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ARL3_TAEGU
ID   ARL3_TAEGU              Reviewed;         182 AA.
AC   B5FYQ0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=ADP-ribosylation factor-like protein 3;
GN   Name=ARL3;
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=17018643; DOI=10.1073/pnas.0607098103;
RA   Wada K., Howard J.T., McConnell P., Whitney O., Lints T., Rivas M.V.,
RA   Horita H., Patterson M.A., White S.A., Scharff C., Haesler S., Zhao S.,
RA   Sakaguchi H., Hagiwara M., Shiraki T., Hirozane-Kishikawa T., Skene P.,
RA   Hayashizaki Y., Carninci P., Jarvis E.D.;
RT   "A molecular neuroethological approach for identifying and characterizing a
RT   cascade of behaviorally regulated genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15212-15217(2006).
CC   -!- FUNCTION: Small GTP-binding protein which cycles between an inactive
CC       GDP-bound and an active GTP-bound form, and the rate of cycling is
CC       regulated by guanine nucleotide exchange factors (GEF) and GTPase-
CC       activating proteins (GAP). Required for normal cytokinesis and cilia
CC       signaling. Required for targeting proteins to the ciliary membrane by
CC       releasing myristoylated protein from unc119 cargo adapters into the
CC       cilium (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC       centrosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection,
CC       cilium {ECO:0000250}. Note=Detected predominantly in the photoreceptor
CC       connecting cilium. Centrosome-associated throughout the cell cycle. Not
CC       detected to interphase microtubules. Present on the mitotic spindle (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; DQ214094; ACH44161.1; -; mRNA.
DR   EMBL; DQ214098; ACH44164.1; -; mRNA.
DR   AlphaFoldDB; B5FYQ0; -.
DR   SMR; B5FYQ0; -.
DR   STRING; 59729.ENSTGUP00000032998; -.
DR   Ensembl; ENSTGUT00000034756; ENSTGUP00000032998; ENSTGUG00000019757.
DR   GeneTree; ENSGT00940000155737; -.
DR   InParanoid; B5FYQ0; -.
DR   Proteomes; UP000007754; Chromosome 6.
DR   GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR   GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0032794; F:GTPase activating protein binding; IEA:Ensembl.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:Ensembl.
DR   GO; GO:0042073; P:intraciliary transport; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   GO; GO:0042461; P:photoreceptor cell development; ISS:UniProtKB.
DR   GO; GO:1903441; P:protein localization to ciliary membrane; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; ISS:UniProtKB.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR044612; ARL2/3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR45697; PTHR45697; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00178; SAR; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cell projection; Cytoplasm; Cytoskeleton;
KW   Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Myristate;
KW   Nucleotide-binding; Nucleus; Protein transport; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..182
FT                   /note="ADP-ribosylation factor-like protein 3"
FT                   /id="PRO_0000356299"
FT   BINDING         24..31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   182 AA;  20442 MW;  67FE4D6F5184F881 CRC64;
     MGLLSILRKL KSTPDQEVRI LLLGLDNAGK TTLLKQLASE DISHITPTQG FNIKSVQSQG
     FKLNVWDIGG QRKIRPYWRN YFENTDILIY VIDSADRKRF EETGQELAEL LDEEKLSGVP
     VLIFANKQDL LTAAPASEIA EGLNLHTIRD RVWQIQSCSA LSGEGVQDGM NWVCKNVSTK
     KK
 
 
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