ID   PRAF1_PIG               Reviewed;         185 AA.
AC   Q52NJ0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Prenylated Rab acceptor protein 1;
DE   AltName: Full=PRA1 family protein 1;
GN   Name=RABAC1; Synonyms=PRAF1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Liu G.Y., Xiong Z.Y.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: General Rab protein regulator required for vesicle formation
CC       from the Golgi complex. May control vesicle docking and fusion by
CC       mediating the action of Rab GTPases to the SNARE complexes. In addition
CC       it inhibits the removal of Rab GTPases from the membrane by GDI1.
CC       {ECO:0000250|UniProtKB:O35394}.
CC   -!- SUBUNIT: Homodimer. Interacts with VAMP2 (synaptobrevin-2), prenylated
CC       Rab proteins, GDI1, NRDG1 and PCLO (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O35394};
CC       Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O35394}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:O35394}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle {ECO:0000250|UniProtKB:O35394}. Note=According to some
CC       authors, it is an integral membrane protein, while others showed that
CC       it is cytoplasmic and membrane-associated to Golgi and synaptic
CC       vesicles. {ECO:0000250|UniProtKB:O35394}.
CC   -!- SIMILARITY: Belongs to the PRA1 family. {ECO:0000305}.
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DR   EMBL; AY996815; AAY17511.1; -; mRNA.
DR   RefSeq; NP_001026965.1; NM_001031795.1.
DR   AlphaFoldDB; Q52NJ0; -.
DR   STRING; 9823.ENSSSCP00000003300; -.
DR   PaxDb; Q52NJ0; -.
DR   PeptideAtlas; Q52NJ0; -.
DR   PRIDE; Q52NJ0; -.
DR   GeneID; 595125; -.
DR   KEGG; ssc:595125; -.
DR   CTD; 10567; -.
DR   eggNOG; KOG3142; Eukaryota.
DR   InParanoid; Q52NJ0; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; 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:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR   InterPro; IPR004895; Prenylated_rab_accept_PRA1.
DR   PANTHER; PTHR19317; PTHR19317; 1.
DR   Pfam; PF03208; PRA1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW   Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN           1..185
FT                   /note="Prenylated Rab acceptor protein 1"
FT                   /id="PRO_0000266023"
FT   TOPO_DOM        1..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        79..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        95..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        113..131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        132..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        149..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        166..185
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          30..54
FT                   /note="Required for interaction with prenylated RAB3A and
FT                   VAMP2"
FT                   /evidence="ECO:0000250"
FT   REGION          165..185
FT                   /note="Required for interaction with GDI1"
FT                   /evidence="ECO:0000250"
FT   REGION          175..185
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          175..185
FT                   /note="Required for interaction with prenylated RAB3A and
FT                   VAMP2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   185 AA;  20665 MW;  701B472E5673AC43 CRC64;
     MAAQKDQQKD AEAEGLSATT LLPKLIPSGA GREWLERRRA TIRPWGSFVD QRRFSRPRNL
     GELCQRLVRN VEYYQSNYVF VFLGLILYCV VTSPMLLVAL AVFFGACYIL YLRTLQSKFV
     LFGREVSPAH QYALAGGVSF PFFWLAGAGS AVFWVLGATL VVIGSHAAFH QIEAVDGEEL
     QMEPV