ID   XRP2_XENLA              Reviewed;         353 AA.
AC   Q8AVX5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Protein XRP2;
GN   Name=rp2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2002) 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. Acts as a GTPase-activating protein. May act as
CC       guanine nucleotide dissociation inhibitor towards ADP-ribosylation
CC       factor-like proteins (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75695};
CC       Lipid-anchor {ECO:0000250|UniProtKB:O75695}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:O75695}. Note=Detected predominantly at the
CC       plasma membrane of rod and cone photoreceptors. Not detected in the
CC       nucleus. {ECO:0000250|UniProtKB:O75695}.
CC   -!- PTM: Myristoylated on Gly-2; which may be required for membrane
CC       targeting. {ECO:0000305}.
CC   -!- PTM: Palmitoylated on Cys-3; which may be required for plasma membrane
CC       targeting. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000305}.
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DR   EMBL; BC041222; AAH41222.1; -; mRNA.
DR   RefSeq; NP_001080087.1; NM_001086618.1.
DR   AlphaFoldDB; Q8AVX5; -.
DR   SMR; Q8AVX5; -.
DR   DNASU; 379779; -.
DR   GeneID; 379779; -.
DR   KEGG; xla:379779; -.
DR   CTD; 379779; -.
DR   Xenbase; XB-GENE-961413; rp2.S.
DR   OMA; DYMLTGL; -.
DR   OrthoDB; 1458550at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 379779; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR   Gene3D; 2.160.20.70; -; 1.
DR   Gene3D; 3.30.70.141; -; 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; PTHR15440; 1.
DR   Pfam; PF07986; TBCC; 1.
DR   PIRSF; PIRSF037947; Protein_XRP2; 1.
DR   SMART; SM00673; CARP; 2.
DR   SUPFAM; SSF54919; SSF54919; 1.
DR   SUPFAM; SSF69340; SSF69340; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; GTPase activation; Lipoprotein; Membrane;
KW   Myristate; Nucleotide-binding; Palmitate; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..353
FT                   /note="Protein XRP2"
FT                   /id="PRO_0000235806"
FT   DOMAIN          27..182
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101..102
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         118..121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   353 AA;  39967 MW;  86E2BC5306A0E816 CRC64;
     MGCFFSKKAK RKRNSEEEQP QQDGEEPKQY SWDKREKVDP KDYMFTGLKD QTVGKLPDKV
     AGQQFVIQEC ENCNIYIFDH SATITIDDCT NCRIFLGPVK GSVFFRDCKD CKCVVACQQF
     RTRDCRRMDV FLCCSTQPII ESSTSMKFGC FQYYYPELAL QFKEAGLSIL NNTWSNIHDF
     TPVAGETNWS LLPPDAVIQD FIPLPDSDEL KCVRVSADVH KSIIPVTWGQ RLKKSDESCL
     VVFFAGDYTT ANARKMIDEM VGKGLSLIQT KEVAMKIEDA KRVFQDNITD LICLLEKGPV
     VALEFNGEGA VDSCQTVINN TFSGTKVFVS ESKESASRDV DNFYNFADMQ MGM