XRP2_MOUSE
ID XRP2_MOUSE Reviewed; 347 AA.
AC Q9EPK2; Q8BLN8; Q8BVQ8; Q8BZP9;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein XRP2;
GN Name=Rp2; Synonyms=Rp2h;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11371510; DOI=10.1093/hmg/10.11.1177;
RA Schwahn U., Paland N., Techritz S., Lenzner S., Berger W.;
RT "Mutations in the X-linked RP2 gene cause intracellular misrouting and loss
RT of the protein.";
RL Hum. Mol. Genet. 10:1177-1183(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Colon, Diencephalon, Liver tumor, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12417528; DOI=10.1093/hmg/11.24.3065;
RA Grayson C., Bartolini F., Chapple J.P., Willison K.R., Bhamidipati A.,
RA Lewis S.A., Luthert P.J., Hardcastle A.J., Cowan N.J., Cheetham M.E.;
RT "Localization in the human retina of the X-linked retinitis pigmentosa
RT protein RP2, its homologue cofactor C and the RP2 interacting protein
RT Arl3.";
RL Hum. Mol. Genet. 11:3065-3074(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a GTPase-activating protein (GAP) involved in
CC trafficking between the Golgi and the ciliary membrane. Involved in
CC localization of proteins, such as NPHP3, to the cilium membrane by
CC inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or
CC UNC119B). 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 guanine nucleotide dissociation inhibitor
CC towards ADP-ribosylation factor-like proteins.
CC -!- SUBUNIT: Found in a complex with ARL3, RP2 and UNC119 (or UNC119B); RP2
CC induces hydrolysis of GTP ARL3 in the complex, leading to the release
CC of UNC119 (or UNC119B). Interacts with ARL3; interaction is direct and
CC stimulated with the activated GTP-bound form of ARL3 (By similarity).
CC {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}. Cell projection, cilium
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9EPK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EPK2-2; Sequence=VSP_018482;
CC Name=3;
CC IsoId=Q9EPK2-3; Sequence=VSP_018483, VSP_018484;
CC Name=4;
CC IsoId=Q9EPK2-4; Sequence=VSP_018481;
CC -!- TISSUE SPECIFICITY: Retina (at protein level).
CC {ECO:0000269|PubMed:12417528}.
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; AJ303371; CAC21499.1; -; mRNA.
DR EMBL; AK033954; BAC28525.1; -; mRNA.
DR EMBL; AK044002; BAC31734.1; -; mRNA.
DR EMBL; AK050418; BAC34245.1; -; mRNA.
DR EMBL; AK076907; BAC36524.1; -; mRNA.
DR EMBL; AK132713; BAE21316.1; -; mRNA.
DR EMBL; AK162309; BAE36846.1; -; mRNA.
DR EMBL; BC049698; AAH49698.1; -; mRNA.
DR CCDS; CCDS30041.1; -. [Q9EPK2-1]
DR CCDS; CCDS72346.1; -. [Q9EPK2-4]
DR RefSeq; NP_001277572.1; NM_001290643.1. [Q9EPK2-1]
DR RefSeq; NP_001277573.1; NM_001290644.1. [Q9EPK2-4]
DR RefSeq; NP_598430.1; NM_133669.5. [Q9EPK2-1]
DR RefSeq; XP_017173928.1; XM_017318439.1. [Q9EPK2-4]
DR AlphaFoldDB; Q9EPK2; -.
DR SMR; Q9EPK2; -.
DR BioGRID; 202960; 2.
DR IntAct; Q9EPK2; 2.
DR MINT; Q9EPK2; -.
DR STRING; 10090.ENSMUSP00000033372; -.
DR iPTMnet; Q9EPK2; -.
DR PhosphoSitePlus; Q9EPK2; -.
DR SwissPalm; Q9EPK2; -.
DR EPD; Q9EPK2; -.
DR jPOST; Q9EPK2; -.
DR MaxQB; Q9EPK2; -.
DR PaxDb; Q9EPK2; -.
DR PeptideAtlas; Q9EPK2; -.
DR PRIDE; Q9EPK2; -.
DR ProteomicsDB; 300011; -. [Q9EPK2-1]
DR ProteomicsDB; 300012; -. [Q9EPK2-2]
DR ProteomicsDB; 300013; -. [Q9EPK2-3]
DR ProteomicsDB; 300014; -. [Q9EPK2-4]
DR Antibodypedia; 373; 161 antibodies from 26 providers.
DR DNASU; 19889; -.
DR Ensembl; ENSMUST00000033372; ENSMUSP00000033372; ENSMUSG00000060090. [Q9EPK2-1]
DR Ensembl; ENSMUST00000115387; ENSMUSP00000111045; ENSMUSG00000060090. [Q9EPK2-4]
DR Ensembl; ENSMUST00000115391; ENSMUSP00000111049; ENSMUSG00000060090. [Q9EPK2-1]
DR Ensembl; ENSMUST00000133619; ENSMUSP00000138724; ENSMUSG00000060090. [Q9EPK2-3]
DR Ensembl; ENSMUST00000134349; ENSMUSP00000138352; ENSMUSG00000060090. [Q9EPK2-2]
DR GeneID; 19889; -.
DR KEGG; mmu:19889; -.
DR UCSC; uc009ssv.2; mouse. [Q9EPK2-1]
DR CTD; 6102; -.
DR MGI; MGI:1277953; Rp2.
DR VEuPathDB; HostDB:ENSMUSG00000060090; -.
DR eggNOG; KOG2512; Eukaryota.
DR GeneTree; ENSGT00940000158262; -.
DR HOGENOM; CLU_056119_0_0_1; -.
DR InParanoid; Q9EPK2; -.
DR OMA; DYMLTGL; -.
DR OrthoDB; 1458550at2759; -.
DR PhylomeDB; Q9EPK2; -.
DR TreeFam; TF105832; -.
DR Reactome; R-MMU-5624138; Trafficking of myristoylated proteins to the cilium.
DR BioGRID-ORCS; 19889; 2 hits in 41 CRISPR screens.
DR PRO; PR:Q9EPK2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9EPK2; protein.
DR Bgee; ENSMUSG00000060090; Expressed in olfactory epithelium and 227 other tissues.
DR Genevisible; Q9EPK2; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1990075; C:periciliary membrane compartment; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cilium; GTP-binding;
KW GTPase activation; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
KW Palmitate; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75695"
FT CHAIN 2..347
FT /note="Protein XRP2"
FT /id="PRO_0000235804"
FT DOMAIN 21..176
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95..96
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 112..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
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"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018481"
FT VAR_SEQ 321..347
FT /note="MFVSEKKETASGDVDSFYNFAEIQMGI -> VLGMEPRTLLGKKTECQKVWM
FT ACQAQTIVTELQCQKRALDPLNCGYKWL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018482"
FT VAR_SEQ 321..322
FT /note="MF -> IP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018483"
FT VAR_SEQ 323..347
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018484"
SQ SEQUENCE 347 AA; 39377 MW; B5F0A3C4C0F4913B CRC64;
MGCCFTKRRK SEKAEGEEEQ PKLYSWDQRE KVDPKDYMFS GLKDETVGRL PGKVAGQQFV
IQDCENCNIY IFDHSATITI DDCTNCVIFL GPVKGSVFFR NCRDCKCTLA CQQFRVRDCR
KLEVFLCCAT QPIIESSTNI KFGCFQWYYP ELAAQFKDAG LSIFNNIWSH VHDFTPVSGE
LNWSLLPENA VVQDYVPIPM TEEFKAVRIS TEANRSIVPV SRGQRQKYSD ESCLVVLFAD
DYTTANARKL IDEMVGKGFS LVQTKEMSMK TEDAQRVFQE KASDFLLLLN KGPVIALEFN
GDDAVQECHL IVNGMFNGTK MFVSEKKETA SGDVDSFYNF AEIQMGI
