DEX1_CAEEL
ID DEX1_CAEEL Reviewed; 1137 AA.
AC P41950; D7SFI8; Q8TA75; Q95QP5; Q95QP6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dendrite extension defective protein 1 {ECO:0000312|WormBase:D1044.2c};
DE Flags: Precursor;
GN Name=dex-1 {ECO:0000312|WormBase:D1044.2c};
GN ORFNames=D1044.2 {ECO:0000312|WormBase:D1044.2c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19344940; DOI=10.1016/j.cell.2009.01.057;
RA Heiman M.G., Shaham S.;
RT "DEX-1 and DYF-7 establish sensory dendrite length by anchoring dendritic
RT tips during cell migration.";
RL Cell 137:344-355(2009).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=30409788; DOI=10.1534/genetics.118.301557;
RA Flatt K.M., Beshers C., Unal C., Cohen J.D., Sundaram M.V., Schroeder N.E.;
RT "Epidermal Remodeling in Caenorhabditis elegans Dauers Requires the Nidogen
RT Domain Protein DEX-1.";
RL Genetics 211:169-183(2019).
CC -!- FUNCTION: Along with dyf-7, enables neurite growth and maintenance by
CC anchoring amphid dendritic tips during neuron cell body migration in
CC embryonic and larval development (PubMed:19344940). Promotes seam cell
CC remodeling during the dauer phase (PubMed:30409788). Plays a role in
CC positively regulating locomotion during the dauer phase
CC (PubMed:30409788). {ECO:0000269|PubMed:19344940,
CC ECO:0000269|PubMed:30409788}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000269|PubMed:19344940}. Secreted {ECO:0000269|PubMed:30409788,
CC ECO:0000305|PubMed:19344940}. Note=Located at dendritic tips. When
CC transmembrane anchor domain is absent, secreted in vitro.
CC {ECO:0000269|PubMed:19344940, ECO:0000305|PubMed:19344940}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:D1044.2c};
CC IsoId=P41950-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:D1044.2a};
CC IsoId=P41950-2; Sequence=VSP_060616, VSP_060617, VSP_060619;
CC Name=b {ECO:0000312|WormBase:D1044.2b};
CC IsoId=P41950-3; Sequence=VSP_060616, VSP_060618;
CC -!- DEVELOPMENTAL STAGE: Expression is first apparent in bean-stage
CC embryos, peaks in late embryogenesis, reduces in L1 larvae and is
CC negligible in later larval stages and adults (PubMed:19344940). In the
CC embryo, expressed in the excretory cell and, during dendrite formation,
CC in the non-neuronal cells surrounding the sensory neurons, including
CC hypodermal cells (PubMed:19344940). Expressed in pharyngeal cells
CC throughout the larval stages (PubMed:30409788). Expression in the seam
CC cells and glia socket cells of the anterior and posterior deirid
CC neurons begins at the L2 pre-dauer stage and persists throughout the
CC dauer phase (PubMed:30409788). During the dauer phase expressed along
CC the length of the animal above seam cells, alternating between alae
CC under the outer ridges and below the lateral ridge (PubMed:30409788).
CC {ECO:0000269|PubMed:19344940, ECO:0000269|PubMed:30409788}.
CC -!- PTM: May be proteolytically cleaved and secreted.
CC {ECO:0000269|PubMed:19344940}.
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DR EMBL; BX284603; CCD68377.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD68378.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD68379.1; -; Genomic_DNA.
DR PIR; T15884; T15884.
DR RefSeq; NP_498181.3; NM_065780.4. [P41950-2]
DR RefSeq; NP_498182.2; NM_065781.4. [P41950-1]
DR RefSeq; NP_498183.2; NM_065782.3.
DR AlphaFoldDB; P41950; -.
DR STRING; 6239.D1044.2c; -.
DR EPD; P41950; -.
DR PaxDb; P41950; -.
DR PeptideAtlas; P41950; -.
DR EnsemblMetazoa; D1044.2a.1; D1044.2a.1; WBGene00017028. [P41950-2]
DR EnsemblMetazoa; D1044.2b.1; D1044.2b.1; WBGene00017028. [P41950-3]
DR EnsemblMetazoa; D1044.2c.1; D1044.2c.1; WBGene00017028. [P41950-1]
DR GeneID; 175761; -.
DR KEGG; cel:CELE_D1044.2; -.
DR UCSC; D1044.2c; c. elegans. [P41950-1]
DR CTD; 175761; -.
DR WormBase; D1044.2a; CE44889; WBGene00017028; dex-1. [P41950-2]
DR WormBase; D1044.2b; CE44959; WBGene00017028; dex-1. [P41950-3]
DR WormBase; D1044.2c; CE45008; WBGene00017028; dex-1. [P41950-1]
DR eggNOG; KOG4291; Eukaryota.
DR InParanoid; P41950; -.
DR OMA; YDRCGEP; -.
DR OrthoDB; 138133at2759; -.
DR PRO; PR:P41950; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00017028; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0032590; C:dendrite membrane; IDA:WormBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003391; P:amphid sensory organ dendrite retrograde extension; IMP:WormBase.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR003886; NIDO_dom.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF06119; NIDO; 2.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00539; NIDO; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51220; NIDO; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell projection; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Neurogenesis; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..1137
FT /note="Dendrite extension defective protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000007782"
FT TOPO_DOM 43..1005
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1006..1026
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1027..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 163..302
FT /note="NIDO 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 409..450
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 519..659
FT /note="NIDO 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT REGION 738..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 413..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 420..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 437..449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060616"
FT VAR_SEQ 1084..1098
FT /note="QAGKVSLYGSYWNLE -> QKTTSESTLIECVRL (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060617"
FT VAR_SEQ 1085..1129
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060618"
FT VAR_SEQ 1099..1137
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060619"
SQ SEQUENCE 1137 AA; 126144 MW; 5554994531B9183A CRC64;
MLAHTHRINK CLYGQNQMRN RHALLGALPP IFLLLLPLIS CMKFDPERIA ARLRIDEKWD
QLDAFQSIKS RRGRQIQPKE ISIQVTAPLF SSRLFDYGTT AGDEELPQAL DVGKKLDLVH
PISFFGSDYK TIYILSNGAV GFEASSRSYK SGILPSSTRF LAPFWNRNDL RNGGKVYYRE
VTKGRVLERG QSEIRYQYDK NVKVKSALII TWDKMQPLNT AALPEENTNT FQAAIFITAN
GTFANFIYSN IGWTQGAEAG FNAGDATNHF KLPTSGTPNI MYLEEYGNTG IPGEWMFELS
ELRVISCKSG IKGDTCDQEC SNGEWGPDCA YCCHCSEGTC HPISGDCQRG CATCWDGVAC
QTRQEKCATK TQCASNALSF NDYDRCGEPI QRCQCLNGYK GDGYNNCEDV DECKTNSTIC
HKNAICTNTP GRYFCMCKEG FSGDGQNDCS QSFLFQYDTH HQLPRKKNSK MEWNLKKPLK
IFGETTEKLT VTSTGLIAIN EVNRDNGRLE DMQLVGIAPF FGPIDLSRNG AVSVEEVDDV
EVLRRVTRTI GENYNDPTFV AKSALVVTFS NVTDGRQTKG NTFQALLIDG SNSKNEKMTF
VELMYRDLPW ASGAEAGILS SDASSSILLP ASGTEAISQL SKNSNIKQPG TWLYRIDKAQ
LMPCAQPIQV PPYCDRLLST APRLPSKLLE EKKEGLTLPS PGAFLVDQPS ETIVPTLVRG
GGTVTRGRNV LTVTTSPIGN QQRQQTTKAV TRPRPNFSST PHRPIVSLSD EDFELGPDAF
EVTFPPFVTV QPELFRPNQR NGVQKSTQRP LPDFSIRTPL KEEATTSVPR EKTSSAAPAH
SPIEEMSENE ESPFEAGSFD GEAVKFNEEL EAIDKALQTT KKQRPELSVT PQPEDLSGDA
RVIETTEEDE EEAEISTETT TEMSSTTTTT KAHTTTTTMM IPTEAPPSIF VFTTTQKPRA
QSTTQKRIIV QQPSIVVNSQ PPKQRNDNQP TVNVGHAEEQ SPRLAILLPV MIILAWLVIL
VCIGAVVCCK RRNSRESSQL RAMYGAAYGV RPTAYESKRK ESTYEDHLER AARLSGQPAL
SGQQAGKVSL YGSYWNLEPL SNHSPARLST QERQSPPSFV NNGYTNQTTR YTYAGHY