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FEH1_CAEEL
ID   FEH1_CAEEL              Reviewed;         665 AA.
AC   Q9BKZ9; H2L0Q7; H2L0Q8; Q8WQE2;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Protein Fe65 homolog {ECO:0000312|WormBase:Y54F10AM.2a};
GN   Name=feh-1 {ECO:0000312|WormBase:Y54F10AM.2a};
GN   ORFNames=Y54F10AM.2 {ECO:0000312|WormBase:Y54F10AM.2a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {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   [2] {ECO:0000312|EMBL:CAC87812.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 89-665 (ISOFORM A), FUNCTION, INTERACTION
RP   WITH APL-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11896189; DOI=10.1242/jcs.115.7.1411;
RA   Zambrano N., Bimonte M., Arbucci S., Gianni D., Russo T., Bazzicalupo P.;
RT   "feh-1 and apl-1, the Caenorhabditis elegans orthologues of mammalian Fe65
RT   and beta-amyloid precursor protein genes, are involved in the same pathway
RT   that controls nematode pharyngeal pumping.";
RL   J. Cell Sci. 115:1411-1422(2002).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15355315; DOI=10.1111/j.1460-9568.2004.03611.x;
RA   Bimonte M., Gianni D., Allegra D., Russo T., Zambrano N.;
RT   "Mutation of the feh-1 gene, the Caenorhabditis elegans orthologue of
RT   mammalian Fe65, decreases the expression of two acetylcholinesterase
RT   genes.";
RL   Eur. J. Neurosci. 20:1483-1488(2004).
CC   -!- FUNCTION: Modulates pharyngeal pumping activity, at least in part by
CC       regulating expression of the acetylcholinesterase genes ace-1 and ace-2
CC       (PubMed:11896189, PubMed:15355315). {ECO:0000269|PubMed:11896189,
CC       ECO:0000269|PubMed:15355315}.
CC   -!- SUBUNIT: Interacts (via PID 2 domain) with apl-1 (via cytoplasmic
CC       domain). {ECO:0000269|PubMed:11896189}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11896189}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11896189}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a {ECO:0000312|WormBase:Y54F10AM.2a};
CC         IsoId=Q9BKZ9-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:Y54F10AM.2b};
CC         IsoId=Q9BKZ9-2; Sequence=VSP_057961;
CC       Name=c {ECO:0000312|WormBase:Y54F10AM.2c};
CC         IsoId=Q9BKZ9-3; Sequence=VSP_057960;
CC   -!- TISSUE SPECIFICITY: Expressed in the pharynx (including pharyngeal
CC       muscle and nerve cells), ventral nerve cord and tail neurons.
CC       {ECO:0000269|PubMed:11896189}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the pharynx from three-fold stage
CC       embryos to adulthood. {ECO:0000269|PubMed:11896189}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11896189}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality or larval arrest
CC       (PubMed:11896189, PubMed:15355315). Heterozygous animals are viable and
CC       display increased pharyngeal pumping rates associated with reduced
CC       acetylcholinesterase activity (PubMed:11896189, PubMed:15355315).
CC       {ECO:0000269|PubMed:11896189, ECO:0000269|PubMed:15355315}.
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DR   EMBL; BX284603; CCD73819.2; -; Genomic_DNA.
DR   EMBL; BX284603; CCD73820.1; -; Genomic_DNA.
DR   EMBL; BX284603; CCD73821.1; -; Genomic_DNA.
DR   EMBL; AJ345015; CAC87812.1; -; mRNA.
DR   RefSeq; NP_001022906.1; NM_001027735.3. [Q9BKZ9-2]
DR   RefSeq; NP_001022907.1; NM_001027736.4.
DR   RefSeq; NP_497578.4; NM_065177.4. [Q9BKZ9-1]
DR   AlphaFoldDB; Q9BKZ9; -.
DR   SMR; Q9BKZ9; -.
DR   DIP; DIP-25952N; -.
DR   IntAct; Q9BKZ9; 2.
DR   STRING; 6239.Y54F10AM.2a; -.
DR   EPD; Q9BKZ9; -.
DR   PaxDb; Q9BKZ9; -.
DR   PeptideAtlas; Q9BKZ9; -.
DR   EnsemblMetazoa; Y54F10AM.2a.1; Y54F10AM.2a.1; WBGene00001410. [Q9BKZ9-1]
DR   EnsemblMetazoa; Y54F10AM.2b.1; Y54F10AM.2b.1; WBGene00001410. [Q9BKZ9-2]
DR   EnsemblMetazoa; Y54F10AM.2c.1; Y54F10AM.2c.1; WBGene00001410. [Q9BKZ9-3]
DR   EnsemblMetazoa; Y54F10AM.2c.2; Y54F10AM.2c.2; WBGene00001410. [Q9BKZ9-3]
DR   GeneID; 175373; -.
DR   KEGG; cel:CELE_Y54F10AM.2; -.
DR   UCSC; Y54F10AM.2c.2; c. elegans.
DR   CTD; 175373; -.
DR   WormBase; Y54F10AM.2a; CE50322; WBGene00001410; feh-1. [Q9BKZ9-1]
DR   WormBase; Y54F10AM.2b; CE32985; WBGene00001410; feh-1. [Q9BKZ9-2]
DR   WormBase; Y54F10AM.2c; CE38648; WBGene00001410; feh-1. [Q9BKZ9-3]
DR   eggNOG; ENOG502QT08; Eukaryota.
DR   GeneTree; ENSGT00390000000002; -.
DR   InParanoid; Q9BKZ9; -.
DR   OMA; NMAVDYS; -.
DR   OrthoDB; 437627at2759; -.
DR   Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   PRO; PR:Q9BKZ9; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00001410; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   ExpressionAtlas; Q9BKZ9; baseline and differential.
DR   GO; GO:0005884; C:actin filament; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001540; F:amyloid-beta binding; IDA:WormBase.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR   GO; GO:0007631; P:feeding behavior; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR039576; APBB1/2/3.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR14058; PTHR14058; 1.
DR   Pfam; PF00640; PID; 2.
DR   SMART; SM00462; PTB; 2.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; SSF51045; 1.
DR   PROSITE; PS01179; PID; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Reference proteome; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..665
FT                   /note="Protein Fe65 homolog"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000434596"
FT   DOMAIN          233..266
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          330..456
FT                   /note="PID 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          499..615
FT                   /note="PID 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..111
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057960"
FT   VAR_SEQ         639..665
FT                   /note="KGWTETFRDAFGSVTSRMVPSRSAQRL -> MD (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057961"
SQ   SEQUENCE   665 AA;  76322 MW;  A26E8260C2852D3F CRC64;
     MREGTPRVRI EVNKGSNRPS QFVSESEEQR LQRVQSRDSD TATMNFVTDD RMMEEHDEYS
     AFKEAYEEEE SREYVIENGV KRLVNQHYDS RGYSSAGRGQ KGRREEERRR NMAVDYSSQD
     FRQSLAAIDQ ASRDGAISRG EDGVRVRQIG DTTIMTEHRD PYSFYWQLDQ ARREAESPPR
     RPPPTDYVID EEEEVLETVY SPEADDVMFE NQYRRPVRHP LPPPPPIMEE EPKDLPPGWE
     KHEDPQGYSY YWHVDSGTIQ RQPPPPVNRE TQADAPPPQI IQLPPQQPVI EEHAFKQTTT
     KRRIEQDEMS EREIEDVAMI ENGDTYHKPV RFAVRSLGWT DISEDELTAE KSSRAVNRAI
     VDLTTRSDID SIPKWGDGRE LIMELDDNEL ALLDPDSMNV IHSERIQAIR VWGVGRDNGR
     DFAYVSRDRG TRRFMCHVFR CDTSAKTIAN TLRDICKRLM LHRRPSSLHA IESGEKRIVR
     SEGLTAPIDE PRKVIRCHFL GVTQVPKATG IEILNEAVDR LVSQVRSERW ILADVSIAPS
     TIAIVEVNGQ QIAECRVRYL SFLGIGRDVK HCAFIMQTSS ESFMCYVFHV EPNAAAMAKM
     VEAACKLRYQ KVLDAHSSSR HHSGMSIHGQ HPPSTYHGKG WTETFRDAFG SVTSRMVPSR
     SAQRL
 
 
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