ID A0A2J7QJW7_9NEOP Unreviewed; 331 AA.
AC A0A2J7QJW7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Protein XRP2 {ECO:0000256|ARBA:ARBA00015771, ECO:0000256|PIRNR:PIRNR037947};
GN Name=RP2_1 {ECO:0000313|EMBL:PNF28865.1};
GN ORFNames=B7P43_G04422 {ECO:0000313|EMBL:PNF28865.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF28865.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF28865.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF28865.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNF28865.1}.
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DR EMBL; NEVH01013549; PNF28865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7QJW7; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
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:UP000235965}.
FT DOMAIN 29..177
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT BINDING 96..97
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 331 AA; 37213 MW; 47465D034A1E6D9C CRC64;
MGCLFHKGRQ NASVTGKEDA KLKEYSWDKR NAVNLKDYTV ENTEDGEVLK MPGSVNGQQF
VIQNCKNTCI YIFDHANTVT VDDCINCKII LAAVKGSVFL RDCKECVCVI ACGQFRTRDC
RKMDIFLCCA TQPIIEASSS IHFGCYQLFY TDLEEHFQQA GLSVFNNNWS SIHDFTPIEG
ENNWCLFPDT IRIQDYISLP ASEELQRMNT SLLEEKSVVP HTWGPHKTPT GESCLVAFFS
DGQQVQRAKA FINSLKIENP DCLLLMSKEI QMQQAGAEHV FKTNSYNSVV QRGLVVGLQC
SGPNCIQSCQ KVAVRIATGF EVFTAVWFIA Y
//
