DSCL1_MOUSE
ID DSCL1_MOUSE Reviewed; 2053 AA.
AC Q4VA61;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cell adhesion molecule DSCAML1 {ECO:0000305};
DE AltName: Full=Down syndrome cell adhesion molecule-like protein 1 homolog;
DE Flags: Precursor;
GN Name=Dscaml1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 723-2053.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19945391; DOI=10.1016/j.neuron.2009.09.027;
RA Fuerst P.G., Bruce F., Tian M., Wei W., Elstrott J., Feller M.B.,
RA Erskine L., Singer J.H., Burgess R.W.;
RT "DSCAM and DSCAML1 function in self-avoidance in multiple cell types in the
RT developing mouse retina.";
RL Neuron 64:484-497(2009).
CC -!- FUNCTION: Cell adhesion molecule that plays a role in neuronal self-
CC avoidance. Promotes repulsion between specific neuronal processes of
CC either the same cell or the same subtype of cells. Promotes both
CC isoneuronal self-avoidance for creating an orderly neurite arborization
CC in retinal rod bipolar cells and heteroneuronal self-avoidance to
CC maintain mosaic spacing between AII amacrine cells (PubMed:19945391).
CC Adhesion molecule that promotes lamina-specific synaptic connections in
CC the retina: expressed in specific subsets of interneurons and retinal
CC ganglion cells (RGCs) and promotes synaptic connectivity via homophilic
CC interactions (By similarity). {ECO:0000250|UniProtKB:E1C8P7,
CC ECO:0000269|PubMed:19945391}.
CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC adhesion. {ECO:0000250|UniProtKB:E1C8P7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TD84};
CC Single-pass type I membrane protein {ECO:0000305}. Synapse
CC {ECO:0000250|UniProtKB:E1C8P7}.
CC -!- TISSUE SPECIFICITY: In the retina, expressed in the rod photoreceptors,
CC AII amacrine cells and rod bipolar cells (at protein level).
CC {ECO:0000269|PubMed:19945391}.
CC -!- DISRUPTION PHENOTYPE: The inner nuclear and inner plexiform layers in
CC the retina are disorganised at postnatal day 20 (P20). AII amacrine
CC cell populations are randomly distributed or pulled into clumps and rod
CC bipolar show fasciculated dendrites. {ECO:0000269|PubMed:19945391}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH96527.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC119237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC174644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096527; AAH96527.1; ALT_INIT; mRNA.
DR CCDS; CCDS40608.1; -.
DR AlphaFoldDB; Q4VA61; -.
DR SMR; Q4VA61; -.
DR STRING; 10090.ENSMUSP00000034592; -.
DR GlyConnect; 2267; 4 N-Linked glycans (4 sites).
DR GlyGen; Q4VA61; 11 sites, 4 N-linked glycans (4 sites).
DR jPOST; Q4VA61; -.
DR PaxDb; Q4VA61; -.
DR PRIDE; Q4VA61; -.
DR ProteomicsDB; 277409; -.
DR Antibodypedia; 62371; 26 antibodies from 15 providers.
DR Ensembl; ENSMUST00000034592; ENSMUSP00000034592; ENSMUSG00000032087.
DR UCSC; uc009pga.1; mouse.
DR MGI; MGI:2150309; Dscaml1.
DR VEuPathDB; HostDB:ENSMUSG00000032087; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155354; -.
DR InParanoid; Q4VA61; -.
DR PhylomeDB; Q4VA61; -.
DR Reactome; R-MMU-376172; DSCAM interactions.
DR ChiTaRS; Dscaml1; mouse.
DR PRO; PR:Q4VA61; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q4VA61; protein.
DR Bgee; ENSMUSG00000032087; Expressed in retinal neural layer and 123 other tissues.
DR ExpressionAtlas; Q4VA61; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; ISO:MGI.
DR GO; GO:0070593; P:dendrite self-avoidance; IMP:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISO:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP:UniProtKB.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 16.
DR InterPro; IPR033029; DSCAML1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR13817:SF54; PTHR13817:SF54; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 10.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 10.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 9.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..2053
FT /note="Cell adhesion molecule DSCAML1"
FT /id="PRO_0000392480"
FT TOPO_DOM 19..1591
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1592..1612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1613..2053
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..119
FT /note="Ig-like C2-type 1"
FT DOMAIN 115..217
FT /note="Ig-like C2-type 2"
FT DOMAIN 226..310
FT /note="Ig-like C2-type 3"
FT DOMAIN 314..396
FT /note="Ig-like C2-type 4"
FT DOMAIN 408..501
FT /note="Ig-like C2-type 5"
FT DOMAIN 506..586
FT /note="Ig-like C2-type 6"
FT DOMAIN 596..685
FT /note="Ig-like C2-type 7"
FT DOMAIN 690..784
FT /note="Ig-like C2-type 8"
FT DOMAIN 788..885
FT /note="Ig-like C2-type 9"
FT DOMAIN 887..984
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 989..1088
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1093..1189
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1193..1288
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1278..1377
FT /note="Ig-like C2-type 10"
FT DOMAIN 1383..1477
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1478..1578
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1716..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1974..2053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2011
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 146..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 247..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 336..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 429..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 526..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 617..669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 711..767
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 810..867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1311..1363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 2053 AA; 224240 MW; 0C0806C47D7ADCD6 CRC64;
MWLVTFLLLL DSLHKARPED VGTSLYFVND SLQHVTFSSS VGVVVPCPAA GSPSAALRWY
LATGDDIYDV PHIRHVHANG TLQLFPFSPS AFNSFIHDND YFCTAENAAG KIRSPNIRIK
AVFREPYTVR VEDQRSMRGN VAVFKCLIPS SVQEYVSVVS WEKDTVSITP ENRFFITSHG
GLYISDVQKE DALSTYRCIT QHKYSGETRQ SNGARLSVTD PAESIPTILD GFHSQEVWTG
HSVELPCAAS GYPIPAIRWL KDGRPLPADS RWAKRITGLT ISDLRTEDSG TYICEVTNTF
GSAEANGILT VIDPLHVTLT PKKLKTGIGS TVILSCALTG SPEFTIRWYR NTELVLPGEA
ISIRGLSNET LLISSAQKSH SGAYQCFATR KAQTAQDFAI IVLEDGTPRI VSSFSEKVVN
PGEQFSLMCA AKGAPPPTVT WALDDEPVVR DGSHRTNQYT MSDGTTISHM NVTGPQIRDG
GVYRCTARNS 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 NGVGTDISKA
MFLTVKIPAM ITSHPNTTIA IKGHPKELNC 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
EMQNVTTTRE RVELRGMEKF TNYSVQVLAY TQAGDGVRSS VLYIQTKEDV PGPPAGIKAV
PSSASSVVVS WLPPTKPNGV IRKYTIFCSS PGSGQPAPSE YETSPEQLFY RIAHLNRGQQ
YLLWVAAVTS AGRGNSSEKV TIEPAGKAPA KIISFGGTVT TPWMKDVRLP CNSVGDPAPA
VKWTKDSEDS AIPVSLDGHR LIHTNGTLLL RAVKAEDSGY YTCTATNTGG FDTIIVNLLV
QVPPDQPRLT VSKTSASSIT LTWIPGDNGG SSIRGFVLQY SVDNSEEWKD VFISSSERSF
KLDSLKCGTW YKVKLAAKNS VGSGRISEII EAKTHGREPS FSKDQHLFTH INSTHARLNL
QGWNNGGCPI TAIVLEYRPK GTWAWQGVRA NSSTEVFLTE LREATWYELR MRACNSAGCG
NETAQFATLD YDGSTIPPIK SAQGEGDDVK KLFTIGCPVI LATLGVALLF VVRKKRKEKR
LKRLRDAKSL AEMLISKNNR SFDTPVKGPP QGPRLHIDIP RVQLLIEDKE GIKQLGDDKA
TIPVTDAEFS QAVNPQSFCT GVSLHHPALI QSTGPLIDMS DIRPGTNPVS RKNVKSAHST
RNRYSSQWTL TKCQASTPAR TLTSDWRTVG SQHGVTVTES DSYSASLSQD TDKGRNSMVS
TESASSTYEE LARAYEHAKL EEQLQHAKFE ITECFISDSS SDQMTTGTNE NADSMTSMST
PSEPGICRFT ASPPKPQDAD RGKNVAVPIP HRANKSDYCN LPLYTKSEAF FRKADGREPC
PVVPPREASM RNLTRAYHTQ ARHLTLDPAS KPLGLPHPGA TAATATATLP QRTLAMPAPP
AGTAPPAPGP TPSEPSAAPS AAPPAPSTEP PRAGGPHTKM GGSRDSLLEM STPGVGRSQK
QGAGAYSKSY TLV
