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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
 
 
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