ID   RGPA1_PIG               Reviewed;         337 AA.
AC   P86409;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Ral GTPase-activating protein subunit alpha-1;
DE   AltName: Full=GAP-related-interacting partner to E12 {ECO:0000250|UniProtKB:Q6GYQ0};
DE            Short=GRIPE {ECO:0000250|UniProtKB:Q6GYQ0};
DE   AltName: Full=GTPase-activating Rap/Ran-GAP domain-like 1 {ECO:0000250|UniProtKB:Q6GYQ0};
DE   AltName: Full=Tuberin-like protein 1 {ECO:0000250|UniProtKB:Q6GYQ0};
DE   AltName: Full=p240 {ECO:0000303|PubMed:19520869};
DE   Flags: Fragment;
GN   Name=RALGAPA1 {ECO:0000303|PubMed:19520869};
GN   Synonyms=GARNL1 {ECO:0000250|UniProtKB:Q6GYQ0},
GN   TULIP1 {ECO:0000250|UniProtKB:Q6GYQ0};
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] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=19520869; DOI=10.1074/jbc.m109.012112;
RA   Shirakawa R., Fukai S., Kawato M., Higashi T., Kondo H., Ikeda T.,
RA   Nakayama E., Okawa K., Nureki O., Kimura T., Kita T., Horiuchi H.;
RT   "Tuberous sclerosis tumor suppressor complex-like complexes act as GTPase-
RT   activating proteins for Ral GTPases.";
RL   J. Biol. Chem. 284:21580-21588(2009).
CC   -!- FUNCTION: Catalytic subunit of the heterodimeric RalGAP1 complex which
CC       acts as a GTPase activator for the Ras-like small GTPases RALA and
CC       RALB. {ECO:0000269|PubMed:19520869}.
CC   -!- SUBUNIT: Component of the heterodimeric RalGAP1 complex with RALGAPB.
CC       Heterodimerization is required for activity. Interacts with the HLH
CC       region of TCF3/isoform E12. {ECO:0000250|UniProtKB:Q6GYP7,
CC       ECO:0000269|PubMed:19520869}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6GYP7}. Nucleus
CC       {ECO:0000250|UniProtKB:Q6GYP7}. Note=Translocated to the nucleus, when
CC       associated with TCF3/E12. {ECO:0000250|UniProtKB:Q6GYP7}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CT797476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P86409; -.
DR   SMR; P86409; -.
DR   STRING; 9823.ENSSSCP00000020297; -.
DR   PaxDb; P86409; -.
DR   eggNOG; KOG3686; Eukaryota.
DR   InParanoid; P86409; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
DR   InterPro; IPR027107; Tuberin/Ral-act_asu.
DR   PANTHER; PTHR10063; PTHR10063; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; GTPase activation; Nucleus; Reference proteome.
FT   CHAIN           1..>337
FT                   /note="Ral GTPase-activating protein subunit alpha-1"
FT                   /id="PRO_0000390694"
FT   NON_TER         337
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   337 AA;  39654 MW;  BA90361845897D99 CRC64;
     MFSKKPHGDV KKSTQKVLDT KKDALTRLKH LRIVIENAES IDLKQFFDQH FSHIYYVFFE
     NFVTIEASLK QKGHKSQREE LDAILFIFEK ILQLLPERIH QRWQFHSIGL ILKKLLHTGN
     SLKIRREGVR LFLLWLQALQ NNCSREQLWM FSCLIPGFSA PQSEYGPRTL DNLINPPLNL
     QETQVTIEEI TPLVPPQSGD KGQEDLTSYF LEALLKYIVI QVKSLEWKNK ENQERGFSFL
     FSHFKKYYLP YIFPNICKEN SLYHPVLDIP QMRPKPHYVM IKKDAETNEA IYCTKEPFIK
     ARVIVIRWLV SFWLEPKPHT GPHIPGMEGE VLPKNIQ