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EFA6_CAEEL
ID   EFA6_CAEEL              Reviewed;         818 AA.
AC   G5EET6; D4YWC5; G5EBY7; Q9XWG7;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Exchange factor for Arf-6 {ECO:0000303|PubMed:26339988};
DE   AltName: Full=Arf guanine nucleotide exchange factor efa-6 {ECO:0000303|PubMed:21943602};
DE   AltName: Full=Pleckstrin homology domain-containing protein efa-6 {ECO:0000303|PubMed:17676955};
GN   Name=efa-6 {ECO:0000303|PubMed:17676955, ECO:0000312|WormBase:Y55D9A.1a};
GN   ORFNames=Y55D9A.1 {ECO:0000312|WormBase:Y55D9A.1a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000312|EMBL:ABQ42569.1, ECO:0000312|EMBL:ABQ42570.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:ABQ42569.1};
RX   PubMed=17676955; DOI=10.1371/journal.pgen.0030128;
RA   O'Rourke S.M., Dorfman M.D., Carter J.C., Bowerman B.;
RT   "Dynein modifiers in C. elegans: light chains suppress conditional heavy
RT   chain mutants.";
RL   PLoS Genet. 3:E128-E128(2007).
RN   [2] {ECO:0000312|EMBL:CAA21701.1, ECO:0000312|EMBL:CAC70120.1, ECO:0000312|EMBL:CAM82814.1, ECO:0000312|EMBL:CBL43465.1, ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:CAC70120.1,
RC   ECO:0000312|Proteomes:UP000001940};
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   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   GLU-449.
RX   PubMed=21076413; DOI=10.1038/ncb2128;
RA   O'Rourke S.M., Christensen S.N., Bowerman B.;
RT   "Caenorhabditis elegans EFA-6 limits microtubule growth at the cell
RT   cortex.";
RL   Nat. Cell Biol. 12:1235-1241(2010).
RN   [4]
RP   FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-449.
RX   PubMed=21943602; DOI=10.1016/j.neuron.2011.07.009;
RA   Chen L., Wang Z., Ghosh-Roy A., Hubert T., Yan D., O'Rourke S.,
RA   Bowerman B., Wu Z., Jin Y., Chisholm A.D.;
RT   "Axon regeneration pathways identified by systematic genetic screening in
RT   C. elegans.";
RL   Neuron 71:1043-1057(2011).
RN   [5]
RP   FUNCTION, INTERACTION WITH TAC-1 AND ZYG-8, SUBCELLULAR LOCATION, DOMAIN,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=26339988; DOI=10.7554/elife.08695;
RA   Chen L., Chuang M., Koorman T., Boxem M., Jin Y., Chisholm A.D.;
RT   "Axon injury triggers EFA-6 mediated destabilization of axonal microtubules
RT   via TACC and doublecortin like kinase.";
RL   Elife 4:0-0(2015).
CC   -!- FUNCTION: Guanine nucleotide exchange factor for arf-6 (By similarity).
CC       Involved in response to injury in mechanosensory neurons. Inhibits axon
CC       regrowth via microtubule dynamics, possibly by inducing axonal
CC       microtubule catastrophes (PubMed:21943602, PubMed:26339988). Limits
CC       microtubule growth near the cellular cortex of early embryonic cells
CC       (PubMed:21076413). {ECO:0000250|UniProtKB:Q9NYI0,
CC       ECO:0000269|PubMed:21076413, ECO:0000269|PubMed:21943602,
CC       ECO:0000269|PubMed:26339988}.
CC   -!- SUBUNIT: Interacts (via short N-terminal region) with microtubule-
CC       associated proteins tac-1 and zyg-8. {ECO:0000269|PubMed:26339988}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000269|PubMed:17676955, ECO:0000269|PubMed:21076413,
CC       ECO:0000269|PubMed:26339988}. Cell membrane
CC       {ECO:0000269|PubMed:26339988}. Note=Present throughout the embryonic
CC       cortex during the first embryonic mitosis, but at reduced levels in the
CC       posterior cortex (PubMed:21076413). Localizes to the plasma membrane of
CC       the soma and processes of neurons. Localizes to the cellular cortex in
CC       the steady (uninjured) state. Following injury, transiently relocalizes
CC       to the sites marked by the microtubule minus end binding protein ptrn-1
CC       together with tac-1 (PubMed:26339988). {ECO:0000269|PubMed:21076413,
CC       ECO:0000269|PubMed:26339988}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=b {ECO:0000303|PubMed:17676955, ECO:0000303|PubMed:9851916};
CC         IsoId=G5EET6-1; Sequence=Displayed;
CC       Name=a {ECO:0000303|PubMed:9851916};
CC         IsoId=G5EET6-2; Sequence=VSP_058547;
CC       Name=c {ECO:0000303|PubMed:17676955, ECO:0000303|PubMed:9851916};
CC         IsoId=G5EET6-3; Sequence=VSP_058547, VSP_058548;
CC       Name=d {ECO:0000303|PubMed:9851916};
CC         IsoId=G5EET6-4; Sequence=VSP_058546;
CC   -!- DEVELOPMENTAL STAGE: Isoform b: Enriched cortically both in the
CC       anterior portion of the one-cell zygote and at the blastomere boundary
CC       in two-cell embryos. Isoform c: Localizes to nonpolarized cellular
CC       cortex in oocytes and early one-cell zygotes and anterior cellular
CC       cortex in one-cell embryos subsequent to pseudocleavage. Present at the
CC       interface of the AB and P1 cells. Undetectable by the four-cell stage.
CC       {ECO:0000269|PubMed:17676955}.
CC   -!- DOMAIN: A short conserved N-terminal region is necessary for the
CC       function of this protein (PubMed:21943602, PubMed:26339988). Transient
CC       relocalization to microtubule minus ends after neuronal injury also
CC       requires this region (PubMed:26339988). {ECO:0000269|PubMed:21943602,
CC       ECO:0000269|PubMed:26339988}.
CC   -!- DISRUPTION PHENOTYPE: Abnormally long and dense microtubules at the
CC       cellular cortex of early embryonic cells and growing microtubule plus
CC       ends reside at the cortex for up to five times longer. Causes excess
CC       centrosome separation and displacement towards the cellular cortex
CC       early in mitosis and subsequently a loss of anaphase spindle-pole
CC       oscillations and increased rates of spindle elongation. The centrosome
CC       separation phenotype is dependent on the motor protein dynein. Weakly
CC       delayed nuclear envelope breakdown (PubMed:21076413). Displays mild
CC       posterior lateral microtubule (PLM) axon overshooting in development
CC       and enhanced PLM regrowth following neuronal injury acting early in
CC       regrowth (PubMed:21943602). Axons display elevated numbers of growing
CC       microtubules in the steady (uninjured) state and display impenetrant
CC       developmental overgrowth in the absence of injury (PubMed:26339988).
CC       {ECO:0000269|PubMed:21076413, ECO:0000269|PubMed:21943602,
CC       ECO:0000269|PubMed:26339988}.
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DR   EMBL; EF473217; ABQ42569.1; -; mRNA.
DR   EMBL; EF473218; ABQ42570.1; -; mRNA.
DR   EMBL; BX284604; CAA21701.1; -; Genomic_DNA.
DR   EMBL; BX284604; CAC70120.1; -; Genomic_DNA.
DR   EMBL; BX284604; CAM82814.1; -; Genomic_DNA.
DR   EMBL; BX284604; CBL43465.1; -; Genomic_DNA.
DR   PIR; T27189; T27189.
DR   RefSeq; NP_001122818.1; NM_001129346.1. [G5EET6-3]
DR   RefSeq; NP_001255652.1; NM_001268723.1. [G5EET6-4]
DR   RefSeq; NP_502416.1; NM_070015.4. [G5EET6-1]
DR   RefSeq; NP_502417.1; NM_070016.3. [G5EET6-2]
DR   AlphaFoldDB; G5EET6; -.
DR   SMR; G5EET6; -.
DR   STRING; 6239.Y55D9A.1b; -.
DR   PaxDb; G5EET6; -.
DR   EnsemblMetazoa; Y55D9A.1a.1; Y55D9A.1a.1; WBGene00013223. [G5EET6-2]
DR   EnsemblMetazoa; Y55D9A.1b.1; Y55D9A.1b.1; WBGene00013223. [G5EET6-1]
DR   EnsemblMetazoa; Y55D9A.1c.1; Y55D9A.1c.1; WBGene00013223. [G5EET6-3]
DR   EnsemblMetazoa; Y55D9A.1d.1; Y55D9A.1d.1; WBGene00013223. [G5EET6-4]
DR   GeneID; 178217; -.
DR   KEGG; cel:CELE_Y55D9A.1; -.
DR   UCSC; Y55D9A.1b; c. elegans.
DR   CTD; 178217; -.
DR   WormBase; Y55D9A.1a; CE19234; WBGene00013223; efa-6. [G5EET6-2]
DR   WormBase; Y55D9A.1b; CE29066; WBGene00013223; efa-6. [G5EET6-1]
DR   WormBase; Y55D9A.1c; CE40826; WBGene00013223; efa-6. [G5EET6-3]
DR   WormBase; Y55D9A.1d; CE44770; WBGene00013223; efa-6. [G5EET6-4]
DR   eggNOG; KOG0932; Eukaryota.
DR   GeneTree; ENSGT00940000155061; -.
DR   InParanoid; G5EET6; -.
DR   OMA; EWCEKIN; -.
DR   OrthoDB; 532213at2759; -.
DR   PhylomeDB; G5EET6; -.
DR   PRO; PR:G5EET6; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00013223; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR   GO; GO:0036449; C:microtubule minus-end; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0007019; P:microtubule depolymerization; IMP:UniProtKB.
DR   GO; GO:0007077; P:mitotic nuclear membrane disassembly; IMP:UniProtKB.
DR   GO; GO:0048692; P:negative regulation of axon extension involved in regeneration; IMP:UniProtKB.
DR   GO; GO:0048681; P:negative regulation of axon regeneration; IMP:WormBase.
DR   GO; GO:1902845; P:negative regulation of mitotic spindle elongation; IMP:UniProtKB.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IDA:UniProtKB.
DR   GO; GO:0046602; P:regulation of mitotic centrosome separation; IMP:UniProtKB.
DR   GO; GO:0048678; P:response to axon injury; IDA:UniProtKB.
DR   CDD; cd00171; Sec7; 1.
DR   Gene3D; 1.10.1000.11; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041681; PH_9.
DR   InterPro; IPR001605; PH_dom-spectrin-type.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR023394; Sec7_C_sf.
DR   InterPro; IPR000904; Sec7_dom.
DR   InterPro; IPR035999; Sec7_dom_sf.
DR   Pfam; PF15410; PH_9; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; SSF48425; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Membrane; Reference proteome.
FT   CHAIN           1..818
FT                   /note="Exchange factor for Arf-6"
FT                   /id="PRO_0000437502"
FT   DOMAIN          356..532
FT                   /note="SEC7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT   DOMAIN          569..681
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          92..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..803
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..184
FT                   /note="Missing (in isoform d)"
FT                   /id="VSP_058546"
FT   VAR_SEQ         99..100
FT                   /note="Missing (in isoform a and isoform c)"
FT                   /id="VSP_058547"
FT   VAR_SEQ         180..230
FT                   /note="Missing (in isoform c)"
FT                   /id="VSP_058548"
FT   MUTAGEN         449
FT                   /note="E->K: Localizes to the cellular cortex of embryo and
FT                   promotes robust spindle rocking as in wild-type during the
FT                   first embryonic mitosis. Inhibits axon regrowth following
FT                   neuronal injury."
FT                   /evidence="ECO:0000269|PubMed:21076413,
FT                   ECO:0000269|PubMed:21943602"
SQ   SEQUENCE   818 AA;  90646 MW;  9E0B4E87563262C0 CRC64;
     MAKVASSGAE EALATIDGAP RRNVKKSEAF VMSGDVLISL NRNVSSTYAK LLGDQLPPGT
     TVASSIHPHQ LSRATASAGV SFPSMNRNGA AAQKLSRLPV PVSTSQIERR GSLARKTSEE
     SSPTAIRMLK TAPIERMEST DVEESEEETV MMTTDEKENQ KKPNENDDEV MVVDEEQFIV
     VSNDMKSPNE EIVAKSLRSA MFTMPTDNHH HSYNSSPQIS TLSPHLRSNG DGPSRSPVYD
     DVDDDLNGSL DAKDMSNNSH QQSFRSPENY SEKDTPSKHS VVTIDGSGVS NHYDQDGMFS
     HVYYSTQDTT PKHGSPSLRK QIFESRTTPN TAASNSSASA SPSLHATSES RGATGGVSLR
     SAESSNLNQT AVPSTSTNSV GGEREAAQIA RNLYELKNCT STQVADRLNE QNEFSFLILV
     KYLELFQFST TRIDAALREF LSRVELRGES SARERLLRVF SARYLECNPA IFDSLDEVHT
     LTCALLLLNS DLHGPNMGKK MTARDFITNI AHTGCTFKRE MLKTLFQSIK DNAISLQNSA
     KNSTANGSVA STSRRQPQQI YEVDPDSVVE YYSGFLMRKY VRETDGGKTP FGRRSWRMVY
     ARLRGLVLYF DTDEHPKATS RYASLENAVS LHHALAEPAP DYKKKSFVFR VRIAHGGEIL
     FQTSNQKELQ EWCEKINFVA AAFSSPTLPL PVTSKPETAP MPRLPRIPCL APITKQLSTH
     EARVAELNEM IEIVSQSVSP NQPQQLITDR WVLLSFEKRR YSTYINVLRR SLEARKASSA
     TTMNIMMTPT RRQQQNQKPV VSEDRLSYTD AVNGAAAH
 
 
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