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PRAF3_BOVIN
ID   PRAF3_BOVIN             Reviewed;         188 AA.
AC   Q5E9M1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=PRA1 family protein 3;
DE   AltName: Full=ADP-ribosylation factor-like protein 6-interacting protein 5;
DE            Short=ARL-6-interacting protein 5;
DE            Short=Aip-5;
GN   Name=ARL6IP5; Synonyms=PRAF3;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates intracellular concentrations of taurine and
CC       glutamate. Negatively modulates SLC1A1/EAAC1 glutamate transport
CC       activity by decreasing its affinity for glutamate in a PKC activity-
CC       dependent manner. Plays a role in the retention of SLC1A1/EAAC1 in the
CC       endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8R5J9,
CC       ECO:0000250|UniProtKB:Q9ES40}.
CC   -!- SUBUNIT: Homodimer. Heterodimer with ARL6IP1. Forms multimers.
CC       Interacts with ARL6. Interacts with prenylated RAB1A and RAB3A.
CC       Interacts with SLC1A1/EAAC1. Interacts with RTN2 (via first
CC       transmembrane domain). Does not interact with VAMP1, VAMP2 or VAMP3.
CC       {ECO:0000250|UniProtKB:Q8R5J9, ECO:0000250|UniProtKB:Q9ES40}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9ES40}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9ES40}; Multi-pass
CC       membrane protein {ECO:0000255}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9ES40}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9ES40}. Note=Also exists as a soluble form in
CC       the cytoplasm. Associated with microtubules.
CC       {ECO:0000250|UniProtKB:Q9ES40}.
CC   -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
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DR   EMBL; BT020899; AAX08916.1; -; mRNA.
DR   EMBL; BC102757; AAI02758.1; -; mRNA.
DR   RefSeq; NP_001014891.1; NM_001014891.1.
DR   AlphaFoldDB; Q5E9M1; -.
DR   SMR; Q5E9M1; -.
DR   STRING; 9913.ENSBTAP00000028661; -.
DR   PaxDb; Q5E9M1; -.
DR   PeptideAtlas; Q5E9M1; -.
DR   PRIDE; Q5E9M1; -.
DR   Ensembl; ENSBTAT00000028661; ENSBTAP00000028661; ENSBTAG00000021506.
DR   GeneID; 509977; -.
DR   KEGG; bta:509977; -.
DR   CTD; 10550; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021506; -.
DR   VGNC; VGNC:26151; ARL6IP5.
DR   eggNOG; KOG4050; Eukaryota.
DR   GeneTree; ENSGT00390000008631; -.
DR   HOGENOM; CLU_097683_0_0_1; -.
DR   InParanoid; Q5E9M1; -.
DR   OMA; QMKKRYP; -.
DR   OrthoDB; 1288023at2759; -.
DR   TreeFam; TF105479; -.
DR   Reactome; R-BTA-210500; Glutamate Neurotransmitter Release Cycle.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000021506; Expressed in cardiac atrium and 104 other tissues.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0098712; P:L-glutamate import across plasma membrane; IEA:Ensembl.
DR   GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:AgBase.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0002037; P:negative regulation of L-glutamate import across plasma membrane; ISS:UniProtKB.
DR   GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IEA:Ensembl.
DR   GO; GO:0051051; P:negative regulation of transport; IBA:GO_Central.
DR   GO; GO:0036475; P:neuron death in response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IEA:Ensembl.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR   InterPro; IPR004895; Prenylated_rab_accept_PRA1.
DR   PANTHER; PTHR12859; PTHR12859; 1.
DR   Pfam; PF03208; PRA1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..188
FT                   /note="PRA1 family protein 3"
FT                   /id="PRO_0000256847"
FT   TOPO_DOM        1..35
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          103..117
FT                   /note="Required for homodimer formation and heterodimer
FT                   formation with ARL6IP1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R5J9"
FT   REGION          136..188
FT                   /note="Targeting to endoplasmic reticulum membrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ES40"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O75915"
SQ   SEQUENCE   188 AA;  21666 MW;  DDCB3D3CC815AF4F CRC64;
     MDVNIAPLRA WDDFFPGSDR FARPDFRDIS KWNNRVVSNL LYYQTNYLVV AAMMISVVGF
     LSPFNMILGG IVVVLVFTGF VWAAHNKDIL RRMKKQYPTA FVMVVMLASY FLISLFGGVM
     VFVFGITFPL LLMFIHASLR LRNLKNKLEN KMEEIGLKRT PMGIVLDALE QQEETITKFS
     DYISKMKE
 
 
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