ID A0A3Q3LVV8_9TELE Unreviewed; 370 AA.
AC A0A3Q3LVV8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Protein XRP2 {ECO:0000256|ARBA:ARBA00015771, ECO:0000256|PIRNR:PIRNR037947};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000018628.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000018628.1}
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 AlphaFoldDB; A0A3Q3LVV8; -.
DR STRING; 205130.ENSMAMP00000018628; -.
DR Ensembl; ENSMAMT00000019111.2; ENSMAMP00000018628.1; ENSMAMG00000012547.2.
DR GeneTree; ENSGT00940000158262; -.
DR InParanoid; A0A3Q3LVV8; -.
DR OrthoDB; 127089at2759; -.
DR Proteomes; UP000261640; Unplaced.
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 GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR GO; GO:0048793; P:pronephros development; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
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:UP000261640}.
FT DOMAIN 43..198
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117..118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|PIRSR:PIRSR037947-1"
FT BINDING 134..137
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 370 AA; 41404 MW; E27AA34FE6AEB2F4 CRC64;
MGCFFSKKSK RKSSEKEDRT PSTAAENTTS NAVPPGNNTA EAPKQYSWDI REKVDPKDYM
LTGLKDVTVG RLPGKLNGQQ FVIQECENCS IYVFDHSATI TIDDCVNCRI VLGPVKGSVF
FRDCKDIKCV VACQQFRTRD CKKMEVFLCC ATQPIIESST GMKFSCFQYF YPELAFHFKD
AGLSIFNNNW SNIHDFTPVS GENNWSLLPE GSSVLDFVPA PDPESDFKSI RISTDPARSI
VPLTKGGRRK DSEESCLFIF FAGEYTTANA RKLIDEVTAK GFELIQTKEV SMRPEDVKRV
FQNNAEDLVE WITKGPVTAL ELNGDGVVEA CKNIANEVFS GTKVFVSDNK STSSRDVDNF
FNFADMQMSM
//
