DSCAM_CHICK
ID DSCAM_CHICK Reviewed; 2034 AA.
AC F1NY98;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 3.
DT 03-AUG-2022, entry version 72.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=18216854; DOI=10.1038/nature06469;
RA Yamagata M., Sanes J.R.;
RT "Dscam and Sidekick proteins direct lamina-specific synaptic connections in
RT vertebrate retina.";
RL Nature 451:465-469(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 (By similarity). Adhesion molecule that promotes
CC lamina-specific synaptic connections in the retina: expressed in
CC specific subsets of interneurons and retinal ganglion cells (RGCs) and
CC promotes synaptic connectivity via homophilic interactions
CC (PubMed:18216854). {ECO:0000250|UniProtKB:O60469,
CC ECO:0000250|UniProtKB:Q8VHZ8, ECO:0000269|PubMed:18216854}.
CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC adhesion. {ECO:0000269|PubMed:18216854}.
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}. Synapse
CC {ECO:0000269|PubMed:18216854}. Note=Localized in the soma, cell
CC membrane, axon and growth cone of dissociated commissural axons.
CC {ECO:0000250|UniProtKB:Q9ERC8}.
CC -!- TISSUE SPECIFICITY: SDK1, SDK2, DSCAM and DSCAML1 are expressed in non-
CC overlapping subsets of interneurons and retinal ganglion cells (RGCs)
CC that form synapses in distinct inner plexiform layer (IPL) sublaminae
CC (PubMed:18216854). {ECO:0000269|PubMed:18216854}.
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DR EMBL; AADN03000073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN03000437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN03000849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1NY98; -.
DR SMR; F1NY98; -.
DR STRING; 9031.ENSGALP00000025946; -.
DR PaxDb; F1NY98; -.
DR PRIDE; F1NY98; -.
DR Ensembl; ENSGALT00000025993; ENSGALP00000025946; ENSGALG00000016138.
DR VEuPathDB; HostDB:geneid_418525; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000154678; -.
DR HOGENOM; CLU_001038_0_1_1; -.
DR InParanoid; F1NY98; -.
DR OMA; WTTAHRT; -.
DR OrthoDB; 14047at2759; -.
DR TreeFam; TF316846; -.
DR PRO; PR:F1NY98; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000016138; Expressed in brain and 2 other tissues.
DR ExpressionAtlas; F1NY98; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:1990890; F:netrin receptor binding; IEA:Ensembl.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IDA:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0070593; P:dendrite self-avoidance; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IEA:Ensembl.
DR GO; GO:0060060; P:post-embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IDA:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IDA: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; 10.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..2034
FT /note="Cell adhesion molecule DSCAM"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434543"
FT TOPO_DOM 19..1621
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1622..1642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1643..2034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 39..145
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 151..242
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 251..321
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 339..427
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 433..526
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 530..618
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 622..711
FT /note="Ig-like C2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 716..809
FT /note="Ig-like C2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 813..909
FT /note="Ig-like C2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 911..1008
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1013..1112
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1117..1213
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1217..1311
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1311..1403
FT /note="Ig-like C2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1405..1499
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1500..1601
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1744..1833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2001..2034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1808..1833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2004..2018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 950
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 72..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 171..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 272..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 361..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 454..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 551..601
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 643..695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 737..792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 835..891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1333..1385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 2034 AA; 225021 MW; 3C0747DA3E5CF27C CRC64;
MWMLAVALLH SISHGILTEN FLSHHAFPSL LLSLHFSHPS VFSEDLHASL YFVNASLQEV
VFASTTGTLV PCPAAGIPPV TLRWYLATGE EIYDVPGIRH VHPNGTLQIF PFPPSSFNNL
IHDNTYYCTA ENPSGKIRSQ DVHIKAVLRE PYTVRVEDQK AMRGNVAVFK CIIPSSVEAY
ITVVSWEKDT VSLVSGPRFL ITSTGALYIL DVQNEDGLYN YRCITRHRYT GETRQSNSAR
LFVSDPANSA PSILDGFDHR KAMAGQRVEL PCKASGHPTP KYRWLKDNIP WEPDSRFRQT
VTGLLIENTR PSDSGNYVCE VWNNYGTAEM IGRLYVKQPL KATISPRKVK SSVGSQVSLS
CSVTGTEDQE LSWYRNGEII NPGNNVRITG INRENLIMDG MAKSDGGAYQ CFVRKDKMSA
QDYVQVILED GTPKIISAFS EKVVSPGEPV SLMCNVKGTP LPTITWTLDE DPIVKDGSHR
ISQIITSEGN VVSYLNISNT QVRDGGVYRC TANNSAGVVL YQARINVRGP ASIRPMKNIT
AIAGRDTYIH CRVIGYPYYS IKWYKNSNLL PFNHRQVAFE NNGTLKLSDV QKEVDEGEYT
CNVLVQPQLS TSQSVHVTVK VPPFIQPFEF PRFSIGQRVF IPCVVVSGDL PITITWQKDG
RPIPASLGVT IDNIDFTSSL RISNLSLMHN GNYTCIARND AAAVEHQSQL IVRVPPRFVV
QPSDQDGIYG KAVILNCSAE GYPVPTIVWK YSKGAGVPQF QPIALNGRIQ LLTNGSLLIK
HVLEEDSGYY LCKVSNDVGA DVSKSMYLTV KIPAMITSYP NTTLATQGQK KEMSCTAHGE
KPIIVRWEKE DRIINPEMSR YLVSTKEVGD EVISTLQILP TVREDSGFFS CHAINSYGED
RGIIQLTVQE PPDPPEIEIR EVRARSIALR WTMGFDGNSP ITGYDIECKN KSDSWDSVQR
TKDVSPQLNQ ATIIDLHPSS TYNIRMYAKN RIGKSEASNE LTITTDEAAP DGPPQDVQLE
PISSQSIRVT WKAPKKHLQN GIIRGYQIGY REYSAGGNFQ FNIISIDTTG DSEVYTLNNL
KKFTQYGMVV QACNRAGIGP SSQEIITTTL EDVPSCPPGN VQATATSPET ISISWSTLAK
ETLNGILQGF RVIYWANLLD GELGEIRNVT TTQPSLELDG LEKYTNYSIQ VLAFTRAGDG
VRSEQIFTRT KEDVPGPPAG VKAAASSAST VFVSWLPPLK LNGIIRKYTV FCSHPYPTVI
SEFEASPDSF SYRIPNLSRN RQYSVWVVAV TAAGRGNSSE IITVEPLAKA PARILTFSGT
VTTPWMKDIV LPCKAVGDPA PTVKWMKDSN GTPSLVMIDG RRSIFSNGSF VIRTVKAEDS
GYYSCVASNN WGSDEIILNL QVQVPPDQPR LTVSKTTSSS ITLSWIPGDN GGSSIRGYIL
QYSEDNSEQW GSFPISPSER SYRLETLKCG TWYKFTLTAQ NGVGPGRISE IIEAKTLGKE
PQFSKEQELF ASINTTRVRL NLIGWNDGGC PITSFTLEYR PFGTTVWTTA QRTSLSKSYI
LYDLQEATWY ELQMRVCNSA GCAEKQAKFA TLNYDGSTIP PLIKSVVQSE EGLATNEGLK
MLVTISCILV GVLLLFVMLL IVRRRRREQR LKRLRDAKSL AEMLMSKNTR TSDTLNKQQQ
TLRMHIDIPR AQLLIEERDT METIDDRSTV LLTDADFGET SKQKSLTVTH TVHYQSVSQA
TGPLVDVSDA RPGTNPTTRR SAKTGPTARN RYASQWTLNR PHPTISAHTL TTDWRLPTPR
PAGSVDKESD SYSVSPSQDT DRARSSMVST ESASSTYEEL ARAYEHAKME EQLRHAKFTI
TECFISDTSS EQLTAGTNDY TDSLTSSTPS ESGICRFTAS PPKPQDGGRV MNMAVPKAHR
PGDLVHLPPY LRMDFLLNRG AQGASRDLGL GQACLEPQKS RTLKRPTVLE PIPMEASSTR
EAQSWQPGAV ATLPQREGAE LGQAAKMSSS QESLLDSRGH LKGNNPYAKS YTLV
