ID   XRP2_CHICK              Reviewed;         357 AA.
AC   Q5ZHN4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Protein XRP2;
GN   Name=RP2; ORFNames=RCJMB04_35c24;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ721100; CAG32759.1; -; mRNA.
DR   RefSeq; NP_001008680.1; NM_001008680.1.
DR   AlphaFoldDB; Q5ZHN4; -.
DR   SMR; Q5ZHN4; -.
DR   STRING; 9031.ENSGALP00000026942; -.
DR   PaxDb; Q5ZHN4; -.
DR   Ensembl; ENSGALT00000026993; ENSGALP00000026942; ENSGALG00000016728.
DR   GeneID; 418675; -.
DR   KEGG; gga:418675; -.
DR   CTD; 6102; -.
DR   VEuPathDB; HostDB:geneid_418675; -.
DR   eggNOG; KOG2512; Eukaryota.
DR   GeneTree; ENSGT00940000158262; -.
DR   HOGENOM; CLU_056119_0_0_1; -.
DR   InParanoid; Q5ZHN4; -.
DR   OMA; DYMLTGL; -.
DR   OrthoDB; 1458550at2759; -.
DR   PhylomeDB; Q5ZHN4; -.
DR   TreeFam; TF105832; -.
DR   Reactome; R-GGA-5624138; Trafficking of myristoylated proteins to the cilium.
DR   PRO; PR:Q5ZHN4; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000016728; Expressed in granulocyte and 14 other tissues.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:1990075; C:periciliary membrane compartment; IBA:GO_Central.
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   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
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..357
FT                   /note="Protein XRP2"
FT                   /id="PRO_0000235805"
FT   DOMAIN          32..186
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         105..106
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..125
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   357 AA;  39723 MW;  0EC08E3C9E1CAF66 CRC64;
     MGCFFSKRRK PAQGGQQQGA SQEPAAGEEK APQYSWDQRA KVDPKDYTFS GLKDETVGRL
     PGRVAGQQFV IQDCENCSIY IFDHSATVTI DDCVNCQIFL GPIKGSVFFR NCKDCKCIVA
     CQQFRTRDCR RLEVFLCCAT QPIIESSTGM KFGCFQYYYP ELALQFKDAG LSIFNNTWSN
     IHDFTPVSGE NNWGLLPENA VVQDYVPLPA SEELKAVRVS TDAMKSIIPI TRGQRQKNSD
     ESCLAVFFAG DYTTANARKL IDEMTGKGFQ LVQTKEVSMK AEDAQRVFQQ CASEFIPLLE
     RGPVVALEFN GDGAVEGCRN TVNDVFNGTK VFVSESKASA SQDVDNFYNF ADMQMGM