XRP2_DANRE
ID XRP2_DANRE Reviewed; 376 AA.
AC F1QC45; F1D694; Q802Z6;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protein XRP2 {ECO:0000250|UniProtKB:O75695};
GN Name=rp2 {ECO:0000312|ZFIN:ZDB-GENE-040426-2795};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:ADR82635.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21282572; DOI=10.1167/iovs.10-6800;
RA Shu X., Zeng Z., Gautier P., Lennon A., Gakovic M., Cheetham M.E.,
RA Patton E.E., Wright A.F.;
RT "Knockdown of the zebrafish ortholog of the retinitis pigmentosa 2 (RP2)
RT gene results in retinal degeneration.";
RL Invest. Ophthalmol. Vis. Sci. 52:2960-2966(2011).
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000312|EMBL:AAH46879.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB {ECO:0000312|EMBL:AAH46879.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26034134; DOI=10.1093/hmg/ddv197;
RA Liu F., Chen J., Yu S., Raghupathy R.K., Liu X., Qin Y., Li C., Huang M.,
RA Liao S., Wang J., Zou J., Shu X., Tang Z., Liu M.;
RT "Knockout of RP2 decreases GRK1 and rod transducin subunits and leads to
RT photoreceptor degeneration in zebrafish.";
RL Hum. Mol. Genet. 24:4648-4659(2015).
CC -!- FUNCTION: Acts as a GTPase-activating protein (GAP) involved in
CC trafficking between the Golgi and the ciliary membrane (By similarity).
CC Acts as a GTPase-activating protein (GAP) for tubulin in concert with
CC tubulin-specific chaperone C, but does not enhance tubulin
CC heterodimerization (By similarity). In the retina, required for
CC maintenance of rod and cone photoreceptor cells (PubMed:26034134). May
CC have a role in normal retinal localization of the transducins GNB1 and
CC GNAT1, and the rhodopsin kinase GRK1 (PubMed:26034134).
CC {ECO:0000250|UniProtKB:O75695, ECO:0000269|PubMed:26034134}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26034134};
CC Lipid-anchor {ECO:0000250|UniProtKB:O75695}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O75695}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:O75695}.
CC -!- TISSUE SPECIFICITY: In the retina, detected in both rod and cone
CC photoreceptors (at protein level) (PubMed:21282572, PubMed:26034134).
CC Has strongest expression in the retinal outer nuclear layer (ONL) and
CC weaker expression in the outer plexiform layer (OPL) and inner
CC plexiform layer (IPL) (at protein level) (PubMed:26034134). Expressed
CC in all tissues tested (PubMed:21282572). {ECO:0000269|PubMed:21282572,
CC ECO:0000269|PubMed:26034134}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:21282572}.
CC -!- PTM: Myristoylated on Gly-2; which may be required for membrane
CC targeting. {ECO:0000250|UniProtKB:O75695}.
CC -!- PTM: Palmitoylated on Cys-3; which may be required for plasma membrane
CC targeting. {ECO:0000250|UniProtKB:O75695}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile. Early retinal development
CC appears to be grossly normal. Outer segments of rod and cone
CC photoreceptors show progressive degeneration from 2 months of age, with
CC rod cells more severely affected in the early stages.
CC {ECO:0000269|PubMed:26034134}.
CC -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46879.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAI64845.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin at the N terminus.; Evidence={ECO:0000305};
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DR EMBL; HQ641392; ADR82635.1; -; mRNA.
DR EMBL; BX322552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046879; AAH46879.1; ALT_FRAME; mRNA.
DR EMBL; BC164845; AAI64845.1; ALT_FRAME; mRNA.
DR RefSeq; NP_998611.1; NM_213446.1.
DR RefSeq; XP_005166034.1; XM_005165977.1.
DR RefSeq; XP_005166035.1; XM_005165978.1.
DR AlphaFoldDB; F1QC45; -.
DR SMR; F1QC45; -.
DR STRING; 7955.ENSDARP00000120363; -.
DR PaxDb; F1QC45; -.
DR Ensembl; ENSDART00000136920; ENSDARP00000120363; ENSDARG00000044339.
DR Ensembl; ENSDART00000182707; ENSDARP00000155269; ENSDARG00000044339.
DR GeneID; 406755; -.
DR KEGG; dre:406755; -.
DR CTD; 6102; -.
DR ZFIN; ZDB-GENE-040426-2795; rp2.
DR eggNOG; KOG2512; Eukaryota.
DR GeneTree; ENSGT00940000158262; -.
DR HOGENOM; CLU_056119_0_0_1; -.
DR InParanoid; F1QC45; -.
DR OMA; DYMLTGL; -.
DR OrthoDB; 1458550at2759; -.
DR PhylomeDB; F1QC45; -.
DR TreeFam; TF105832; -.
DR Reactome; R-DRE-5624138; Trafficking of myristoylated proteins to the cilium.
DR PRO; PR:F1QC45; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000044339; Expressed in cleaving embryo and 46 other tissues.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:1990075; C:periciliary membrane compartment; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0042461; P:photoreceptor cell development; IMP:ZFIN.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:ZFIN.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:ZFIN.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0048793; P:pronephros development; IMP:ZFIN.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
DR GO; GO:0010842; P:retina layer formation; IMP:ZFIN.
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; IPR034907; NDK-like_dom.
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; PF00334; NDK; 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 1: Evidence at protein level;
KW Cell membrane; Cell projection; GTP-binding; GTPase activation;
KW Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75695"
FT CHAIN 2..376
FT /note="Protein XRP2"
FT /id="PRO_0000437371"
FT DOMAIN 49..204
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O75695"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O75695"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:O75695"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O75695"
FT CONFLICT 349
FT /note="Q -> K (in Ref. 1; ADR82635 and 3; AAH46879/
FT AAI64845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41872 MW; 5D737877C4388345 CRC64;
MGCFFSKKSR RKSPKKDAAL PTGDESATGN DLAETNNTAL GSNSNQEAPK QYSWDKREKV
DPKDFMLTGL KNETVGRLPG KLNGQQFVIQ DCENCNIFVL DHSATITIDD CVNCRIVLGP
VKGSVFFRDC KDIKCVVACQ QFRTRDCKKM DVFLCCATQP IIESSTGMKF GCFQYYYPEL
AFHFKDAGLS IFNNNWSNIH DFTPVSGETN WSLLPEDAVV LDHVPLPDPE SEFKSVRIAT
EAGRSIVPLT KGSRRTESEE SCLFVFFAGD YTTANARKLI DEATAKGFVL IQTKEVSMRP
EDVSRVFQNN AESLTEWITK GPVVALELNG DGVVEACRSF ANEVFNGTQL FVSESKNTSS
RDVDNFFNFA DMQMGL
