ID   PRAF3_MACFA             Reviewed;         188 AA.
AC   Q4R4R4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 52.
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; ORFNames=QnpA-10140;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-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; AB169830; BAE01911.1; -; mRNA.
DR   RefSeq; NP_001272079.1; NM_001285150.1.
DR   AlphaFoldDB; Q4R4R4; -.
DR   STRING; 9541.XP_005547637.1; -.
DR   GeneID; 101925344; -.
DR   CTD; 10550; -.
DR   eggNOG; KOG4050; Eukaryota.
DR   OrthoDB; 1288023at2759; -.
DR   Proteomes; UP000233100; Unplaced.
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:0002037; P:negative regulation of L-glutamate import across plasma membrane; ISS:UniProtKB.
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_0000256848"
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;  21527 MW;  30E004CB5FE8EA49 CRC64;
     MDVNIAPLRA WDDFFPGSDR FAQPDFRDIS KWNNRVVSNL LYYQTNYLVV AAMMISVVGF
     LSPFNMILGG IVVVLVFTGF VWAAHNKDAL RRLKKRYPTT FVMVVMLASY FLISMFGGVM
     VFVFGITFPL LLMFIHASLR LRNLKNKLEN KMEGIGLKRT PMGIVLDALE QQEEGINRLT
     DYISKVKE