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AR2BP_BOVIN
ID   AR2BP_BOVIN             Reviewed;         163 AA.
AC   Q32PC9; A4IFR7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=ADP-ribosylation factor-like protein 2-binding protein;
DE            Short=ARF-like 2-binding protein;
DE   AltName: Full=Binder of ARF2 protein 1;
GN   Name=ARL2BP; Synonyms=BART1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Crossbred X Angus, and Hereford; TISSUE=Fetal pons, and Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ARL2, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10488091; DOI=10.1074/jbc.274.39.27553;
RA   Sharer J.D., Kahn R.A.;
RT   "The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and
RT   initial characterization.";
RL   J. Biol. Chem. 274:27553-27561(1999).
RN   [3]
RP   IDENTIFICATION IN A COMPLEX WITH ARL2 AND SLC25A6, AND TISSUE SPECIFICITY.
RX   PubMed=11809823; DOI=10.1091/mbc.01-05-0245;
RA   Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.;
RT   "ARL2 and BART enter mitochondria and bind the adenine nucleotide
RT   transporter.";
RL   Mol. Biol. Cell 13:71-83(2002).
CC   -!- FUNCTION: Together with ARL2, plays a role in the nuclear
CC       translocation, retention and transcriptional activity of STAT3. May
CC       play a role as an effector of ARL2 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GTP bound ARL2 and ARL3; the complex ARL2-
CC       ARL2BP as well as ARL2BP alone, binds to SLC25A4/ANT1. Interaction with
CC       ARL2 may be required for targeting to cilia basal body (By similarity).
CC       Interacts with STAT3; interaction is enhanced with ARL2. Found in a
CC       complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and
CC       STAT4. Found in a complex with ARL2BP, ARL2 and SLC25A6. {ECO:0000250,
CC       ECO:0000269|PubMed:10488091, ECO:0000269|PubMed:11809823}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
CC       intermembrane space {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, cilium basal body {ECO:0000250}. Note=Detected in the
CC       midbody matrix. Not detected in the Golgi, nucleus and on the mitotic
CC       spindle. Centrosome-associated throughout the cell cycle. Not detected
CC       to interphase microtubules (By similarity). In retina photoreceptor
CC       cells, localized in the distal connecting cilia, basal body, ciliary-
CC       associated centriole, and ciliary rootlet. Interaction with ARL2 may be
CC       required for cilia basal body localization (By similarity). The complex
CC       formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q32PC9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q32PC9-2; Sequence=VSP_025316;
CC   -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:10488091,
CC       ECO:0000269|PubMed:11809823}.
CC   -!- SIMILARITY: Belongs to the ARL2BP family. {ECO:0000305}.
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DR   EMBL; BC108166; AAI08167.1; -; mRNA.
DR   EMBL; BC134728; AAI34729.1; -; mRNA.
DR   RefSeq; NP_001069742.2; NM_001076274.2. [Q32PC9-1]
DR   AlphaFoldDB; Q32PC9; -.
DR   SMR; Q32PC9; -.
DR   BioGRID; 541183; 1.
DR   STRING; 9913.ENSBTAP00000006363; -.
DR   PaxDb; Q32PC9; -.
DR   Ensembl; ENSBTAT00000006363; ENSBTAP00000006363; ENSBTAG00000004844. [Q32PC9-1]
DR   GeneID; 613462; -.
DR   KEGG; bta:613462; -.
DR   CTD; 23568; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004844; -.
DR   eggNOG; ENOG502RYJD; Eukaryota.
DR   GeneTree; ENSGT00390000015052; -.
DR   HOGENOM; CLU_116781_0_0_1; -.
DR   InParanoid; Q32PC9; -.
DR   OMA; LIQRNFM; -.
DR   OrthoDB; 1403493at2759; -.
DR   TreeFam; TF315143; -.
DR   Reactome; R-BTA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000004844; Expressed in spermatid and 106 other tissues.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; TAS:AgBase.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0051457; P:maintenance of protein location in nucleus; ISS:UniProtKB.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
DR   Gene3D; 1.20.1520.10; -; 1.
DR   InterPro; IPR038849; ARL2BP.
DR   InterPro; IPR023379; BART_dom.
DR   InterPro; IPR042541; BART_sf.
DR   PANTHER; PTHR15487; PTHR15487; 1.
DR   Pfam; PF11527; ARL2_Bind_BART; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW   Mitochondrion; Nucleus; Reference proteome.
FT   CHAIN           1..163
FT                   /note="ADP-ribosylation factor-like protein 2-binding
FT                   protein"
FT                   /id="PRO_0000287112"
FT   VAR_SEQ         1..13
FT                   /note="MDALEEESFALSF -> MR (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_025316"
SQ   SEQUENCE   163 AA;  18772 MW;  B4E2678AC0383EA7 CRC64;
     MDALEEESFA LSFSSASDAE FDAVVGYLED IIMDDEFQLL QRNFMDKYYQ EFEDTEENKL
     TYTPIFNEYI SLVEKYIEEQ LLERIPGFNM AAFTTTLQHH KDEVAGDIFD MLLTFTDFLA
     FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK SSSVPASQNN LRP
 
 
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