RIC1_HUMAN
ID RIC1_HUMAN Reviewed; 1423 AA.
AC Q4ADV7; B2RN24; B7ZM67; G5E932; Q4VXJ8; Q4VXJ9; Q76MT5; Q8N6E0; Q8TEH4;
AC Q9H0A5; Q9H9S1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Guanine nucleotide exchange factor subunit RIC1 {ECO:0000305};
DE AltName: Full=Connexin-43-interacting protein of 150 kDa {ECO:0000303|PubMed:16112082};
DE AltName: Full=Protein RIC1 homolog {ECO:0000250|UniProtKB:P40395};
DE AltName: Full=RAB6A-GEF complex partner protein 1 {ECO:0000312|HGNC:HGNC:17686};
GN Name=RIC1 {ECO:0000312|HGNC:HGNC:17686};
GN Synonyms=CIP150 {ECO:0000303|PubMed:16112082},
GN KIAA1432 {ECO:0000312|EMBL:BAA92670.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-1423 (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-1423 (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH GJA1.
RC TISSUE=Placenta;
RX PubMed=16112082; DOI=10.1016/j.bbrc.2005.08.019;
RA Akiyama M., Ishida N., Ogawa T., Yogo K., Takeya T.;
RT "Molecular cloning and functional analysis of a novel Cx43 partner protein
RT CIP150.";
RL Biochem. Biophys. Res. Commun. 335:1264-1271(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-1423 (ISOFORMS 1 AND 3).
RC TISSUE=Bone marrow;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 531-1423 (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 628-1423 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [8]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 656-1423.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-996, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RGP1; RAB33B AND
RP RAB6A.
RX PubMed=23091056; DOI=10.1074/jbc.m112.414565;
RA Pusapati G.V., Luchetti G., Pfeffer S.R.;
RT "Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late
RT Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase.";
RL J. Biol. Chem. 287:42129-42137(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-992; SER-1015; SER-1017;
RP SER-1019 AND SER-1037, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP VARIANT CATIFA PRO-1265, AND INVOLVEMENT IN CATIFA.
RX PubMed=27878435; DOI=10.1007/s00439-016-1747-6;
RA Patel N., Anand D., Monies D., Maddirevula S., Khan A.O., Algoufi T.,
RA Alowain M., Faqeih E., Alshammari M., Qudair A., Alsharif H., Aljubran F.,
RA Alsaif H.S., Ibrahim N., Abdulwahab F.M., Hashem M., Alsedairy H.,
RA Aldahmesh M.A., Lachke S.A., Alkuraya F.S.;
RT "Novel phenotypes and loci identified through clinical genomics approaches
RT to pediatric cataract.";
RL Hum. Genet. 136:205-225(2017).
RN [18]
RP VARIANTS CATIFA PRO-1265 AND 1266-TYR--SER-1423 DEL, CHARACTERIZATION OF
RP VARIANTS CATIFA PRO-1265 AND 1266-TYR--SER-1423 DEL, INVOLVEMENT IN CATIFA,
RP AND FUNCTION.
RX PubMed=31932796; DOI=10.1038/s41591-019-0705-y;
RA Unlu G., Qi X., Gamazon E.R., Melville D.B., Patel N., Rushing A.R.,
RA Hashem M., Al-Faifi A., Chen R., Li B., Cox N.J., Alkuraya F.S.,
RA Knapik E.W.;
RT "Phenome-based approach identifies RIC1-linked Mendelian syndrome through
RT zebrafish models, biobank associations and clinical studies.";
RL Nat. Med. 26:98-109(2020).
CC -!- FUNCTION: The RIC1-RGP1 complex acts as a guanine nucleotide exchange
CC factor (GEF), which activates RAB6A by exchanging bound GDP for free
CC GTP, and may thereby be required for efficient fusion of endosome-
CC derived vesicles with the Golgi compartment (PubMed:23091056). The
CC RIC1-RGP1 complex participates in the recycling of mannose-6-phosphate
CC receptors (PubMed:23091056). Required for phosphorylation and
CC localization of GJA1 (PubMed:16112082). Is a regulator of procollagen
CC transport and secretion, and is required for correct cartilage
CC morphogenesis and development of the craniofacial skeleton
CC (PubMed:31932796). {ECO:0000269|PubMed:16112082,
CC ECO:0000269|PubMed:23091056, ECO:0000269|PubMed:31932796}.
CC -!- SUBUNIT: Forms a complex with RGP1; the interaction enhances RAB6A
CC GTPase activity (PubMed:16112082). Interacts (via central domain) with
CC RGP1 (PubMed:16112082). Interacts with RAB6A; the interaction is direct
CC with a preference for RAB6A-GDP (PubMed:16112082). Interacts (via C-
CC terminus domain) with RAB33B; the interaction is direct with a
CC preference for RAB33B-GTP (PubMed:16112082). Interacts with GJA1
CC (PubMed:23091056). {ECO:0000269|PubMed:16112082,
CC ECO:0000269|PubMed:23091056}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23091056}.
CC Membrane {ECO:0000269|PubMed:23091056}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q4ADV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4ADV7-2; Sequence=VSP_031706, VSP_031707;
CC Name=3;
CC IsoId=Q4ADV7-3; Sequence=VSP_042408;
CC -!- TISSUE SPECIFICITY: Present in kidney and various cell lines (at
CC protein level). Widely expressed at low level.
CC {ECO:0000269|PubMed:10718198, ECO:0000269|PubMed:16112082}.
CC -!- DISEASE: CATIFA syndrome (CATIFA) [MIM:618761]: An autosomal recessive
CC disorder characterized by global developmental delay, intellectual
CC disability, and behavioral abnormalities with mild to severe attention-
CC deficit hyperactivity disorder. Motor, speech and cognitive deficits
CC range from mild to severe. Patients show craniofacial dysmorphism
CC including elongated face, short, broad upturned nose with anteverted
CC nares and long philtrum. Additional clinical features are cleft
CC lip/palate, tooth abnormalities, and visual impairment due to cataract,
CC strabismus and poor visual tracking. {ECO:0000269|PubMed:27878435,
CC ECO:0000269|PubMed:31932796}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the RIC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI36617.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI44297.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14150.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE16982.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB66809.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL136980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58760.1; -; Genomic_DNA.
DR EMBL; AL136875; CAB66809.1; ALT_INIT; mRNA.
DR EMBL; AB205401; BAE16982.1; ALT_INIT; mRNA.
DR EMBL; AK022642; BAB14150.1; ALT_INIT; mRNA.
DR EMBL; AB037853; BAA92670.2; -; mRNA.
DR EMBL; AK074150; BAB84976.1; -; mRNA.
DR EMBL; BC030576; AAH30576.1; -; mRNA.
DR EMBL; BC136616; AAI36617.1; ALT_INIT; mRNA.
DR EMBL; BC144296; AAI44297.1; ALT_INIT; mRNA.
DR CCDS; CCDS34982.2; -. [Q4ADV7-1]
DR CCDS; CCDS47949.2; -. [Q4ADV7-2]
DR CCDS; CCDS75811.1; -. [Q4ADV7-3]
DR RefSeq; NP_001129392.2; NM_001135920.2. [Q4ADV7-2]
DR RefSeq; NP_001193486.1; NM_001206557.1. [Q4ADV7-3]
DR RefSeq; NP_065880.2; NM_020829.3. [Q4ADV7-1]
DR AlphaFoldDB; Q4ADV7; -.
DR BioGRID; 121640; 29.
DR IntAct; Q4ADV7; 6.
DR MINT; Q4ADV7; -.
DR STRING; 9606.ENSP00000416696; -.
DR iPTMnet; Q4ADV7; -.
DR PhosphoSitePlus; Q4ADV7; -.
DR BioMuta; RIC1; -.
DR DMDM; 182702127; -.
DR EPD; Q4ADV7; -.
DR jPOST; Q4ADV7; -.
DR MassIVE; Q4ADV7; -.
DR MaxQB; Q4ADV7; -.
DR PaxDb; Q4ADV7; -.
DR PeptideAtlas; Q4ADV7; -.
DR PRIDE; Q4ADV7; -.
DR ProteomicsDB; 62090; -. [Q4ADV7-1]
DR ProteomicsDB; 62091; -. [Q4ADV7-2]
DR ProteomicsDB; 62092; -. [Q4ADV7-3]
DR Antibodypedia; 70521; 28 antibodies from 7 providers.
DR DNASU; 57589; -.
DR Ensembl; ENST00000251879.10; ENSP00000251879.6; ENSG00000107036.12. [Q4ADV7-2]
DR Ensembl; ENST00000414202.7; ENSP00000416696.2; ENSG00000107036.12. [Q4ADV7-1]
DR Ensembl; ENST00000418622.7; ENSP00000402240.4; ENSG00000107036.12. [Q4ADV7-3]
DR GeneID; 57589; -.
DR KEGG; hsa:57589; -.
DR MANE-Select; ENST00000414202.7; ENSP00000416696.2; NM_020829.4; NP_065880.2.
DR UCSC; uc003zjh.5; human. [Q4ADV7-1]
DR CTD; 57589; -.
DR DisGeNET; 57589; -.
DR GeneCards; RIC1; -.
DR HGNC; HGNC:17686; RIC1.
DR HPA; ENSG00000107036; Low tissue specificity.
DR MalaCards; RIC1; -.
DR MIM; 610354; gene.
DR MIM; 618761; phenotype.
DR neXtProt; NX_Q4ADV7; -.
DR OpenTargets; ENSG00000107036; -.
DR PharmGKB; PA134884486; -.
DR VEuPathDB; HostDB:ENSG00000107036; -.
DR eggNOG; KOG2006; Eukaryota.
DR GeneTree; ENSGT00390000002955; -.
DR HOGENOM; CLU_002060_3_1_1; -.
DR InParanoid; Q4ADV7; -.
DR OMA; MVYDRAM; -.
DR OrthoDB; 261419at2759; -.
DR PhylomeDB; Q4ADV7; -.
DR TreeFam; TF105927; -.
DR PathwayCommons; Q4ADV7; -.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q4ADV7; -.
DR BioGRID-ORCS; 57589; 365 hits in 1088 CRISPR screens.
DR ChiTaRS; RIC1; human.
DR GenomeRNAi; 57589; -.
DR Pharos; Q4ADV7; Tbio.
DR PRO; PR:Q4ADV7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q4ADV7; protein.
DR Bgee; ENSG00000107036; Expressed in tibialis anterior and 184 other tissues.
DR ExpressionAtlas; Q4ADV7; baseline and differential.
DR Genevisible; Q4ADV7; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:1904888; P:cranial skeletal system development; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0003330; P:regulation of extracellular matrix constituent secretion; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR009771; Ribosome_control_1.
DR InterPro; IPR040096; Ric1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22746; PTHR22746; 1.
DR Pfam; PF07064; RIC1; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant;
KW Guanine-nucleotide releasing factor; Intellectual disability; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1423
FT /note="Guanine nucleotide exchange factor subunit RIC1"
FT /id="PRO_0000320662"
FT REPEAT 64..103
FT /note="WD 1"
FT REPEAT 304..343
FT /note="WD 2"
FT REGION 437..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 992
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 996
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZJ7"
FT VAR_SEQ 498..534
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042408"
FT VAR_SEQ 1142..1165
FT /note="VGEQLLKSQSADPFLNLEMDAGIS -> GNVDFMSLVQGELYFTPCIYTFCY
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_031706"
FT VAR_SEQ 1166..1423
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_031707"
FT VARIANT 1265
FT /note="R -> P (in CATIFA; patient cells contain normally
FT spliced transcripts corresponding to protein variant P-1265
FT but also transcripts that fail to splice due to intron 24
FT retention leading to a stop codon at position 1266; loss-
FT of-function variant affecting procollagen secretion)"
FT /evidence="ECO:0000269|PubMed:27878435,
FT ECO:0000269|PubMed:31932796"
FT /id="VAR_083541"
FT VARIANT 1266..1423
FT /note="Missing (in CATIFA; patient cells contain
FT transcripts that fail to splice due to intron 24 retention
FT leading to a stop codon at position 1266, but also normally
FT spliced transcripts corresponding to protein variant P-
FT 1265; loss-of-function variant affecting procollagen
FT secretion)"
FT /evidence="ECO:0000269|PubMed:31932796"
FT /id="VAR_083542"
FT CONFLICT 659
FT /note="L -> F (in Ref. 7; BAB84976)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="Q -> E (in Ref. 7; BAB84976)"
FT /evidence="ECO:0000305"
FT CONFLICT 1012
FT /note="R -> G (in Ref. 8; AAH30576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1423 AA; 159301 MW; 9F6F43F572021930 CRC64;
MYFLSGWPKR LLCPLGSPAE APFHVQSDPQ RAFFAVLAAA RLSIWYSRPS VLIVTYKEPA
KSSTQFGSYK QAEWRPDSTM IAVSTANGYI LFFHITSTRG DKYLYEPVYP KGSPQMKGTP
HFKEEQCAPA LNLEMRKILD LQAPIMSLQS VLEDLLVATS DGLLHLIHWE GMTNGRKAIN
LCTVPFSVDL QSSRVGSFLG FTDVHIRDME YCATLDGFAV VFNDGKVGFI TPVSSRFTAE
QLHGVWPQDV VDGTCVAVNN KYRLMAFGCV SGSVQVYTID NSTGAMLLSH KLELTAKQYP
DIWNKTGAVK LMRWSPDNSV VIVTWEYGGL SLWSVFGAQL ICTLGGDFAY RSDGTKKDPL
KINSMSWGAE GYHLWVISGF GSQNTEIESD LRSVVKQPSI LLFQFIKSVL TVNPCMSNQE
QVLLQGEDRL YLNCGEASQT QNPRSSSTHS EHKPSREKSP FADGGLESQG LSTLLGHRHW
HVVQISSTYL ESNWPIRFSA IDKLGQNIAV VGKFGFAHYS LLTKKWKLFG NITQEQNMIV
TGGLAWWNDF MVLACYNIND RQEELRVYLR TSNLDNAFAH VTKAQAETLL LSVFQDMVIV
FRADCSICLY SIERKSDGPN TTAGIQVLQE VSMSRYIPHP FLVVSVTLTS VSTENGITLK
MPQQARGAES IMLNLAGQLI MMQRDRSGPQ IREKDSNPNN QRKLLPFCPP VVLAQSVENV
WTTCRANKQK RHLLEALWLS CGGAGMKVWL PLFPRDHRKP HSFLSQRIML PFHINIYPLA
VLFEDALVLG AVNDTLLYDS LYTRNNAREQ LEVLFPFCVV ERTSQIYLHH ILRQLLVRNL
GEQALLLAQS CATLPYFPHV LELMLHEVLE EEATSREPIP DPLLPTVAKF ITEFPLFLQT
VVHCARKTEY ALWNYLFAAV GNPKDLFEEC LMAQDLDTAA SYLIILQNME VPAVSRQHAT
LLFNTALEQG KWDLCRHMIR FLKAIGSGES ETPPSTPTAQ EPSSSGGFEF FRNRSISLSQ
SAENVPASKF SLQKTLSMPS GPSGKRWSKD SDCAENMYID MMLWRHARRL LEDVRLKDLG
CFAAQLGFEL ISWLCKERTR AARVDNFVIA LKRLHKDFLW PLPIIPASSI SSPFKNGKYR
TVGEQLLKSQ SADPFLNLEM DAGISNIQRS QSWLSNIGPT HHEIDTASSH GPQMQDAFLS
PLSNKGDECS IGSATDLTES SSMVDGDWTM VDENFSTLSL TQSELEHISM ELASKGPHKS
QVQLRYLLHI FMEAGCLDWC IVIGLILRES SIINQILVIT QSSEVDGEML QNIKTGLHAV
DRWASTDCPG YKPFLNIIKP QLQKLSEITE EQVQPDAFQP ITMGKTPEQT SPRAEESRGS
SSHGSIPQGE VGSSNMVSRK EEDTAQAEEE EPFQDGTYDC SVS
