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Entry version 118 (12 Aug 2020)
Sequence version 1 (01 Mar 2002)
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Protein

Down syndrome cell adhesion molecule homolog

Gene

Dscam

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (By similarity). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (PubMed:18585357). Might also collaborate with UNC5C in NTN1-mediated axon repulsion independently of DCC (By similarity). In spinal cord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding. Enhances netrin-induced phosphorylation of PAK1 and FYN. Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38 (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).By similarity1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion, Neurogenesis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-376172, DSCAM interactions

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Down syndrome cell adhesion molecule homolog
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Dscam
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
619992, Dscam

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini19 – 1594ExtracellularSequence analysisAdd BLAST1576
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1595 – 1615HelicalSequence analysisAdd BLAST21
Topological domaini1616 – 2013CytoplasmicSequence analysisAdd BLAST398

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Synapse

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000039247918 – 2013Down syndrome cell adhesion molecule homologAdd BLAST1996

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi46 ↔ 102PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi78N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi145 ↔ 197PROSITE-ProRule annotation
Disulfide bondi246 ↔ 293PROSITE-ProRule annotation
Disulfide bondi335 ↔ 385PROSITE-ProRule annotation
Disulfide bondi428 ↔ 484PROSITE-ProRule annotation
Glycosylationi470N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi525 ↔ 575PROSITE-ProRule annotation
Disulfide bondi617 ↔ 669PROSITE-ProRule annotation
Glycosylationi666N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi711 ↔ 766PROSITE-ProRule annotation
Disulfide bondi809 ↔ 865PROSITE-ProRule annotation
Glycosylationi1160N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1250N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1307 ↔ 1359PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated at tyrosine residues. Phosphorylation is enhanced by NTN1.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q8VHZ8

PRoteomics IDEntifications database

More...
PRIDEi
Q8VHZ8

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
Q8VHZ8

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q8VHZ8, 5 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8VHZ8

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q8VHZ8

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in spinal cord at 11 dpc. Expressed in precrossing commissural axons and growth cones of neurons that crossed the midline at 12 dpc. Expressed in axons coursing in the ventral and dorsal funiculus ar 13 dpc. Expressed in postcrossing axons at 15 dpc (at protein level).1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity).

Interacts with DCC; the interaction is abolished in response to NTN1 (By similarity).

Interacts (via extracellular domain) with NTN1 (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (By similarity).

Interacts (via cytoplasmic domain) with PAK1; the interaction is direct and enhanced in presence of RAC1 (By similarity).

Interacts with RAC1; the interaction requires PAK1 (By similarity).

Interacts (via extracellular domain) with UNC5C (via Ig-like C2-type domain) (By similarity).

Interacts with PTK2 (By similarity).

Interacts with FYN (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q8VHZ8, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000002215

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q8VHZ8

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini20 – 119Ig-like C2-type 1Add BLAST100
Domaini125 – 216Ig-like C2-type 2Add BLAST92
Domaini225 – 305Ig-like C2-type 3Add BLAST81
Domaini313 – 401Ig-like C2-type 4Add BLAST89
Domaini407 – 500Ig-like C2-type 5Add BLAST94
Domaini504 – 592Ig-like C2-type 6Add BLAST89
Domaini596 – 685Ig-like C2-type 7Add BLAST90
Domaini690 – 783Ig-like C2-type 8Add BLAST94
Domaini787 – 883Ig-like C2-type 9Add BLAST97
Domaini885 – 982Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST98
Domaini987 – 1086Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST100
Domaini1091 – 1187Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST97
Domaini1191 – 1285Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST95
Domaini1285 – 1377Ig-like C2-type 10Add BLAST93
Domaini1379 – 1473Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST95
Domaini1474 – 1575Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST102

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1616 – 2013Required for netrin-mediated axon repulsion of neuronal growth conesBy similarityAdd BLAST398

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1617 – 1621Poly-Arg5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Ig-like C2-type domains 7 to 9 are sufficient for interaction with NTN1 and commissural axon outgrowth. The transmembrane domain is necessary for interaction with DCC (By similarity).By similarity

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3510, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8VHZ8

KEGG Orthology (KO)

More...
KOi
K06767

Database of Orthologous Groups

More...
OrthoDBi
14047at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8VHZ8

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00063, FN3, 6 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 16 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR043204, Basigin-like
IPR033027, DSCAM_chordates
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR007110, Ig-like_dom
IPR036179, Ig-like_dom_sf
IPR013783, Ig-like_fold
IPR013098, Ig_I-set
IPR003599, Ig_sub
IPR003598, Ig_sub2
IPR013106, Ig_V-set

The PANTHER Classification System

More...
PANTHERi
PTHR10075, PTHR10075, 1 hit
PTHR10075:SF51, PTHR10075:SF51, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00041, fn3, 5 hits
PF07679, I-set, 6 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00060, FN3, 6 hits
SM00409, IG, 9 hits
SM00408, IGc2, 9 hits
SM00406, IGv, 4 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726, SSF48726, 10 hits
SSF49265, SSF49265, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50853, FN3, 6 hits
PS50835, IG_LIKE, 10 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q8VHZ8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWILALSLFQ SFANVFSEEP HSSLYFVNAS LQEVVFASTS GTLVPCPAAG
60 70 80 90 100
IPPVTLRWYL ATGEEIYDVP GIRHVHPNGT LQIFPFPPSS FSTLIHDNTY
110 120 130 140 150
YCTAENPSGK IRSQDVHIKA VLREPYTVRV EDQKTMRGNV AVFKCIIPSS
160 170 180 190 200
VEAYVTVVSW EKDTVSLVSG SRFLITSTGA LYIKDVQNED GLYNYRCITR
210 220 230 240 250
HRYTGETRQS NSARLFVSDP ANSAPSILDG FDHRKAMAGQ RVELPCKALG
260 270 280 290 300
HPEPDYRWLK DNMPLELSGR FQKTVTGLLI ENSRPSDSGS YVCEVSNRYG
310 320 330 340 350
TAKVIGRLYV KQPLKATISP RKVKSSVGSQ VSLSCSVTGN EDQELSWYRN
360 370 380 390 400
GEILNPGKNV RITGLNHANL IMDHMVKSDG GAYQCFVRKD KLSAQDYVQV
410 420 430 440 450
VLEDGTPKII SAFSEKVVSP AEPVSLVCNV KGTPLPTVTW TLDDDPILKG
460 470 480 490 500
SGHRISQMIT SEGNVVSYLN ISSSQVRDGG VYRCTANNSA GVVLYQARIN
510 520 530 540 550
VRGPASIRPM KNITAIAGRD TYIHCRVIGY PYYSIKWYKN ANLLPFNHRQ
560 570 580 590 600
VAFENNGTLK LSDVQKEVDE GEYTCNVLVQ PQLSTSQSVH VTVKVPPFIQ
610 620 630 640 650
PFEFPRFSIG QRVFIPCVVV SGDLPITITW QKDGRPIPAS LGVTIDNIDF
660 670 680 690 700
TSSLRISNLS LMHNGNYTCI ARNEAAAVEH QSQLIVRVPP KFVVQPRDQD
710 720 730 740 750
GIYGKAVILN CSAEGYPVPT IVWKFSKGAG VPQFQPIALN GRIQVLSNGS
760 770 780 790 800
LLIKHVVEED SGYYLCKVSN DVGADVSKSM YLTVKIPAMI TSYPNTTLAT
810 820 830 840 850
QGQRKEMSCT AHGEKPIIVR WEKEDRIINP EMARYLVSTK EVGEEVISTL
860 870 880 890 900
QILPTVREDS GFFSCHAINS YGEDRGIIQL TVQEPPDPPE IEIKDVKART
910 920 930 940 950
ITLRWTMGFD GNSPITGYDI ECKNKSDSWD SAQRTKDVSP QLNSATIIDI
960 970 980 990 1000
HPSSTYSIRM YAKNRIGKSE PSNEITITAD EAAPDGPPQE VHLEPTSSQS
1010 1020 1030 1040 1050
IRVTWKAPKK HLQNGIIRGY QIGYREYSTG GNFQFNIISI DTTGDSEVYT
1060 1070 1080 1090 1100
LDNLNKFTQY GLVVQACNRA GTGPSSQEII TTTLEDVPSY PPENVQAIAT
1110 1120 1130 1140 1150
SPESISISWS TLSKEALNGI LQGFRVIYWA NLIDGELGEI KNVTTTQPSL
1160 1170 1180 1190 1200
ELDGLEKYTN YSIQVLAFTR AGDGVRSEQI FTRTKEDVPG PPAGVKAAAA
1210 1220 1230 1240 1250
SASMVFVSWL PPLKLNGIIR KYTVFCSHPY PTVISEFEAS PDSFSYRIPN
1260 1270 1280 1290 1300
LSRNRQYSVW VVAVTSAGRG NSSEIITVEP LAKAPARILT FSGTVTTPWM
1310 1320 1330 1340 1350
KDIVLPCKAV GDPSPAVKWM KDSNGTPSLV TIDGRRSIFS NGSFVIRTVK
1360 1370 1380 1390 1400
AEDSGYYSCV ANNNWGSDEI ILNLQVQVPP DQPRLTVSKT TSSSITLSWL
1410 1420 1430 1440 1450
PGDNGGSSIR GYILQYSEDN SEQWGSFPIS PSERSYRLEN LKCGTWYKFT
1460 1470 1480 1490 1500
LTAQNGVGPG RISEIIEAKT LGKEPQFSKE QELFASINTT RVRLNLIGWN
1510 1520 1530 1540 1550
DGGCPITSFT LEYRPFGTTV WTTAQRTSLS KSYILYDLQE ATWYELQMRV
1560 1570 1580 1590 1600
CNSAGCAEKQ ANFATLNYDG STIPPLIKSV VQSEEGLTTN EGLKILVTIS
1610 1620 1630 1640 1650
CILVGVLLLF VLLLVVRRRR REQRLKRLRD AKSLAEMLMS KNTRTSDTLS
1660 1670 1680 1690 1700
KQQQTLRMHI DIPRAQLLIE ERDTMETIDD RSTVLLTDAD FGEAAKQKSL
1710 1720 1730 1740 1750
TVTHTVHYQS VSQATGPLVD VSDARPGTNP TTRRNAKAGP TARNRYASQW
1760 1770 1780 1790 1800
TLNRPHPTIS AHTLTTDWRL PTPRATGSVD KESDSYSVSP SQDTDRARSS
1810 1820 1830 1840 1850
MVSTESASST YEELARAYEH AKMEEQLRHA KFTITECFIS DTSSEQLTAG
1860 1870 1880 1890 1900
TNEYTDSLTS STPSESGICR FTASPPKPQD GGRVVNMAVP KAHRPGDLIH
1910 1920 1930 1940 1950
LPPYLRMDFL LNRGAPGTSR DLSLGQACLE PQKSRTLKRP TVLEPTPMEA
1960 1970 1980 1990 2000
SSSTSSTREG QQSWQQGAVA TLPQREGAEL GQAAKMSSSQ ESLLDSRGHL
2010
KGNNPYAKSY TLV
Length:2,013
Mass (Da):222,254
Last modified:March 1, 2002 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i92E76AE44CE0929A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1M9F4F1M9F4_RAT
Down syndrome cell adhesion molecul...
Dscam
1,849Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF334385 mRNA Translation: AAL57167.1

NCBI Reference Sequences

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RefSeqi
NP_598271.1, NM_133587.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
171119

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:171119

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF334385 mRNA Translation: AAL57167.1
RefSeqiNP_598271.1, NM_133587.1

3D structure databases

SMRiQ8VHZ8
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ8VHZ8, 1 interactor
STRINGi10116.ENSRNOP00000002215

PTM databases

CarbonylDBiQ8VHZ8
GlyGeniQ8VHZ8, 5 sites
iPTMnetiQ8VHZ8
PhosphoSitePlusiQ8VHZ8

Proteomic databases

PaxDbiQ8VHZ8
PRIDEiQ8VHZ8

Genome annotation databases

GeneIDi171119
KEGGirno:171119

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1826
RGDi619992, Dscam

Phylogenomic databases

eggNOGiKOG3510, Eukaryota
InParanoidiQ8VHZ8
KOiK06767
OrthoDBi14047at2759
PhylomeDBiQ8VHZ8

Enzyme and pathway databases

ReactomeiR-RNO-376172, DSCAM interactions

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q8VHZ8

Family and domain databases

CDDicd00063, FN3, 6 hits
Gene3Di2.60.40.10, 16 hits
InterProiView protein in InterPro
IPR043204, Basigin-like
IPR033027, DSCAM_chordates
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR007110, Ig-like_dom
IPR036179, Ig-like_dom_sf
IPR013783, Ig-like_fold
IPR013098, Ig_I-set
IPR003599, Ig_sub
IPR003598, Ig_sub2
IPR013106, Ig_V-set
PANTHERiPTHR10075, PTHR10075, 1 hit
PTHR10075:SF51, PTHR10075:SF51, 1 hit
PfamiView protein in Pfam
PF00041, fn3, 5 hits
PF07679, I-set, 6 hits
SMARTiView protein in SMART
SM00060, FN3, 6 hits
SM00409, IG, 9 hits
SM00408, IGc2, 9 hits
SM00406, IGv, 4 hits
SUPFAMiSSF48726, SSF48726, 10 hits
SSF49265, SSF49265, 3 hits
PROSITEiView protein in PROSITE
PS50853, FN3, 6 hits
PS50835, IG_LIKE, 10 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDSCAM_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8VHZ8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 1, 2002
Last modified: August 12, 2020
This is version 118 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome
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