DSCAM_HUMAN » Down syndrome cell adhesion molecule

DSCAM_HUMAN » Down syndrome cell adhesion molecule
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
DSCAM_HUMAN » Down syndrome cell adhesion molecule » CHD2;
Hydrophobic Thickness 33.2 ± 0.6 Å
Tilt Angle 0 ± 1°
ΔGtransfer -47.0 kcal/mol
ΔGfold -25.7 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 1595-1617 (1589-1626)
Pathways

Cell-Cell communication (Reactome)

PDB none
OPM none
Complexes none
Interactions

ESR1, Complex: ESR1:DSCAM, PubMed

Domains

AA: 225-310, PDBID: 3S97, Subunit D, Seq Identity:35%, Immunoglobulin I-set domain

AA: 314-401, PDBID: 1RHF, Subunit B, Seq Identity:32%, Immunoglobulin I-set domain

AA: 406-488, PDBID: 4WVR, Subunit D, Seq Identity:31%, Immunoglobulin domain

AA: 504-595, PDBID: 2V5R, Subunit B, Seq Identity:28%, Immunoglobulin I-set domain

AA: 596-673, PDBID: 3DMK, Subunit C, Seq Identity:42%, Immunoglobulin domain

AA: 689-770, PDBID: 4X8X, Subunit B, Seq Identity:34%, Immunoglobulin domain

AA: 788-882, PDBID: 1CS6, Subunit A, Seq Identity:29%, Immunoglobulin I-set domain

AA: 886-972, PDBID: 1UEY, Subunit A, Seq Identity:32%, Fibronectin type III domain

AA: 986-1076, PDBID: 1VA9, Subunit A, Seq Identity:73%, Fibronectin type III domain

AA: 1090-1177, PDBID: 2ED8, Subunit A, Seq Identity:33%, Fibronectin type III domain

AA: 1190-1273, PDBID: 1VA9, Subunit A, Seq Identity:35%, Fibronectin type III domain

AA: 1287-1376, PDBID: 4CBP, Subunit A, Seq Identity:34%, Immunoglobulin I-set domain

AA: 1379-1463, PDBID: 1X5I, Subunit A, Seq Identity:33%, Fibronectin type III domain

UniProt annotation for DSCAM_HUMAN » Down syndrome cell adhesion molecule
FUNCTION: 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. Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC. In spinal chord 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.

SUBUNIT: Interacts with DCC; the interaction is abolished in response to NTN1 (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts (via extracellular domain) with NTN1. Interacts (via cytoplasmic domain) with PAK1; the interaction is direct and enhanced in presence of RAC1. Interacts with RAC1; the interaction requires PAK1.

TISSUE SPECIFICITY: Primarily expressed in brain.

DOMAIN: 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).

UniProt features for DSCAM_HUMAN » Down syndrome cell adhesion molecule
SIGNAL 1 17 Potential.
CHAIN 18 2012 Down syndrome cell adhesion molecule.
DOMAIN 39 129 Ig-like C2-type 1.
DOMAIN 125 216 Ig-like C2-type 2.
DOMAIN 225 305 Ig-like C2-type 3.
DOMAIN 313 401 Ig-like C2-type 4.
DOMAIN 407 500 Ig-like C2-type 5.
DOMAIN 504 592 Ig-like C2-type 6.
DOMAIN 596 685 Ig-like C2-type 7.
DOMAIN 690 783 Ig-like C2-type 8.
DOMAIN 787 883 Ig-like C2-type 9.
DOMAIN 885 978 Fibronectin type-III 1.
DOMAIN 984 1082 Fibronectin type-III 2.
DOMAIN 1088 1183 Fibronectin type-III 3.
DOMAIN 1189 1279 Fibronectin type-III 4.
DOMAIN 1285 1377 Ig-like C2-type 10.
DOMAIN 1376 1470 Fibronectin type-III 5.
DOMAIN 1476 1566 Fibronectin type-III 6.
DISULFID 46 102 By similarity.
DISULFID 145 197 By similarity.
DISULFID 246 293 By similarity.
DISULFID 335 385 By similarity.
DISULFID 428 484 By similarity.
DISULFID 525 575 By similarity.
DISULFID 617 669 By similarity.
DISULFID 711 766 By similarity.
DISULFID 809 865 By similarity.
DISULFID 1307 1359 By similarity.
Amino Acid Sequence for DSCAM_HUMAN » Down syndrome cell adhesion molecule
MWILALSLFQ SFANVFSEDL HSSLYFVNAS LQEVVFASTT GTLVPCPAAG IPPVTLRWYL ATGEEIYDVP GIRHVHPNGT LQIFPFPPSS FSTLIHDNTY YCTAENPSGK IRSQDVHIKA VLREPYTVRV EDQKTMRGNV AVFKCIIPSS VEAYITVVSW EKDTVSLVSG SRFLITSTGA LYIKDVQNED GLYNYRCITR HRYTGETRQS NSARLFVSDP ANSAPSILDG FDHRKAMAGQ RVELPCKALG HPEPDYRWLK DNMPLELSGR FQKTVTGLLI ENIRPSDSGS YVCEVSNRYG TAKVIGRLYV KQPLKATISP RKVKSSVGSQ VSLSCSVTGT EDQELSWYRN GEILNPGKNV RITGINHENL IMDHMVKSDG GAYQCFVRKD KLSAQDYVQV VLEDGTPKII SAFSEKVVSP AEPVSLMCNV KGTPLPTITW TLDDDPILKG GSHRISQMIT SEGNVVSYLN ISSSQVRDGG VYRCTANNSA GVVLYQARIN VRGPASIRPM KNITAIAGRD TYIHCRVIGY PYYSIKWYKN SNLLPFNHRQ VAFENNGTLK LSDVQKEVDE GEYTCNVLVQ PQLSTSQSVH VTVKVPPFIQ PFEFPRFSIG QRVFIPCVVV SGDLPITITW QKDGRPIPGS LGVTIDNIDF TSSLRISNLS LMHNGNYTCI ARNEAAAVEH QSQLIVRVPP KFVVQPRDQD GIYGKAVILN CSAEGYPVPT IVWKFSKGAG VPQFQPIALN GRIQVLSNGS LLIKHVVEED SGYYLCKVSN DVGADVSKSM YLTVKIPAMI TSYPNTTLAT QGQKKEMSCT AHGEKPIIVR WEKEDRIINP EMARYLVSTK EVGEEVISTL QILPTVREDS GFFSCHAINS YGEDRGIIQL TVQEPPDPPE IEIKDVKART ITLRWTMGFD GNSPITGYDI ECKNKSDSWD SAQRTKDVSP QLNSATIIDI HPSSTYSIRM YAKNRIGKSE PSNELTITAD EAAPDGPPQE VHLEPISSQS IRVTWKAPKK HLQNGIIRGY QIGYREYSTG GNFQFNIISV DTSGDSEVYT LDNLNKFTQY GLVVQACNRA GTGPSSQEII TTTLEDVPSY PPENVQAIAT SPESISISWS TLSKEALNGI LQGFRVIYWA NLMDGELGEI KNITTTQPSL ELDGLEKYTN YSIQVLAFTR AGDGVRSEQI FTRTKEDVPG PPAGVKAAAA SASMVFVSWL PPLKLNGIIR KYTVFCSHPY PTVISEFEAS PDSFSYRIPN LSRNRQYSVW VVAVTSAGRG NSSEIITVEP LAKAPARILT FSGTVTTPWM KDIVLPCKAV GDPSPAVKWM KDSNGTPSLV TIDGRRSIFS NGSFIIRTVK AEDSGYYSCI ANNNWGSDEI ILNLQVQVPP DQPRLTVSKT TSSSITLSWL PGDNGGSSIR GYILQYSEDN SEQWGSFPIS PSERSYRLEN LKCGTWYKFT LTAQNGVGPG RISEIIEAKT LGKEPQFSKE QELFASINTT RVRLNLIGWN DGGCPITSFT LEYRPFGTTV WTTAQRTSLS KSYILYDLQE ATWYELQMRV CNSAGCAEKQ ANFATLNYDG STIPPLIKSV VQNEEGLTTN EGLKMLVTIS CILVGVLLLF VLLLVVRRRR REQRLKRLRD AKSLAEMLMS KNTRTSDTLS KQQQTLRMHI DIPRAQLLIE ERDTMETIDD RSTVLLTDAD FGEAAKQKSL TVTHTVHYQS VSQATGPLVD VSDARPGTNP TTRRNAKAGP TARNRYASQW TLNRPHPTIS AHTLTTDWRL PTPRAAGSVD KESDSYSVSP SQDTDRARSS MVSTESASST YEELARAYEH AKMEEQLRHA KFTITECFIS DTSSEQLTAG TNEYTDSLTS STPSESGICR FTASPPKPQD GGRVMNMAVP KAHRPGDLIH LPPYLRMDFL LNRGGPGTSR DLSLGQACLE PQKSRTLKRP TVLEPIPMEA ASSASSTREG QSWQPGAVAT LPQREGAELG QAAKMSSSQE SLLDSRGHLK GNNPYAKSYT LV