ID A0A452SLJ6_URSAM Unreviewed; 310 AA.
AC A0A452SLJ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Protein XRP2 {ECO:0000256|ARBA:ARBA00015771, ECO:0000256|PIRNR:PIRNR037947};
GN Name=RP2 {ECO:0000313|Ensembl:ENSUAMP00000033526.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000033526.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000033526.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSUAMT00000037341.1; ENSUAMP00000033524.1; ENSUAMG00000025546.1.
DR Ensembl; ENSUAMT00000037343.1; ENSUAMP00000033526.1; ENSUAMG00000025546.1.
DR GeneTree; ENSGT00940000158262; -.
DR Proteomes; UP000291022; 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 SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 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:UP000291022}.
FT DOMAIN 1..139
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT BINDING 58..59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR037947-1"
FT BINDING 75..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR037947-1"
SQ SEQUENCE 310 AA; 34463 MW; 77B88E7B4853DED4 CRC64;
MFSGLKDETV GRLPGQVAGQ QFLIQDCENC NIYIFDHSAT ITIDDCTNCV IFLGPVKGSV
FFRNCRDCKC TLACQQFRVR DCRKLEVFLC CATQPIIESS TNIKFGCFQW YYPELAFQFK
DAGLSIFNNT WSNVHDFTPV SGELNWSLLP EDAVVQDHVP LPTTEELKAV RVATEANRSI
VPVSRGQRPK SSDESCLVVL FAGDYTIANA RKLIDEMVGK GFFLVQTKEV SMKAEDAQRV
FGEKAPDFLP LLNKGPVIAL EFNGDGAVEG CQLIVNEIFN GTKMFVSESK ETASGDVDSF
YNFADIQMGI
//
