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ARL14_MOUSE
ID   ARL14_MOUSE             Reviewed;         192 AA.
AC   Q3SXC5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=ADP-ribosylation factor-like protein 14;
DE   AltName: Full=ADP-ribosylation factor 7;
GN   Name=Arl14; Synonyms=Arf7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GTPase that recruits MYO1E to MHC class II-containing
CC       vesicles via the effector protein ARL14EP and hence controls the
CC       movement of these vesicles along the actin cytoskeleton in dendritic
CC       cells. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ARL14EP. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Colocalizes with MHC
CC       II-containing cytoplasmic vesicles. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC       {ECO:0000305}.
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DR   EMBL; BC104368; AAI04369.1; -; mRNA.
DR   EMBL; BC104369; AAI04370.1; -; mRNA.
DR   CCDS; CCDS59645.1; -.
DR   AlphaFoldDB; Q3SXC5; -.
DR   SMR; Q3SXC5; -.
DR   STRING; 10090.ENSMUSP00000138370; -.
DR   PhosphoSitePlus; Q3SXC5; -.
DR   PRIDE; Q3SXC5; -.
DR   ProteomicsDB; 283221; -.
DR   MGI; MGI:1918869; Arl14.
DR   eggNOG; KOG0070; Eukaryota.
DR   InParanoid; Q3SXC5; -.
DR   PhylomeDB; Q3SXC5; -.
DR   PRO; PR:Q3SXC5; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q3SXC5; protein.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR11711; PTHR11711; 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   Cytoplasmic vesicle; GTP-binding; Lipoprotein; Myristate;
KW   Nucleotide-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..192
FT                   /note="ADP-ribosylation factor-like protein 14"
FT                   /id="PRO_0000281148"
FT   BINDING         20..27
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..68
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         124..127
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   192 AA;  21835 MW;  E8FAFF2C5D08DAE2 CRC64;
     MGLLNSKNPQ SKQAHILLLG LDSAGKSTLL YRLKFAETLA TIPTIGFNVE MVQLQSSLTL
     TVWDVGGQEK MRTVWDCYCE NAQGLMYVVD CSEGKKRLED SRKEFKHILK NEHIKNTPVV
     ILANKQDLPG ALSAEDITRM FKVKKLCSNR NWYVQPCCAV TGEGLDDGFR KLTEFLKSYR
     RTRETLAIFK QK
 
 
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