PRAF3_PONAB
ID PRAF3_PONAB Reviewed; 188 AA.
AC Q5R4X8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 79.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR861111; CAH93188.1; -; mRNA.
DR RefSeq; NP_001127640.1; NM_001134168.1.
DR AlphaFoldDB; Q5R4X8; -.
DR STRING; 9601.ENSPPYP00000015350; -.
DR Ensembl; ENSPPYT00000015963; ENSPPYP00000015350; ENSPPYG00000013728.
DR GeneID; 100174720; -.
DR KEGG; pon:100174720; -.
DR CTD; 10550; -.
DR eggNOG; KOG4050; Eukaryota.
DR GeneTree; ENSGT00390000008631; -.
DR HOGENOM; CLU_097683_0_0_1; -.
DR InParanoid; Q5R4X8; -.
DR OMA; QMKKRYP; -.
DR OrthoDB; 1288023at2759; -.
DR TreeFam; TF105479; -.
DR Proteomes; UP000001595; Chromosome 3.
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: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: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: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_0000256850"
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; 21615 MW; 3AA708C6D0901B44 CRC64;
MDVNIAPLRA WDDFFPGSDR FARPDFRDIS KWNNRVVSNL LYYQTNYLVV AAMMISIVGF
LSPFNMILGG IVVVLVFTGF VWAAHNKDVL RRMKKRYPTT FVMVVMLASY FLISMFGGVM
VFVFGITFPL LLMFIHASLR LRNLKNKLEN KMEGIGLKRT PMGIVLDALE QQEEGINRLT
DYISKVKE
