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis
RT from size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP STRUCTURE BY NMR OF 979-1087.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second FNIII domain of DSCAML1 protein.";
RL Submitted (FEB-2005) to the PDB data bank.
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-659 AND ILE-1702.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cell adhesion molecule that plays a role in neuronal
CC self-avoidance. Promotes repulsion between specific neuronal
CC processes of either the same cell or the same subtype of cells.
CC Promotes both isoneuronal self-avoidance for creating an orderly
CC neurite arborization in retinal rod bipolar cells and
CC heteroneuronal self-avoidance to maintain mosaic spacing between
CC AII amacrine cells (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=1a;
CC IsoId=Q8TD84-1; Sequence=Displayed;
CC Name=2; Synonyms=1b;
CC IsoId=Q8TD84-2; Sequence=VSP_014978;
CC -!- TISSUE SPECIFICITY: Detected in heart, liver, pancreas, skeletal
CC muscle, kidney and in brain, in particular in the amygdala,
CC caudate nucleus, corpus callosum, hippocampus, substantia nigra,
CC thalamus and subthalamus.
CC -!- SIMILARITY: Contains 6 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 10 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM09558.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAA86446.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AF334384; AAL57166.1; -; mRNA.
DR EMBL; AF491813; AAM09558.1; ALT_INIT; mRNA.
DR EMBL; AF304304; AAN32613.1; -; mRNA.
DR EMBL; AF304305; AAN32614.1; -; mRNA.
DR EMBL; AB032958; BAA86446.2; ALT_INIT; mRNA.
DR EMBL; AP000711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_065744.2; NM_020693.2.
DR UniGene; Hs.659513; -.
DR PDB; 1VA9; NMR; -; A=979-1087.
DR PDBsum; 1VA9; -.
DR ProteinModelPortal; Q8TD84; -.
DR SMR; Q8TD84; 27-1563.
DR IntAct; Q8TD84; 3.
DR STRING; 9606.ENSP00000315465; -.
DR DMDM; 73620825; -.
DR PaxDb; Q8TD84; -.
DR PRIDE; Q8TD84; -.
DR Ensembl; ENST00000321322; ENSP00000315465; ENSG00000177103.
DR GeneID; 57453; -.
DR KEGG; hsa:57453; -.
DR UCSC; uc001prh.1; human.
DR CTD; 57453; -.
DR GeneCards; GC11M117332; -.
DR HGNC; HGNC:14656; DSCAML1.
DR HPA; CAB025540; -.
DR MIM; 611782; gene.
DR neXtProt; NX_Q8TD84; -.
DR PharmGKB; PA38384; -.
DR eggNOG; NOG12793; -.
DR HOGENOM; HOG000112277; -.
DR HOVERGEN; HBG051409; -.
DR InParanoid; Q8TD84; -.
DR KO; K06768; -.
DR Reactome; REACT_111155; Cell-Cell communication.
DR ChiTaRS; DSCAML1; human.
DR EvolutionaryTrace; Q8TD84; -.
DR GenomeRNAi; 57453; -.
DR NextBio; 63628; -.
DR PRO; PR:Q8TD84; -.
DR ArrayExpress; Q8TD84; -.
DR Bgee; Q8TD84; -.
DR CleanEx; HS_DSCAML1; -.
DR Genevestigator; Q8TD84; -.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
DR GO; GO:0070593; P:dendrite self-avoidance; IEA:Ensembl.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; NAS:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IDA:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion; IDA:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 16.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 8.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 7.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Complete proteome; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Polymorphism;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 18 Potential.
FT CHAIN 19 2053 Down syndrome cell adhesion molecule-like
FT protein 1.
FT /FTId=PRO_0000014748.
FT TOPO_DOM 19 1591 Extracellular (Potential).
FT TRANSMEM 1592 1612 Helical; (Potential).
FT TOPO_DOM 1613 2053 Cytoplasmic (Potential).
FT DOMAIN 19 119 Ig-like C2-type 1.
FT DOMAIN 115 217 Ig-like C2-type 2.
FT DOMAIN 226 306 Ig-like C2-type 3.
FT DOMAIN 314 402 Ig-like C2-type 4.
FT DOMAIN 408 501 Ig-like C2-type 5.
FT DOMAIN 506 586 Ig-like C2-type 6.
FT DOMAIN 596 685 Ig-like C2-type 7.
FT DOMAIN 690 784 Ig-like C2-type 8.
FT DOMAIN 788 885 Ig-like C2-type 9.
FT DOMAIN 887 984 Fibronectin type-III 1.
FT DOMAIN 989 1088 Fibronectin type-III 2.
FT DOMAIN 1093 1189 Fibronectin type-III 3.
FT DOMAIN 1193 1288 Fibronectin type-III 4.
FT DOMAIN 1278 1377 Ig-like C2-type 10.
FT DOMAIN 1383 1477 Fibronectin type-III 5.
FT DOMAIN 1478 1578 Fibronectin type-III 6.
FT COMPBIAS 1956 2016 Pro-rich.
FT CARBOHYD 29 29 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 79 79 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 368 368 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 471 471 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 513 513 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 556 556 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 666 666 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 710 710 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 749 749 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 796 796 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 809 809 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 926 926 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1082 1082 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1144 1144 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1162 1162 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1275 1275 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1345 1345 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1492 1492 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1531 1531 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1561 1561 N-linked (GlcNAc...) (Potential).
FT DISULFID 47 103 By similarity.
FT DISULFID 146 198 By similarity.
FT DISULFID 247 294 By similarity.
FT DISULFID 336 386 By similarity.
FT DISULFID 429 485 By similarity.
FT DISULFID 526 575 By similarity.
FT DISULFID 617 669 By similarity.
FT DISULFID 711 767 By similarity.
FT DISULFID 810 867 By similarity.
FT DISULFID 1311 1363 By similarity.
FT VAR_SEQ 34 244 Missing (in isoform 2).
FT /FTId=VSP_014978.
FT VARIANT 659 659 V -> I (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035512.
FT VARIANT 1702 1702 V -> I (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035513.
FT CONFLICT 4 4 V -> L (in Ref. 3; AAN32613/AAN32614).
FT CONFLICT 150 152 SSV -> FLG (in Ref. 3; AAN32613).
FT CONFLICT 172 172 H -> N (in Ref. 1; AAL57166 and 4;
FT BAA86446).
FT CONFLICT 250 250 S -> P (in Ref. 3; AAN32614).
FT CONFLICT 469 469 H -> Y (in Ref. 3; AAN32613).
FT CONFLICT 667 667 Y -> D (in Ref. 3; AAN32613/AAN32614).
FT STRAND 991 997
FT STRAND 999 1008
FT STRAND 1021 1030
FT STRAND 1046 1055
FT STRAND 1062 1070
SQ SEQUENCE 2053 AA; 224463 MW; 9CC9644214FF19C4 CRC64;
MWLVTFLLLL DSLHKARPED VGTSLYFVND SLQQVTFSSS VGVVVPCPAA GSPSAALRWY
LATGDDIYDV PHIRHVHANG TLQLYPFSPS AFNSFIHDND YFCTAENAAG KIRSPNIRVK
AVFREPYTVR VEDQRSMRGN VAVFKCLIPS SVQEYVSVVS WEKDTVSIIP EHRFFITYHG
GLYISDVQKE DALSTYRCIT KHKYSGETRQ SNGARLSVTD PAESIPTILD GFHSQEVWAG
HTVELPCTAS GYPIPAIRWL KDGRPLPADS RWTKRITGLT ISDLRTEDSG TYICEVTNTF
GSAEATGILM VIDPLHVTLT PKKLKTGIGS TVILSCALTG SPEFTIRWYR NTELVLPDEA
ISIRGLSNET LLITSAQKSH SGAYQCFATR KAQTAQDFAI IALEDGTPRI VSSFSEKVVN
PGEQFSLMCA AKGAPPPTVT WALDDEPIVR DGSHRTNQYT MSDGTTISHM NVTGPQIRDG
GVYRCTARNL VGSAEYQARI NVRGPPSIRA MRNITAVAGR DTLINCRVIG YPYYSIKWYK
DALLLPDNHR QVVFENGTLK LTDVQKGMDE GEYLCSVLIQ PQLSISQSVH VAVKVPPLIQ
PFEFPPASIG QLLYIPCVVS SGDMPIRITW RKDGQVIISG SGVTIESKEF MSSLQISSVS
LKHNGNYTCI ASNAAATVSR ERQLIVRVPP RFVVQPNNQD GIYGKAGVLN CSVDGYPPPK
VMWKHAKGSG NPQQYHPVPL TGRIQILPNS SLLIRHVLEE DIGYYLCQAS NGVGTDISKS
MFLTVKIPAM ITSHPNTTIA IKGHAKELNC TARGERPIII RWEKGDTVID PDRVMRYAIA
TKDNGDEVVS TLKLKPADRG DSVFFSCHAI NSYGEDRGLI QLTVQEPPDP PELEIREVKA
RSMNLRWTQR FDGNSIITGF DIEYKNKSDS WDFKQSTRNI SPTINQANIV DLHPASVYSI
RMYSFNKIGR SEPSKELTIS TEEAAPDGPP MDVTLQPVTS QSIQVTWKAP KKELQNGVIR
GYQIGYRENS PGSNGQYSIV EMKATGDSEV YTLDNLKKFA QYGVVVQAFN RAGTGPSSSE
INATTLEDVP SQPPENVRAL SITSDVAVIS WSEPPRSTLN GVLKGYRVIF WSLYVDGEWG
EMQNITTTRE RVELRGMEKF TNYSVQVLAY TQAGDGVRSS VLYIQTKEDV PGPPAGIKAV
PSSASSVVVS WLPPTKPNGV IRKYTIFCSS PGSGQPAPSE YETSPEQLFY RIAHLNRGQQ
YLLWVAAVTS AGRGNSSEKV TIEPAGKAPA KIISFGGTVT TPWMKDVRLP CNSVGDPAPA
VKWTKDSEDS AIPVSMDGHR LIHTNGTLLL RAVKAEDSGY YTCTATNTGG FDTIIVNLLV
QVPPDQPRLT VSKTSASSIT LTWIPGDNGG SSIRGFVLQY SVDNSEEWKD VFISSSERSF
KLDSLKCGTW YKVKLAAKNS VGSGRISEII EAKTHGREPS FSKDQHLFTH INSTHARLNL
QGWNNGGCPI TAIVLEYRPK GTWAWQGLRA NSSGEVFLTE LREATWYELR MRACNSAGCG
NETAQFATLD YDGSTIPPIK SAQGEGDDVK KLFTIGCPVI LATLGVALLF IVRKKRKEKR
LKRLRDAKSL AEMLISKNNR SFDTPVKGPP QGPRLHIDIP RVQLLIEDKE GIKQLGDDKA
TIPVTDAEFS QAVNPQSFCT GVSLHHPTLI QSTGPLIDMS DIRPGTNPVS RKNVKSAHST
RNRYSSQWTL TKCQASTPAR TLTSDWRTVG SQHGVTVTES DSYSASLSQD TDKGRNSMVS
TESASSTYEE LARAYEHAKL EEQLQHAKFE ITECFISDSS SDQMTTGTNE NADSMTSMST
PSEPGICRFT ASPPKPQDAD RGKNVAVPIP HRANKSDYCN LPLYAKSEAF FRKADGREPC
PVVPPREASI RNLARTYHTQ ARHLTLDPAS KSLGLPHPGA PAAASTATLP QRTLAMPAPP
AGTAPPAPGP TPAEPPTAPS AAPPAPSTEP PRAGGPHTKM GGSRDSLLEM STSGVGRSQK
QGAGAYSKSY TLV
//
MIM
611782
*RECORD*
*FIELD* NO
611782
*FIELD* TI
*611782 DOWN SYNDROME CELL ADHESION MOLECULE-LIKE 1; DSCAML1
;;DSCAM-LIKE 1;;
KIAA1132
read more*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated brain cDNA
library, Hirosawa et al. (1999) obtained a partial cDNA encoding
DSCAML1, which they designated KIAA1132. RT-PCR ELISA detected moderate
expression in adult and fetal brain and in all specific adult brain
regions examined. Low expression was detected in kidney and ovary, and
little to no expression was detected in all other tissues examined.
Agarwala et al. (2001) cloned full-length DSCAML1 by screening a fetal
brain cDNA library with the partial KIAA1132 cDNA. The deduced
2,053-amino acid protein has a calculated molecular mass of 224 kD. It
has a 1,573-amino acid extracellular domain, a 21-amino acid
transmembrane domain, and a 441-amino acid cytoplasmic domain. The
extracellular domain contains 10 Ig C2-type domains, 6 fibronectin (see
135600) type III domains, 15 N-glycosylation sites, an RGD-type cell
attachment sequence, and a carboxypeptidase (see CPA1; 114850)
zinc-binding region-2. The cytoplasmic domain contains 7 putative
phosphorylation sites and 6 N-myristoylation sites. The domain
structures of DSCAML1 and DSCAM (602523) are identical, and they share
64% and 45% amino acid identity in their extracellular and cytoplasmic
domains, respectively. Northern blot analysis detected a 7.6-kb
transcript in fetal and adult brain and in all adult brain sections
examined, except amygdala. A weak signal was detected in adult kidney.
Northern blot analysis of whole mouse embryos detected expression at 17
days postcoitum and in all postnatal stages tested. In adult mouse,
expression was detected only in brain. In situ hybridization revealed
Dscaml1 in the Purkinje cell layer of mouse cerebellum, in granule cells
of the dentate gyrus and in pyramidal cells of the CA1 and CA3 regions
of the hippocampus, and in olfactory bulb, with moderate expression in
cerebral cortex and thalamus. Immunohistochemical analysis of
transfected mouse fibroblasts and rat PC12 pheochromocytoma cells showed
expression on the cell surface. In differentiated transfected PC12
cells, human DSCAML1 associated with axons, but not with dendrites.
Southern blot analysis suggested that DSCAML1 is highly conserved in
vertebrates.
By RT-PCR of adult human brain, Barlow et al. (2002) identified DSCAML1
splice variants lacking either exon 3 or 4, resulting in removal of
either the N- or C- terminal half of the Ig2 domain, respectively.
Barlow et al. (2002) noted that their full-length DSCAML1 cDNA has an
in-frame ATG 180 bp upstream of the translational start site reported by
Agarwala et al. (2001), resulting in a 60-amino acid N-terminal
extension to the protein. Northern blot analysis detected several
DSCAML1 splice variants in all human adult tissues examined. The 7.5-kb
transcript was expressed predominantly in brain, but was also present in
kidney, skeletal muscle, pancreas, and lung, along with smaller
variants. Expression was detected in all adult brain regions examined,
including amygdala. Mouse tissues showed an expression pattern
significantly different than that in human.
GENE FUNCTION
Agarwala et al. (2001) found that mouse cells expressing human DSCAML1
adhered to each other in large aggregates. Aggregation was mediated by
homophilic interactions between DSCAML1 molecules expressed on the cell
surface and did not require calcium.
Yamagata and Sanes (2008) demonstrated that 4 closely related
immunoglobulin superfamily (IgSF) adhesion molecules--Dscam (602523),
DscamL, Sidekick-1 (SDK1; 607216), and SDK2 (607217)--are expressed in
chick by nonoverlapping subsets of interneurons and retinal ganglion
cells that form synapses in distinct inner plexiform layer (IPL)
sublaminae. Moreover, each protein is concentrated within the
appropriate sublaminae and each mediates homophilic adhesion. Loss- and
gain-of-function studies in vivo indicated that these IgSF members
participate in determining the inner plexiform layer sublaminae in which
synaptic partners arborize and connect. Thus, vertebrate Dscams, like
Drosophila Dscams, play roles in neural connectivity. Yamagata and Sanes
(2008) concluded that, taken together, their results on Dscams and
Sidekicks suggested the existence of an IgSF code for laminar
specificity in retina and, by implication, in other parts of the central
nervous system.
GENE STRUCTURE
Agarwala et al. (2001) determined that the DSCAML1 gene contains at
least 32 exons. Barlow et al. (2002) identified 33 exons in DSCAML1.
MAPPING
By radiation hybrid analysis, Hirosawa et al. (1999) mapped the DSCAML1
gene to chromosome 11. Using FISH, Agarwala et al. (2001) mapped the
human DSCAML1 gene to chromosome 11q23 and the mouse Dscaml1 gene to
chromosome 9B.
*FIELD* RF
1. Agarwala, K. L.; Ganesh, S.; Tsutsumi, Y.; Suzuki, T.; Amano, K.;
Yamakawa, K.: Cloning and functional characterization of DSCAML1,
a novel DSCAM-like cell adhesion molecule that mediates homophilic
intercellular adhesion. Biochem. Biophys. Res. Commun. 285: 760-772,
2001.
2. Barlow, G. M.; Micales, B.; Chen, X.-N.; Lyons, G. E.; Korenberg,
J. R.: Mammalian DSCAMs: roles in the development of the spinal cord,
cortex, and cerebellum? Biochem. Biophys. Res. Commun. 293: 881-891,
2002.
3. Hirosawa, M.; Nagase, T.; Ishikawa, K.; Kikuno, R.; Nomura, N.;
Ohara, O.: Characterization of cDNA clones selected by the GeneMark
analysis from size-fractionated cDNA libraries from human brain. DNA
Res. 6: 329-336, 1999.
4. Yamagata, M.; Sanes, J. R.: Dscam and Sidekick proteins direct
lamina-specific synaptic connections in vertebrate retina. Nature 451:
465-469, 2008.
*FIELD* CN
Ada Hamosh - updated: 02/18/2008
*FIELD* CD
Patricia A. Hartz: 2/11/2008
*FIELD* ED
alopez: 02/18/2008
alopez: 2/18/2008
mgross: 2/11/2008
*RECORD*
*FIELD* NO
611782
*FIELD* TI
*611782 DOWN SYNDROME CELL ADHESION MOLECULE-LIKE 1; DSCAML1
;;DSCAM-LIKE 1;;
KIAA1132
read more*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated brain cDNA
library, Hirosawa et al. (1999) obtained a partial cDNA encoding
DSCAML1, which they designated KIAA1132. RT-PCR ELISA detected moderate
expression in adult and fetal brain and in all specific adult brain
regions examined. Low expression was detected in kidney and ovary, and
little to no expression was detected in all other tissues examined.
Agarwala et al. (2001) cloned full-length DSCAML1 by screening a fetal
brain cDNA library with the partial KIAA1132 cDNA. The deduced
2,053-amino acid protein has a calculated molecular mass of 224 kD. It
has a 1,573-amino acid extracellular domain, a 21-amino acid
transmembrane domain, and a 441-amino acid cytoplasmic domain. The
extracellular domain contains 10 Ig C2-type domains, 6 fibronectin (see
135600) type III domains, 15 N-glycosylation sites, an RGD-type cell
attachment sequence, and a carboxypeptidase (see CPA1; 114850)
zinc-binding region-2. The cytoplasmic domain contains 7 putative
phosphorylation sites and 6 N-myristoylation sites. The domain
structures of DSCAML1 and DSCAM (602523) are identical, and they share
64% and 45% amino acid identity in their extracellular and cytoplasmic
domains, respectively. Northern blot analysis detected a 7.6-kb
transcript in fetal and adult brain and in all adult brain sections
examined, except amygdala. A weak signal was detected in adult kidney.
Northern blot analysis of whole mouse embryos detected expression at 17
days postcoitum and in all postnatal stages tested. In adult mouse,
expression was detected only in brain. In situ hybridization revealed
Dscaml1 in the Purkinje cell layer of mouse cerebellum, in granule cells
of the dentate gyrus and in pyramidal cells of the CA1 and CA3 regions
of the hippocampus, and in olfactory bulb, with moderate expression in
cerebral cortex and thalamus. Immunohistochemical analysis of
transfected mouse fibroblasts and rat PC12 pheochromocytoma cells showed
expression on the cell surface. In differentiated transfected PC12
cells, human DSCAML1 associated with axons, but not with dendrites.
Southern blot analysis suggested that DSCAML1 is highly conserved in
vertebrates.
By RT-PCR of adult human brain, Barlow et al. (2002) identified DSCAML1
splice variants lacking either exon 3 or 4, resulting in removal of
either the N- or C- terminal half of the Ig2 domain, respectively.
Barlow et al. (2002) noted that their full-length DSCAML1 cDNA has an
in-frame ATG 180 bp upstream of the translational start site reported by
Agarwala et al. (2001), resulting in a 60-amino acid N-terminal
extension to the protein. Northern blot analysis detected several
DSCAML1 splice variants in all human adult tissues examined. The 7.5-kb
transcript was expressed predominantly in brain, but was also present in
kidney, skeletal muscle, pancreas, and lung, along with smaller
variants. Expression was detected in all adult brain regions examined,
including amygdala. Mouse tissues showed an expression pattern
significantly different than that in human.
GENE FUNCTION
Agarwala et al. (2001) found that mouse cells expressing human DSCAML1
adhered to each other in large aggregates. Aggregation was mediated by
homophilic interactions between DSCAML1 molecules expressed on the cell
surface and did not require calcium.
Yamagata and Sanes (2008) demonstrated that 4 closely related
immunoglobulin superfamily (IgSF) adhesion molecules--Dscam (602523),
DscamL, Sidekick-1 (SDK1; 607216), and SDK2 (607217)--are expressed in
chick by nonoverlapping subsets of interneurons and retinal ganglion
cells that form synapses in distinct inner plexiform layer (IPL)
sublaminae. Moreover, each protein is concentrated within the
appropriate sublaminae and each mediates homophilic adhesion. Loss- and
gain-of-function studies in vivo indicated that these IgSF members
participate in determining the inner plexiform layer sublaminae in which
synaptic partners arborize and connect. Thus, vertebrate Dscams, like
Drosophila Dscams, play roles in neural connectivity. Yamagata and Sanes
(2008) concluded that, taken together, their results on Dscams and
Sidekicks suggested the existence of an IgSF code for laminar
specificity in retina and, by implication, in other parts of the central
nervous system.
GENE STRUCTURE
Agarwala et al. (2001) determined that the DSCAML1 gene contains at
least 32 exons. Barlow et al. (2002) identified 33 exons in DSCAML1.
MAPPING
By radiation hybrid analysis, Hirosawa et al. (1999) mapped the DSCAML1
gene to chromosome 11. Using FISH, Agarwala et al. (2001) mapped the
human DSCAML1 gene to chromosome 11q23 and the mouse Dscaml1 gene to
chromosome 9B.
*FIELD* RF
1. Agarwala, K. L.; Ganesh, S.; Tsutsumi, Y.; Suzuki, T.; Amano, K.;
Yamakawa, K.: Cloning and functional characterization of DSCAML1,
a novel DSCAM-like cell adhesion molecule that mediates homophilic
intercellular adhesion. Biochem. Biophys. Res. Commun. 285: 760-772,
2001.
2. Barlow, G. M.; Micales, B.; Chen, X.-N.; Lyons, G. E.; Korenberg,
J. R.: Mammalian DSCAMs: roles in the development of the spinal cord,
cortex, and cerebellum? Biochem. Biophys. Res. Commun. 293: 881-891,
2002.
3. Hirosawa, M.; Nagase, T.; Ishikawa, K.; Kikuno, R.; Nomura, N.;
Ohara, O.: Characterization of cDNA clones selected by the GeneMark
analysis from size-fractionated cDNA libraries from human brain. DNA
Res. 6: 329-336, 1999.
4. Yamagata, M.; Sanes, J. R.: Dscam and Sidekick proteins direct
lamina-specific synaptic connections in vertebrate retina. Nature 451:
465-469, 2008.
*FIELD* CN
Ada Hamosh - updated: 02/18/2008
*FIELD* CD
Patricia A. Hartz: 2/11/2008
*FIELD* ED
alopez: 02/18/2008
alopez: 2/18/2008
mgross: 2/11/2008