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RPGRH_CAEEL
ID   RPGRH_CAEEL             Reviewed;        1386 AA.
AC   Q5DX34;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=X-linked retinitis pigmentosa GTPase regulator homolog;
DE   AltName: Full=Gut granule loss protein 4;
GN   Name=glo-4; ORFNames=F07C3.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 99-109; 211-222; 364-370; 390-399; 404-431; 468-477;
RP   541-552; 585-598; 601-612; 859-868; 915-927 AND 1308-1317, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Bienvenut W.V.;
RL   Submitted (FEB-2005) to UniProtKB.
RN   [3] {ECO:0000305}
RP   IDENTIFICATION.
RX   PubMed=10767309; DOI=10.1093/hmg/9.6.869;
RA   Culetto E., Sattelle D.B.;
RT   "A role for Caenorhabditis elegans in understanding the function and
RT   interactions of human disease genes.";
RL   Hum. Mol. Genet. 9:869-877(2000).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15843430; DOI=10.1091/mbc.e05-01-0060;
RA   Hermann G.J., Schroeder L.K., Hieb C.A., Kershner A.M., Rabbitts B.M.,
RA   Fonarev P., Grant B.D., Priess J.R.;
RT   "Genetic analysis of lysosomal trafficking in Caenorhabditis elegans.";
RL   Mol. Biol. Cell 16:3273-3288(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=21968191; DOI=10.1534/genetics.111.134791;
RA   Tulgren E.D., Baker S.T., Rapp L., Gurney A.M., Grill B.;
RT   "PPM-1, a PP2Calpha/beta phosphatase, regulates axon termination and
RT   synapse formation in Caenorhabditis elegans.";
RL   Genetics 189:1297-1307(2011).
CC   -!- FUNCTION: Could be a guanine-nucleotide releasing factor for glo-1
CC       (PubMed:15843430). May play a role in gut granule biogenesis
CC       (PubMed:15843430). Regulates axon termination in PLM and ALM neurons
CC       (PubMed:21968191). {ECO:0000269|PubMed:15843430,
CC       ECO:0000269|PubMed:21968191}.
CC   -!- DISRUPTION PHENOTYPE: Worms exhibit lack of intestinal gut granules.
CC       {ECO:0000269|PubMed:15843430}.
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DR   EMBL; FO081074; CCD68933.2; -; Genomic_DNA.
DR   PIR; T28816; T28816.
DR   PIR; T28817; T28817.
DR   RefSeq; NP_505392.3; NM_072991.4.
DR   AlphaFoldDB; Q5DX34; -.
DR   SMR; Q5DX34; -.
DR   BioGRID; 44344; 1.
DR   STRING; 6239.F07C3.4; -.
DR   EPD; Q5DX34; -.
DR   PaxDb; Q5DX34; -.
DR   PeptideAtlas; Q5DX34; -.
DR   PRIDE; Q5DX34; -.
DR   EnsemblMetazoa; F07C3.4.1; F07C3.4.1; WBGene00017195.
DR   GeneID; 179306; -.
DR   KEGG; cel:CELE_F07C3.4; -.
DR   UCSC; F07C3.4; c. elegans.
DR   CTD; 179306; -.
DR   WormBase; F07C3.4; CE47730; WBGene00017195; glo-4.
DR   eggNOG; KOG1426; Eukaryota.
DR   HOGENOM; CLU_260451_0_0_1; -.
DR   InParanoid; Q5DX34; -.
DR   OMA; MANHEDV; -.
DR   OrthoDB; 1062377at2759; -.
DR   PRO; PR:Q5DX34; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00017195; Expressed in material anatomical entity and 5 other tissues.
DR   GO; GO:0030424; C:axon; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IDA:WormBase.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030517; P:negative regulation of axon extension; IGI:WormBase.
DR   Gene3D; 2.130.10.30; -; 2.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   Pfam; PF00415; RCC1; 3.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SUPFAM; SSF50985; SSF50985; 1.
DR   PROSITE; PS00626; RCC1_2; 3.
DR   PROSITE; PS50012; RCC1_3; 4.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Guanine-nucleotide releasing factor;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1386
FT                   /note="X-linked retinitis pigmentosa GTPase regulator
FT                   homolog"
FT                   /id="PRO_0000206640"
FT   REPEAT          737..787
FT                   /note="RCC1 1"
FT   REPEAT          788..838
FT                   /note="RCC1 2"
FT   REPEAT          839..891
FT                   /note="RCC1 3"
FT   REPEAT          893..943
FT                   /note="RCC1 4"
FT   REPEAT          1034..1085
FT                   /note="RCC1 5"
FT   REPEAT          1087..1139
FT                   /note="RCC1 6"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          972..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        973..993
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1386 AA;  152893 MW;  16C87EDC2151E89B CRC64;
     MFFKRSTNSR KTSANSSSDT STSSESLLLP LLNNTKAGAR SQKGSVHRQS GKKARRKMME
     NPYVCSLELD ELSADDSIID YSVFSDDSFL LILLLTSKGD VQAYLETSRD TKPRKNVVNI
     KTACSLNVSP VTVCIGSQAA FAIFGLADGN LLVTPIRLLI DVTWGGSSWA TTTVIDLSLP
     TVDPCLATPT CTKCFVSNFP PCTMAVVANK AGNILLVDLH LRKCVSELKA PQSLHQIDIL
     LDENSIELLV TGFTGAQWII PIERSGKGFR EVLTTCVPSD LTVLEPATMQ FFAADSCGVV
     ALDTTESIVE VYNTFHSLAH SSKRTFKVPP ETWMVHAGDN MLFTVSNDNE IRSALHFGFM
     SSRLEYTLVR TSTNWRPLGI VAMPSRPHKL AGIFVVNERG LVRVEQSTAL NLTKIASEFF
     FRLSPLQLNS KSVAQVANAC RIDTAEFQSA LIPNLLSTRK NRQLTNKELS QIYSIAKAIN
     LSMSDLLKAF ENESIGEQLL PEVLNTIQTN PAKHDNLMQR VVEMFVKRSL SAEGNMDKIR
     EYDAELSNFL ARHEHLHKGS VDCAKAGMWK CTQTLVRRDV HETKSIDTST EVLLYIIKNR
     LQIWNEANST DRLQIMSLVC HLDWSKLADA DGARVCAILS AWQRDISLPS YHEMCLRIAI
     TNSDRFPRPC QILSLVSSIH ILSEKKISNH ANLPNFLPLA GGNNCGATIT EDDRLMIWGN
     FTNAQQRMEM PQMNAKSKRS DSVTNGAPTL PPPAPKPEQH LPRVLEYPGG RPRAIACGAE
     HILVLSSSGQ LSAWGGNRFG QCGVGHSFRI ANLHQVDGDW PAIEKIACGQ FHSAFICSDG
     SLWTFGWGVW GQLGHGGRNN SNQLVPTRVN GLICKVTQIA CGRAHTVVLT DTGRVLVCGS
     GSYGQMGVDD DIKKVFAFTP LPLGPLRVRD IATHYYHSIC ITEDNRVFEW GRNPQELKMR
     MFVMKKIRSA QLKNTEDPSS PSPSTNGSTP RVNLNLPAEI PREDLGLREV KHFLDGNIVS
     VACGLSHSAL ITSEGTLYTW GKGLDYQLGH GNKNERMEPH QVFEPNGAKW VNVSLGNNHT
     IASTDDGSVF AWGKNDFGQC GVLTKKNGNS ADVTKKFFFQ ARDGRRFMPN VDESQFVQKP
     GLIPDVRVRN LNEDGNEGVD KEEIVDRLKA SDVNVVQAVS KHLYSPIEGK CNGSIIEDEP
     RNGKIQKQNK YDGEDGPLCT TTALVHLIAG DVKRAIRMIE WLKTDSSTCE KSLMVLSSLV
     WEVMANHEDV QSREALSAAF RHVPMSDSMR KGKQIAQLWP AVWNDERVQS SLSIDEKIAM
     LDGFTSASKP VSCPTIPSSS LEVSSKIRVY AQCAHAEPAA VGSPPECSTC LDEWTEKVRH
     TLGTQL
 
 
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