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Database: UniProt
Entry: P41950
LinkDB: P41950
Original site: P41950 
ID   DEX1_CAEEL              Reviewed;        1090 AA.
AC   P41950; D7SFI8; Q8TA75; Q95QP5; Q95QP6;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   16-JAN-2019, entry version 130.
DE   RecName: Full=Dendrite extension defective protein 1 {ECO:0000312|WormBase:D1044.2b};
DE   Flags: Precursor;
GN   Name=dex-1 {ECO:0000312|WormBase:D1044.2b};
GN   ORFNames=D1044.2 {ECO:0000312|WormBase:D1044.2b};
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], AND ALTERNATIVE
RP   SPLICING.
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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   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
RT   dendritic tips during cell migration.";
RL   Cell 137:344-355(2009).
CC   -!- FUNCTION: Along with dyf-7, enables neurite growth and maintenance
CC       by anchoring amphid dendritic tips during neuron cell body
CC       migration in embryonic and larval development.
CC       {ECO:0000269|PubMed:19344940}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:19344940}. Secreted
CC       {ECO:0000305|PubMed:19344940}. Note=Located at dendritic tips.
CC       When 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=b {ECO:0000312|WormBase:D1044.2b};
CC         IsoId=P41950-1; Sequence=Displayed;
CC       Name=a {ECO:0000312|WormBase:D1044.2a};
CC         IsoId=P41950-2; Sequence=VSP_032757, VSP_011899;
CC       Name=c {ECO:0000312|WormBase:D1044.2c};
CC         IsoId=P41950-3; Sequence=VSP_011898, VSP_011899;
CC         Note=No experimental confirmation available. {ECO:0000305};
CC   -!- TISSUE SPECIFICITY: In the embryo, expressed in the excretory cell
CC       and, during dendrite formation, in the non-neuronal cells
CC       surrounding the sensory neurons, including hypodermal cells.
CC       {ECO:0000269|PubMed:19344940}.
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.
CC       {ECO:0000269|PubMed:19344940}.
CC   -!- PTM: May be proteolytically cleaved and secreted.
CC       {ECO:0000269|PubMed:19344940}.
DR   EMBL; FO081000; CCD68377.1; -; Genomic_DNA.
DR   EMBL; FO081000; CCD68378.1; -; Genomic_DNA.
DR   EMBL; FO081000; CCD68379.1; -; Genomic_DNA.
DR   PIR; T15884; T15884.
DR   RefSeq; NP_498181.3; NM_065780.4.
DR   RefSeq; NP_498182.2; NM_065781.4.
DR   RefSeq; NP_498183.2; NM_065782.3.
DR   UniGene; Cel.6121; -.
DR   ProteinModelPortal; P41950; -.
DR   SMR; P41950; -.
DR   STRING; 6239.D1044.2c; -.
DR   EPD; P41950; -.
DR   PaxDb; P41950; -.
DR   PeptideAtlas; P41950; -.
DR   PRIDE; P41950; -.
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.
DR   WormBase; D1044.2b; CE44959; WBGene00017028; dex-1.
DR   WormBase; D1044.2c; CE45008; WBGene00017028; dex-1.
DR   eggNOG; ENOG410IUH2; Eukaryota.
DR   eggNOG; ENOG4112C11; LUCA.
DR   HOGENOM; HOG000155619; -.
DR   InParanoid; P41950; -.
DR   OrthoDB; 138133at2759; -.
DR   PRO; PR:P41950; -.
DR   Proteomes; UP000001940; Chromosome III.
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; IPR013032; EGF-like_CS.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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   SUPFAM; SSF57184; SSF57184; 1.
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; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Neurogenesis;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     41       {ECO:0000255}.
FT   CHAIN        42   1090       Dendrite extension defective protein 1.
FT                                {ECO:0000305}.
FT                                /FTId=PRO_0000007782.
FT   TOPO_DOM     42    958       Extracellular. {ECO:0000255}.
FT   TRANSMEM    959    979       Helical. {ECO:0000255}.
FT   TOPO_DOM    980   1090       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      163    302       NIDO 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00570}.
FT   DOMAIN      409    450       EGF-like; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      452    612       NIDO 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00570}.
FT   COMPBIAS    870    917       Thr-rich.
FT   CARBOHYD    240    240       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    416    416       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    709    709       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    413    426       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    420    435       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    437    449       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ       1    550       Missing (in isoform c). {ECO:0000305}.
FT                                /FTId=VSP_011898.
FT   VAR_SEQ       1     17       Missing (in isoform a). {ECO:0000305}.
FT                                /FTId=VSP_032757.
FT   VAR_SEQ    1038   1090       AGKVSLYGSYWNLEPLSNHSPARLSTQERQSPPSFVNNGYT
FT                                NQTTRYTYAGHY -> KTTSESTLIECVRL (in
FT                                isoform a and isoform c). {ECO:0000305}.
FT                                /FTId=VSP_011899.
SQ   SEQUENCE   1090 AA;  120934 MW;  F09F2AFF3F9C981F 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 AKGNTFQALL
     IDGSNSKNEK MTFVELMYRD LPWASGAEAG ILSSDASSSI LLPASGTEAI SQLSKNSNIK
     QPGTWLYRID KAQLMPCAQP IQVPPYCDRL LSTAPRLPSK LLEEKKEGLT LPSPGAFLVD
     QPSETIVPTL VRGGGTVTRG RNVLTVTTSP IGNQQRQQTT KAVTRPRPNF SSTPHRPIVS
     LSDEDFELGP DAFEVTFPPF VTVQPELFRP NQRNGVQKST QRPLPDFSIR TPLKEEATTS
     VPREKTSSAA PAHSPIEEMS ENEESPFEAG SFDGEAVKFN EELEAIDKAL QTTKKQRPEL
     SVTPQPEDLS GDARVIETTE EDEEEAEIST ETTTEMSSTT TTTKAHTTTT TMMIPTEAPP
     SIFVFTTTQK PRAQSTTQKR IIVQQPSIVV NSQPPKQRND NQPTVNVGHA EEQSPRLAIL
     LPVMIILAWL VILVCIGAVV CCKRRNSRES SQLRAMYGAA YGVRPTAYES KRKESTYEDH
     LERAARLSGQ PALSGQQAGK VSLYGSYWNL EPLSNHSPAR LSTQERQSPP SFVNNGYTNQ
     TTRYTYAGHY
//
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