RPGR_CANLF
ID RPGR_CANLF Reviewed; 1003 AA.
AC Q9N1T2; Q9N1T3; Q9N1T4; Q9N1T5;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=X-linked retinitis pigmentosa GTPase regulator;
DE Flags: Precursor;
GN Name=RPGR;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=10699176; DOI=10.1093/hmg/9.4.531;
RA Zeiss C.J., Ray K., Acland G.M., Aguirre G.D.;
RT "Mapping of X-linked progressive retinal atrophy (XLPRA), the canine
RT homolog of retinitis pigmentosa 3 (RP3).";
RL Hum. Mol. Genet. 9:531-537(2000).
CC -!- FUNCTION: Could be a guanine-nucleotide releasing factor. Plays a role
CC in ciliogenesis. Probably regulates cilia formation by regulating actin
CC stress filaments and cell contractility. May be involved in microtubule
CC organization and regulation of transport in primary cilia. Plays an
CC important role in photoreceptor integrity. May play a critical role in
CC spermatogenesis and in intraflagellar transport processes.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PDE6D (By similarity). Interacts with RPGRIP1
CC (By similarity). Interacts with RPGRIP1L (By similarity). PDE6D,
CC RPGRIP1 and RPGRIP1L may compete for the same binding sites (By
CC similarity). Interacts with NPM1 (By similarity). Interacts with SMC1A
CC and SMC3 (By similarity). Interacts with CEP290 (By similarity).
CC Interacts with WHRN (By similarity). Interacts with SPATA7 (By
CC similarity). {ECO:0000250|UniProtKB:Q92834,
CC ECO:0000250|UniProtKB:Q9R0X5}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q92834}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q9R0X5}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9R0X5}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9R0X5}.
CC Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000250|UniProtKB:Q9R0X5}. Note=In the retinal photoreceptor cell
CC layer, localizes at the connecting cilium (By similarity). Colocalizes
CC with WHRN in the photoreceptor connecting cilium (By similarity).
CC Colocalizes with CEP290 in the photoreceptor connecting cilium (By
CC similarity). Colocalizes with RPGRIP1 in the photoreceptor connecting
CC cilium (By similarity). {ECO:0000250|UniProtKB:Q9R0X5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9N1T2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9N1T2-2; Sequence=VSP_005545, VSP_005546;
CC Name=3;
CC IsoId=Q9N1T2-3; Sequence=VSP_005544;
CC Name=4;
CC IsoId=Q9N1T2-4; Sequence=VSP_005542, VSP_005543;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed exclusively in testis.
CC Isoforms 2, 3 and 4 are widely expressed.
CC {ECO:0000269|PubMed:10699176}.
CC -!- DOMAIN: The RCC1 repeat region mediates interactions with RPGRIP1.
CC {ECO:0000250|UniProtKB:Q92834}.
CC -!- PTM: Prenylated. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in RPGR are the cause of X-linked progressive
CC retinal atrophy (XLPRA) in the Siberian husky dog. XLPRA is a naturally
CC occurring X-linked retinopathy closely resembling X-linked retinitis
CC pigmentosa (XLRP) in humans. {ECO:0000269|PubMed:10699176}.
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DR EMBL; AF148798; AAF73141.1; -; mRNA.
DR EMBL; AF148799; AAF73142.1; -; mRNA.
DR EMBL; AF148800; AAF73143.1; -; mRNA.
DR EMBL; AF148801; AAF73144.1; -; mRNA.
DR RefSeq; NP_001003126.1; NM_001003126.1. [Q9N1T2-1]
DR AlphaFoldDB; Q9N1T2; -.
DR SMR; Q9N1T2; -.
DR STRING; 9615.ENSCAFP00000037530; -.
DR PaxDb; Q9N1T2; -.
DR Ensembl; ENSCAFT00030020227; ENSCAFP00030017637; ENSCAFG00030010611. [Q9N1T2-3]
DR Ensembl; ENSCAFT00040032553; ENSCAFP00040028323; ENSCAFG00040016922. [Q9N1T2-3]
DR GeneID; 403726; -.
DR CTD; 6103; -.
DR InParanoid; Q9N1T2; -.
DR OrthoDB; 1062377at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0042073; P:intraciliary transport; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR Gene3D; 2.130.10.30; -; 1.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR Pfam; PF00415; RCC1; 6.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00626; RCC1_2; 4.
DR PROSITE; PS50012; RCC1_3; 6.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Flagellum;
KW Golgi apparatus; Guanine-nucleotide releasing factor; Lipoprotein;
KW Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat;
KW Retinitis pigmentosa; Sensory transduction; Vision.
FT CHAIN 1..1000
FT /note="X-linked retinitis pigmentosa GTPase regulator"
FT /id="PRO_0000206637"
FT PROPEP 1001..1003
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370843"
FT REPEAT 54..105
FT /note="RCC1 1"
FT REPEAT 106..158
FT /note="RCC1 2"
FT REPEAT 159..208
FT /note="RCC1 3"
FT REPEAT 209..261
FT /note="RCC1 4"
FT REPEAT 262..313
FT /note="RCC1 5"
FT REPEAT 314..367
FT /note="RCC1 6"
FT REGION 460..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..820
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..864
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92834"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92834"
FT MOD_RES 1000
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 1000
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 416
FT /note="E -> V (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005542"
FT VAR_SEQ 417..1003
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005543"
FT VAR_SEQ 527..846
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005544"
FT VAR_SEQ 847..918
FT /note="DHEFSEDEEPEDMAEELDEDLESKKNVPADVASDNSLKKDETTKQEKRAICE
FT YNENPKGNMHYHAKSSSSEV -> VSEGKGKAGGGGEGIQREGDSGVEQRQSEEGQEEE
FT DKRGGEMEGLAKGEKNLEEEEAQEQREREQGHRKKKK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005545"
FT VAR_SEQ 919..1003
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005546"
FT CONFLICT 685
FT /note="V -> M (in Ref. 1; AAF73143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1003 AA; 111097 MW; 43B4BF0D947946AD CRC64;
MGEPEEVMPG SGAVFTFGKT QFAENIPSKF WFRNDVPTFL SCGDEHTAVV TGNNKLYMFG
SNNWGQLGLG SKSTVSKPTC VKALKPEKVK FAACGRNHTL VSTEGGKVYA AGGNNEGQLG
LGDTEERSTF HLISFFTSQR KIKQLSAGSN TSAALTEDGE LFMWGDNSEG QIGLENVTNV
CVPQQVTVGK PISWISCGYY HSAFVTTEGQ LYTFGEPECG KLGLPNQLLV NHRMPQPVPG
IPGKVVQVAC GGGHTVVLTE KAVYTFGLGQ FGQLGLGTFL FETSVPKAIE HIKDQKISFI
ACGENHTALI TDMGLMYTFG DGRHGKLGLG LENSTNQFIP TLCSNFLRFI VQLVSCGGCH
TLVFATPRLG GTEEMELKEI NKSCFSAATS LSLSNLSSGI VLHQTLSARV RRREREKSPD
SFQMTRTLPP IDGIPMPPVC FSPSPIPFYM AASNWSGKMT PEKEGLTQPE PDYFRDNMAK
GKETDNSSAT DSESLGETTD VLNMTHMMSL NSNDKSLKLS PIDKQKKQET IEKLKQHTAH
FGNDDSKGCA SEEMSKTVKE GKAYKQLLAK GIYMTQAAMT MEAFSDEDIG NDSGQPGPRA
DTHAEGVQRK IFSCESKHGL YPPDFKAIAK ESDGGQSQKD PEAEETVSEK ENELAEMAGL
QARRQSEENL RNINMFFDDL PNRDVNIEDE ESKDFVKDSR RNKQDVIFDS ERESIEEPDS
YLEGESESQQ GTTDGFEQPE SVEFSSGEKE DDDEVETDQN LWYSRKFIEQ GHKEETEHIL
SKFMAKYDFK CDHLSEIPEE QEGAEDSEGS GIEEQEVEAN ENVEVPAGKE EKEIEILSDD
LTDRAEDHEF SEDEEPEDMA EELDEDLESK KNVPADVASD NSLKKDETTK QEKRAICEYN
ENPKGNMHYH AKSSSSEVLN DSESTPNKDV KKSKKIFLFK RMSLMSQKSM QSNNEPLPEI
KPIGDQIAFK GNKKDANQNH MGQNHQDTSP PDMERRSKSC TIL
