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Database: UniProt
Entry: A0A2I3GHU9_NOMLE
LinkDB: A0A2I3GHU9_NOMLE
Original site: A0A2I3GHU9_NOMLE 
ID   A0A2I3GHU9_NOMLE        Unreviewed;       343 AA.
AC   A0A2I3GHU9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Protein XRP2 {ECO:0000256|ARBA:ARBA00015771, ECO:0000256|PIRNR:PIRNR037947};
GN   Name=RP2 {ECO:0000313|Ensembl:ENSNLEP00000030881.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000030881.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000030881.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000030881.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Acts as a GTPase-activating protein (GAP) for tubulin in
CC       concert with tubulin-specific chaperone C, but does not enhance tubulin
CC       heterodimerization. {ECO:0000256|PIRNR:PIRNR037947}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342};
CC       Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004342}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004423}.
CC   -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000256|ARBA:ARBA00008848,
CC       ECO:0000256|PIRNR:PIRNR037947}.
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DR   EMBL; ADFV01063403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01063404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01063405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01063406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01063407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01063408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I3GHU9; -.
DR   Ensembl; ENSNLET00000035455.1; ENSNLEP00000030881.1; ENSNLEG00000031771.1.
DR   GeneTree; ENSGT00940000158262; -.
DR   OMA; KDYMLTG; -.
DR   Proteomes; UP000001073; Chromosome X.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.160.20.70; -; 1.
DR   Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 1.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR036223; CAP_C_sf.
DR   InterPro; IPR006599; CARP_motif.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR   InterPro; IPR039093; XRP2.
DR   PANTHER; PTHR15440:SF0; PROTEIN XRP2; 1.
DR   PANTHER; PTHR15440; XRP2 PROTEIN; 1.
DR   Pfam; PF07986; TBCC; 1.
DR   PIRSF; PIRSF037947; Protein_XRP2; 1.
DR   SMART; SM00673; CARP; 2.
DR   SUPFAM; SSF69340; C-terminal domain of adenylylcyclase associated protein; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRNR:PIRNR037947};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468,
KW   ECO:0000256|PIRNR:PIRNR037947};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR037947}; Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073}.
FT   DOMAIN          24..179
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         98..99
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037947-1"
FT   BINDING         115..118
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037947-1"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037947-2"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037947-2"
SQ   SEQUENCE   343 AA;  39020 MW;  180E7BF9D7373B66 CRC64;
     MGCFFSKRRK ADKESRPENE EERPKQYSWD QREKVDPKDY MFSGLKDETV GRLPGTVAGQ
     QFLIQDCENC NIYIFDHSAT VTIDDCTNCI IFLGPVKGSV FFRNCRDCKC TLACQQFRVR
     DCRKLEVFLC CATQPIIESS SNIKFGCFQW YYPELAFQFK DAGLSIFNNT WSNIHDFTPV
     SGELNWSLLP EDAVVQDYVP IPTTEELKAV RVSTEANRSI VPISRGQRQK SSDESCLVVL
     FAGDYSIANA RKLIDEMVGK GFFLVQTKEV SMKAEDAQRV FREKAPDFLP LLNKGTFWMI
     GILFNAGCKL VSINAVFDNT FVVTVVVART CCDPLHESTP EYM
//
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