DSCL1_HUMAN » Down syndrome cell adhesion molecule-like protein 1

DSCL1_HUMAN » Down syndrome cell adhesion molecule-like protein 1
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
DSCL1_HUMAN » Down syndrome cell adhesion molecule-like protein 1 » Down syndrome cell adhesion molecule 2;
Hydrophobic Thickness 39.6 ± 4.4 Å
Tilt Angle 5 ± 7°
ΔGtransfer -29.8 kcal/mol
ΔGfold -18.8 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 1588-1615 (1587-1624)
Pathways

Cell-Cell communication (Reactome)

PDB 1va9 (979-1087)
OPM none
Complexes none
Interactions none
Domains

AA: 226-311, PDBID: 2EDJ, Subunit A, Seq Identity:42%, Immunoglobulin I-set domain

AA: 315-402, PDBID: 3LAF, Subunit A, Seq Identity:31%, Immunoglobulin I-set domain

AA: 407-489, PDBID: 2V9Q, Subunit A, Seq Identity:30%, Immunoglobulin domain

AA: 505-593, PDBID: 2EO1, Subunit A, Seq Identity:35%, Immunoglobulin I-set domain

AA: 596-673, PDBID: 3DMK, Subunit C, Seq Identity:45%, Immunoglobulin domain

AA: 689-771, PDBID: 2EO9, Subunit A, Seq Identity:29%, Immunoglobulin domain

AA: 789-884, PDBID: 4X9G, Subunit A, Seq Identity:28%, Immunoglobulin I-set domain

AA: 888-974, PDBID: 1UEY, Subunit A, Seq Identity:32%, Fibronectin type III domain

AA: 988-1078, PDBID: 1VA9, Subunit A, Seq Identity:100%, Fibronectin type III domain

AA: 1092-1179, PDBID: 2EDX, Subunit A, Seq Identity:33%, Fibronectin type III domain

AA: 1192-1277, PDBID: 1VA9, Subunit A, Seq Identity:32%, Fibronectin type III domain

AA: 1291-1367, PDBID: 4X9H, Subunit B, Seq Identity:34%, Immunoglobulin domain

AA: 1383-1467, PDBID: 1X4Z, Subunit A, Seq Identity:30%, Fibronectin type III domain

UniProt annotation for DSCL1_HUMAN » Down syndrome cell adhesion molecule-like protein 1
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. Promotes both isoneuronal self-avoidance for creating an orderly neurite arborization in retinal rod bipolar cells and heteroneuronal self-avoidance to maintain mosaic spacing between AII amacrine cells (By similarity).

TISSUE SPECIFICITY: Detected in heart, liver, pancreas, skeletal muscle, kidney and in brain, in particular in the amygdala, caudate nucleus, corpus callosum, hippocampus, substantia nigra, thalamus and subthalamus.

UniProt features for DSCL1_HUMAN » Down syndrome cell adhesion molecule-like protein 1
SIGNAL 1 18 Potential.
CHAIN 19 2053 Down syndrome cell adhesion molecule-like protein 1.
DOMAIN 19 119 Ig-like C2-type 1.
DOMAIN 115 217 Ig-like C2-type 2.
DOMAIN 226 306 Ig-like C2-type 3.
DOMAIN 314 402 Ig-like C2-type 4.
DOMAIN 408 501 Ig-like C2-type 5.
DOMAIN 506 586 Ig-like C2-type 6.
DOMAIN 596 685 Ig-like C2-type 7.
DOMAIN 690 784 Ig-like C2-type 8.
DOMAIN 788 885 Ig-like C2-type 9.
DOMAIN 887 980 Fibronectin type-III 1.
DOMAIN 986 1085 Fibronectin type-III 2.
DOMAIN 1090 1186 Fibronectin type-III 3.
DOMAIN 1191 1283 Fibronectin type-III 4.
DOMAIN 1278 1377 Ig-like C2-type 10.
DOMAIN 1380 1474 Fibronectin type-III 5.
DOMAIN 1479 1569 Fibronectin type-III 6.
DISULFID 47 103 By similarity.
DISULFID 146 198 By similarity.
DISULFID 247 294 By similarity.
DISULFID 336 386 By similarity.
DISULFID 429 485 By similarity.
DISULFID 526 575 By similarity.
DISULFID 617 669 By similarity.
DISULFID 711 767 By similarity.
DISULFID 810 867 By similarity.
DISULFID 1311 1363 By similarity.
Amino Acid Sequence for DSCL1_HUMAN » Down syndrome cell adhesion molecule-like protein 1
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