ID G3TN36_LOXAF Unreviewed; 2018 AA.
AC G3TN36;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=DS cell adhesion molecule like 1 {ECO:0000313|Ensembl:ENSLAFP00000016603.2};
GN Name=DSCAML1 {ECO:0000313|Ensembl:ENSLAFP00000016603.2};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000016603.2, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000016603.2, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000016603.2,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000016603.2}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000016603.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000256|ARBA:ARBA00034103}.
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DR STRING; 9785.ENSLAFP00000016603; -.
DR Ensembl; ENSLAFT00000022673.2; ENSLAFP00000016603.2; ENSLAFG00000021385.2.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155354; -.
DR HOGENOM; CLU_001038_0_1_1; -.
DR InParanoid; G3TN36; -.
DR OMA; NFRWERN; -.
DR TreeFam; TF316846; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:Ensembl.
DR CDD; cd00063; FN3; 4.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05734; Ig_DSCAM; 1.
DR CDD; cd05735; Ig_DSCAM; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 15.
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; BASIGIN RELATED; 1.
DR PANTHER; PTHR10075:SF14; DOWN SYNDROME CELL ADHESION MOLECULE 3, ISOFORM E-RELATED; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13927; Ig_3; 4.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 10.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 10.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 10.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1558..1578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..92
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 100..202
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 211..295
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 299..381
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 393..486
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 491..571
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 581..670
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 675..769
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 773..870
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 874..972
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 977..1076
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1081..1177
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1181..1276
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1266..1365
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 1395..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1682..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..2018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1692..1707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1945..1977
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1996..2018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2018 AA; 219833 MW; 91099E60F971370E CRC64;
ARPEDVGTSL YFVNDSLQQV TFSSSVGVVV PCPATGSPSV ALRWYLATGD DIYDVPHIRH
VHANGTLQLY PFSPSAFNSF IHDNDYFCTA ENAAGKIRSP NIRVKAVFRE PYTVRVEDQR
SVRGNVAVFK CLIPSSVQEY VSVVSWEKDT VSIIPENRFF ITYHGGLYIS DVQKEDALST
YRCITKHKYS GETRQSNGAR LSVTDPAESI PIILDGFHSQ EVWAGHTVEL PCTASGYPIP
AIRWLKDGRP LPADSRWTKR ITGLTISDLR TEDSGIYICE VTNTFGSAEA TGVLTVIDPL
HVTLTPKKLK TGIGSTVILS CALTGSPEFT IRWYRNTELV LPNEAISIRG LSNETLLITS
AQKSHSGAYQ CFATRKAQTA QDFAIIVLED GTPRIVSSFS EKVVNPGEQF SLMCAAKGAP
PPTVTWALDD EPILRDGSHR TNQYTMSDGT TISHMNITGP QIRDGGVYRC TARNSVGSAE
YQARINVRGP PSIRAMRNIT AVAGRDTLIN CRVIGYPYYS IKWYKDALLL PDNHRQVVFE
NGTLKLTDVQ KGMDEGEYLC SVLIQPQLSI SQSVHVAVKV PPLIQPFEFP PASIGQLLYI
PCVVSSGDMP IRITWRKDGQ VIISGSGVTI ESKEFMSSLQ ISSVSLKHNG NYTCIASNAA
ATVSRERQLI VRVPPRFVVQ PNNQDGIYGK AGVLNCSVDG YPPPKVMWKH AKGSGNPQQY
HPVPLTGRIQ ILPNSSLLIR HVLEEDIGYY LCQASNGVGT DISKSMFLTV KIPAMITSHP
NTTIAIKGHA KELNCTARGE RPIIIRWEKG DTVIDPDRVM RYAIATKDNG DEVVSTLKLK
PADRGDSVFF SCHAINSYGE DRGLIQLTVQ GIHCPTVPRL LPQRPRCPQL TPPPVAGTRP
APCIITGFDI EYKNKSDSWD FKQSTRNISP TINQANIVDL HPASVYSIRM YSFNKIGRSE
PSKELTISTE EAAPDGPPMD VTLQPVTSQS IQVTWKAPKK ELQNGVIRGY QIGYRENSPG
SNGQYSIVEM KATGDSEVYT LDNLKKFAQY GVVVQAFNRA GTGPSSSEIN ATTLEDVPSQ
PPENVRALSI TSDVAVISWS EPPRSTLNGV LKGYRVIFWS LYVDGEWGEM QNITTTRERV
ELHGMEKFTN YSVQVLAYTQ AGDGVRSSVL YIQTKEDVPG PPAGIKAVPS SASSVVVSWL
PPTKPNGVIR KYTIFCSSPG SGQPAPSEYE TSPEQLFYRI AHLNRGQQYM LWVAAVTSAG
RGNSSEKVTI EPVGKAPAKI ISFGGTVTTP WMKDVRLPCN SVGDPAPAVK WTKDSEDSAI
PVSMDGHRLI HTNGTLLLRA VKAEDSGYYT CTATNTGGFD TIIINLLVQV PPDQPRLTVS
KTSASSITLT WIPGDNGGSS IRGEEGSGGG GEDGKELWVQ GKGKCFTHSH HLPLQHPGND
LGKDSDHKEA SQGPWKAPWH RRLGFSPTTH LWPLLCCVNL ISLFSSLGLS LQICLRANSS
KVFLTELREA TWYELRMRAC NSAGCGNETA QFATLDYDGS TIPPIKSAQG EGDDVKKLFT
IGCPVILATL GVALLFIVRK KRKEKRLKRL RDAKSLAEML ISKNNRSFDT PVKGPPQGPR
LHIDIPRVQL LIEDKEGIKQ LGDDKATIPV TDAEFSQAVN PQSFCTGVSL HHPALIQSTG
PLIDMSDIRP GTNPVSRKNV KSAHSTRNRY SSQWTLTKCQ ASTPARTLTS DWRTVGSQHG
VTVTESDSYS ASLSQDTDKG RNSMVSTESA SSTYEELARA YEHAKLEEQL QHAKFEITEC
FISDSSSDQM TTGTNENADS MTSMSTPSEP GICRFTASPP KPQDADRGKN VAVPIPHRAN
KSDYCNLPLY AKSEAFFRKS EGREPCPVVP PREASIRNLA RTYHPQARHL TLDPASKPLG
LPHPGAPAAT STATLPQRTL AMPAPPAGTA PPAPGPTPAE PPTAPSAAPP APSTEPPRAG
GPHTKMGGSR DSLLEMSSGV GRSQKQGPGA YSKSYTLV
//
