DSCAM_RAT
ID DSCAM_RAT Reviewed; 2013 AA.
AC Q8VHZ8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cell adhesion molecule DSCAM {ECO:0000305};
DE AltName: Full=Down syndrome cell adhesion molecule homolog;
DE Flags: Precursor;
GN Name=Dscam;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Agarwala K.L., Tsutsumi Y., Amano K., Suzuki T., Yamakawa K.;
RT "Rat homolog for Down syndrome cell adhesion molecule (Dscam) mRNA,
RT complete cds.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18585357; DOI=10.1016/j.cell.2008.05.030;
RA Ly A., Nikolaev A., Suresh G., Zheng Y., Tessier-Lavigne M., Stein E.;
RT "DSCAM is a netrin receptor that collaborates with DCC in mediating turning
RT responses to netrin-1.";
RL Cell 133:1241-1254(2008).
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. Mediates within
CC retinal amacrine and ganglion cell subtypes both isoneuronal self-
CC avoidance for creating an orderly dendritic arborization and
CC heteroneuronal self-avoidance to maintain the mosaic spacing between
CC amacrine and ganglion cell bodies (By similarity). Receptor for netrin
CC required for axon guidance independently of and in collaboration with
CC the receptor DCC (PubMed:18585357). Might also collaborate with UNC5C
CC in NTN1-mediated axon repulsion independently of DCC (By similarity).
CC In spinal cord development plays a role in guiding commissural axons
CC projection and pathfinding across the ventral midline to reach the
CC floor plate upon ligand binding. Enhances netrin-induced
CC phosphorylation of PAK1 and FYN. Mediates intracellular signaling by
CC stimulating the activation of MAPK8 and MAP kinase p38 (By similarity).
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:F1NY98,
CC ECO:0000250|UniProtKB:O60469, ECO:0000250|UniProtKB:Q9ERC8,
CC ECO:0000269|PubMed:18585357}.
CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC adhesion (By similarity). Interacts with DCC; the interaction is
CC abolished in response to NTN1 (By similarity). Interacts (via
CC extracellular domain) with NTN1 (By similarity). Probably found in a
CC ternary complex composed of DSCAM, PAK1 and RAC1 (By similarity).
CC Interacts (via cytoplasmic domain) with PAK1; the interaction is direct
CC and enhanced in presence of RAC1 (By similarity). Interacts with RAC1;
CC the interaction requires PAK1 (By similarity). Interacts (via
CC extracellular domain) with UNC5C (via Ig-like C2-type domain) (By
CC similarity). Interacts with PTK2 (By similarity). Interacts with FYN
CC (By similarity). {ECO:0000250|UniProtKB:F1NY98,
CC ECO:0000250|UniProtKB:O60469, ECO:0000250|UniProtKB:Q9ERC8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ERC8};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9ERC8}.
CC Cell projection, axon {ECO:0000250|UniProtKB:Q9ERC8}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:Q9ERC8}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9ERC8}. Synapse {ECO:0000250|UniProtKB:F1NY98}.
CC Note=Localized in the soma, cell membrane, axon and growth cone of
CC dissociated commissural axons. {ECO:0000250|UniProtKB:Q9ERC8}.
CC -!- DEVELOPMENTAL STAGE: Expressed in spinal cord at 11 dpc. Expressed in
CC precrossing commissural axons and growth cones of neurons that crossed
CC the midline at 12 dpc. Expressed in axons coursing in the ventral and
CC dorsal funiculus ar 13 dpc. Expressed in postcrossing axons at 15 dpc
CC (at protein level). {ECO:0000269|PubMed:18585357}.
CC -!- DOMAIN: Ig-like C2-type domains 7 to 9 are sufficient for interaction
CC with NTN1 and commissural axon outgrowth. The transmembrane domain is
CC necessary for interaction with DCC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at tyrosine residues. Phosphorylation is enhanced
CC by NTN1. {ECO:0000250|UniProtKB:O60469}.
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DR EMBL; AF334385; AAL57167.1; -; mRNA.
DR RefSeq; NP_598271.1; NM_133587.1.
DR AlphaFoldDB; Q8VHZ8; -.
DR SMR; Q8VHZ8; -.
DR IntAct; Q8VHZ8; 1.
DR STRING; 10116.ENSRNOP00000002215; -.
DR CarbonylDB; Q8VHZ8; -.
DR GlyGen; Q8VHZ8; 5 sites.
DR iPTMnet; Q8VHZ8; -.
DR PhosphoSitePlus; Q8VHZ8; -.
DR PaxDb; Q8VHZ8; -.
DR PRIDE; Q8VHZ8; -.
DR Ensembl; ENSRNOT00000094934; ENSRNOP00000085284; ENSRNOG00000027992.
DR GeneID; 171119; -.
DR KEGG; rno:171119; -.
DR CTD; 1826; -.
DR RGD; 619992; Dscam.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000154678; -.
DR InParanoid; Q8VHZ8; -.
DR OrthoDB; 14047at2759; -.
DR PhylomeDB; Q8VHZ8; -.
DR Reactome; R-RNO-376172; DSCAM interactions.
DR PRO; PR:Q8VHZ8; -.
DR Proteomes; UP000002494; Chromosome 11.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:1990890; F:netrin receptor binding; ISO:RGD.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0070593; P:dendrite self-avoidance; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0038007; P:netrin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IMP:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0060060; P:post-embryonic retina morphogenesis in camera-type eye; ISO:RGD.
DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 16.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR033027; DSCAM_metazoan.
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; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF51; PTHR10075:SF51; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 5.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 9.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00406; IGv; 4.
DR SUPFAM; SSF48726; SSF48726; 10.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 10.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..2013
FT /note="Cell adhesion molecule DSCAM"
FT /id="PRO_0000392479"
FT TOPO_DOM 19..1594
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1595..1615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1616..2013
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..119
FT /note="Ig-like C2-type 1"
FT DOMAIN 125..216
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..305
FT /note="Ig-like C2-type 3"
FT DOMAIN 313..401
FT /note="Ig-like C2-type 4"
FT DOMAIN 407..500
FT /note="Ig-like C2-type 5"
FT DOMAIN 504..592
FT /note="Ig-like C2-type 6"
FT DOMAIN 596..685
FT /note="Ig-like C2-type 7"
FT DOMAIN 690..783
FT /note="Ig-like C2-type 8"
FT DOMAIN 787..883
FT /note="Ig-like C2-type 9"
FT DOMAIN 885..982
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 987..1086
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1091..1187
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1191..1285
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1285..1377
FT /note="Ig-like C2-type 10"
FT DOMAIN 1379..1473
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1474..1575
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1616..2013
FT /note="Required for netrin-mediated axon repulsion of
FT neuronal growth cones"
FT /evidence="ECO:0000250|UniProtKB:Q9ERC8"
FT REGION 1718..1809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1946..1970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..1997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
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 1160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 145..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 246..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 335..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 428..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 525..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 617..669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 711..766
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 809..865
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1307..1359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 2013 AA; 222254 MW; 92E76AE44CE0929A CRC64;
MWILALSLFQ SFANVFSEEP HSSLYFVNAS LQEVVFASTS GTLVPCPAAG IPPVTLRWYL
ATGEEIYDVP GIRHVHPNGT LQIFPFPPSS FSTLIHDNTY YCTAENPSGK IRSQDVHIKA
VLREPYTVRV EDQKTMRGNV AVFKCIIPSS VEAYVTVVSW EKDTVSLVSG SRFLITSTGA
LYIKDVQNED GLYNYRCITR HRYTGETRQS NSARLFVSDP ANSAPSILDG FDHRKAMAGQ
RVELPCKALG HPEPDYRWLK DNMPLELSGR FQKTVTGLLI ENSRPSDSGS YVCEVSNRYG
TAKVIGRLYV KQPLKATISP RKVKSSVGSQ VSLSCSVTGN EDQELSWYRN GEILNPGKNV
RITGLNHANL IMDHMVKSDG GAYQCFVRKD KLSAQDYVQV VLEDGTPKII SAFSEKVVSP
AEPVSLVCNV KGTPLPTVTW TLDDDPILKG SGHRISQMIT SEGNVVSYLN ISSSQVRDGG
VYRCTANNSA GVVLYQARIN VRGPASIRPM KNITAIAGRD TYIHCRVIGY PYYSIKWYKN
ANLLPFNHRQ VAFENNGTLK LSDVQKEVDE GEYTCNVLVQ PQLSTSQSVH VTVKVPPFIQ
PFEFPRFSIG QRVFIPCVVV SGDLPITITW QKDGRPIPAS LGVTIDNIDF TSSLRISNLS
LMHNGNYTCI ARNEAAAVEH QSQLIVRVPP KFVVQPRDQD GIYGKAVILN CSAEGYPVPT
IVWKFSKGAG VPQFQPIALN GRIQVLSNGS LLIKHVVEED SGYYLCKVSN DVGADVSKSM
YLTVKIPAMI TSYPNTTLAT QGQRKEMSCT AHGEKPIIVR WEKEDRIINP EMARYLVSTK
EVGEEVISTL QILPTVREDS GFFSCHAINS YGEDRGIIQL TVQEPPDPPE IEIKDVKART
ITLRWTMGFD GNSPITGYDI ECKNKSDSWD SAQRTKDVSP QLNSATIIDI HPSSTYSIRM
YAKNRIGKSE PSNEITITAD EAAPDGPPQE VHLEPTSSQS IRVTWKAPKK HLQNGIIRGY
QIGYREYSTG GNFQFNIISI DTTGDSEVYT LDNLNKFTQY GLVVQACNRA GTGPSSQEII
TTTLEDVPSY PPENVQAIAT SPESISISWS TLSKEALNGI LQGFRVIYWA NLIDGELGEI
KNVTTTQPSL ELDGLEKYTN YSIQVLAFTR AGDGVRSEQI FTRTKEDVPG PPAGVKAAAA
SASMVFVSWL PPLKLNGIIR KYTVFCSHPY PTVISEFEAS PDSFSYRIPN LSRNRQYSVW
VVAVTSAGRG NSSEIITVEP LAKAPARILT FSGTVTTPWM KDIVLPCKAV GDPSPAVKWM
KDSNGTPSLV TIDGRRSIFS NGSFVIRTVK AEDSGYYSCV ANNNWGSDEI ILNLQVQVPP
DQPRLTVSKT TSSSITLSWL PGDNGGSSIR GYILQYSEDN SEQWGSFPIS PSERSYRLEN
LKCGTWYKFT LTAQNGVGPG RISEIIEAKT LGKEPQFSKE QELFASINTT RVRLNLIGWN
DGGCPITSFT LEYRPFGTTV WTTAQRTSLS KSYILYDLQE ATWYELQMRV CNSAGCAEKQ
ANFATLNYDG STIPPLIKSV VQSEEGLTTN EGLKILVTIS CILVGVLLLF VLLLVVRRRR
REQRLKRLRD AKSLAEMLMS KNTRTSDTLS KQQQTLRMHI DIPRAQLLIE ERDTMETIDD
RSTVLLTDAD FGEAAKQKSL TVTHTVHYQS VSQATGPLVD VSDARPGTNP TTRRNAKAGP
TARNRYASQW TLNRPHPTIS AHTLTTDWRL PTPRATGSVD KESDSYSVSP SQDTDRARSS
MVSTESASST YEELARAYEH AKMEEQLRHA KFTITECFIS DTSSEQLTAG TNEYTDSLTS
STPSESGICR FTASPPKPQD GGRVVNMAVP KAHRPGDLIH LPPYLRMDFL LNRGAPGTSR
DLSLGQACLE PQKSRTLKRP TVLEPTPMEA SSSTSSTREG QQSWQQGAVA TLPQREGAEL
GQAAKMSSSQ ESLLDSRGHL KGNNPYAKSY TLV
