DSCL1_CHICK
ID DSCL1_CHICK Reviewed; 2042 AA.
AC E1C8P7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cell adhesion molecule DSCAML1 {ECO:0000305};
DE AltName: Full=Down syndrome cell adhesion molecule-like protein 1 homolog;
DE Flags: Precursor;
GN Name=DSCAML1;
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 (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 (PubMed:18216854). {ECO:0000250|UniProtKB:Q4VA61,
CC 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:Q4VA61};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q4VA61}.
CC Synapse {ECO:0000269|PubMed:18216854}.
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; AADN03008271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN03008296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1C8P7; -.
DR SMR; E1C8P7; -.
DR STRING; 9031.ENSGALP00000011821; -.
DR PRIDE; E1C8P7; -.
DR Ensembl; ENSGALT00000011835; ENSGALP00000011821; ENSGALG00000007314.
DR VEuPathDB; HostDB:geneid_428249; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155354; -.
DR HOGENOM; CLU_001038_0_1_1; -.
DR OMA; GHTMELP; -.
DR PRO; PR:E1C8P7; -.
DR Proteomes; UP000000539; Chromosome 24.
DR Bgee; ENSGALG00000007314; Expressed in brain and 2 other tissues.
DR ExpressionAtlas; E1C8P7; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IDA:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
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; IPR033029; DSCAML1.
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; PTHR13817:SF54; PTHR13817:SF54; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 4.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 10.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 10.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 9.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..2042
FT /note="Cell adhesion molecule DSCAML1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434544"
FT TOPO_DOM 18..1592
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1593..1613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1614..2042
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 37..107
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 114..216
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 227..311
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 315..403
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 409..502
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 507..587
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 597..686
FT /note="Ig-like C2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 691..785
FT /note="Ig-like C2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 789..886
FT /note="Ig-like C2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 888..985
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 990..1089
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1094..1190
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1194..1289
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1279..1368
FT /note="Ig-like C2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1384..1478
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1479..1579
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1716..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1781..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1841..1865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..2042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1980..1994
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1995..2042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 927
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1163
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 1346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 46..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 145..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 337..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 430..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 527..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 618..670
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 712..768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 811..868
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1312..1364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 2042 AA; 223884 MW; 580169E8CE770408 CRC64;
MWLVTFFLLY SLRKAHTEDV GTSLYFVNDS IQQVTFSSTV GVVIPCPAAG SPSAVLRWYL
ATGDDIYDVP HIRHVHANGT LQLYPFSPSA FNSFIHDNDY FCTAENSAGK IRSPNIRVKA
VFREPYTVRV EDQRSMRGNV AVFKCLIPSS VQEYVSVVSW EKDTVSIIPE NRFFITSYGG
LYISDVQKED ALSTYRCITK HKYSGETRQS NGARLSVSDA DPAESIPTML DSFQSREVRA
GRLVELPCIA SGYPNPAIRW LKDGRPLPAD GRWAKRITGL SIADLRVEDS GTYICEVTNT
FGSAEVTGTL TVIDPLRVTL TPKKLKTGIG STVILSCALS GSPEYVIRWY RNTDLVVVDD
FISIRGISNE TLLITAAQKS HSGAYQCFAT RKSQTAQDFS IITLEDGTPR IVSSFSEKVV
NPGEQFSLMC AAKGAPPPTV TWALDDEPIP RDNGHRTNQY TMSDGTTVSH MNVTSPQIKD
GGVYRCTARN SVGSAEYQAR INVRGPPSIR AMKNITAVAG RDTFINCRVI GYPYYSIKWY
KDSLLLPDNH RQVVFENGTL KLMDVQKGMD EGEYLCSVLI QPQLSISQSV HVTVKVPPLI
QPFEFPPASI GQLLYIPCVV SSGDMPIHIT WRKDGHVILS GSGVTIESKE FMSSLQISSV
SLKHNGNYTC IASNAAATVS RERQLIVRVP PRFVVQPNNQ DGIYGKAGVL NCSVDGYPPP
KVMWKHAKGS GNPQQYHPIP LTGRIQILPN SSLLIRHVLE EDIGYYLCQA SNGVGTDISK
SMFLTVKIPA MITSHPNTTI AIKGQSKELN CTARGERPII IRWEKGDTVI DPDRNMRYAI
ATKDNGDEVI STLKLKPADR GDSVFFSCHA INSYGEDRGL IQLTVQEPPD PPELEIREVK
ARSMNLRWTQ RFDGNSIITG FDIEYKNKSD SWDFKQSTRN ISPTINQANI VDLHPASVYS
IRMYSFNKIG RSEPSKELTI STEEAAPDGP PMDVTLQPMT SQSIQVTWKA PKKELQNGVI
RGYQIGYREN SPGSNGQYSI VEMKATGDSE VYTLDNLKKF AQYGVVVQAF NRAGTGPSSS
EINATTLEDV PSQPPENVRA ISITSDVAVI SWSEPPRSTL NGVLKGYRVI FWSLYMDGEW
GEMQNITTTR ERVELRGMEK FTNYSVQVLA YTQAGDGVRS SVLYIQTKED IPGPPAGIKA
VPSSASSVVV SWLPPAKPNG IIRKYTIFCS SPGSGQPAPS EYETSPDQLF YRIAHLNRGQ
QYMLWVAAVT SAGRGNISEK VTIEPAGKAP AKIISFGGTV TTPWMKDVRL PCNSVGEPVP
AIKWTKDSED SAIPVTVDGH RLIQANGTLV LRSVKAEDSG YYTCTATNTW GFDTIIINLL
VQVPPDQPRL TVSKTSASSI TLAWIPGDNG GSSIRGFVLQ YSVDNSEEWK DVFISSSERS
FKLESLKCGT WYKVKLAAKN SVGAGRISEI IEAKTHGREP SFSKDQHLFT HINSTHARLN
LQGWSSGGCP ITAIVLEYRP KGNWGWQSLR TNSSGEVFLT ELREATWYEL RMKACNSAGC
GNESTQFATL DYDGSTIPPI KSAQGEGDDV KKLFTIACPI ILATLGVALL FIIRKKRKEK
RLKRLRDAKS LAEMLISKNN RSFDTPVKGP PQGPRLHIDI PRVQLLIEDK EGIKQLGDDK
ATIPVTDTEF SQAVNPQSFC TGVSLHHPAL IQNTGPLIDM SDIRPGTNPV SRKSVKSAHS
TRNRYSSQWT LTKCQASTPA RTLTSDWRTV GSQHGITVTE SDSYSASLSQ DTDKGRNSMV
STESASSTYE ELARAYEHAK LEEQLQHAKF EITECFISDS SSDQMTTGTT DNADSMTSMS
TPSEPGICRF TASPPKPQDS ERGKSVAVPI PHRASKSDYC NLPLYVKSDA FFRKPDSHEP
CPVVPPREAS IRSLARGYHP PARHLTLDPA AKPPGLPPPS SSSSSTTLPQ RTLPMPTAAS
TAPAPAPAPA APAEPPANTT TTTTTHSKVG GSRDSLLEMS TSGAGRAQKQ GAGAYSKSYT
LV
