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 27-MAR-2024, entry version 139. 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}, KIAA1432 GN {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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 35. 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; 9606-ENSP00000416696; -. DR PeptideAtlas; Q4ADV7; -. DR ProteomicsDB; 62090; -. [Q4ADV7-1] DR ProteomicsDB; 62091; -. [Q4ADV7-2] DR ProteomicsDB; 62092; -. [Q4ADV7-3] DR Pumba; Q4ADV7; -. 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 AGR; HGNC:17686; -. 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 Orphanet; 199306; Cleft lip/palate. 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; 121525at2759; -. 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; 386 hits in 1180 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 186 other cell types or tissues. DR ExpressionAtlas; Q4ADV7; baseline and differential. 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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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:SF10; GUANINE NUCLEOTIDE EXCHANGE FACTOR SUBUNIT RIC1; 1. DR PANTHER; PTHR22746; RAB6A-GEF COMPLEX PARTNER PROTEIN 1; 1. DR Pfam; PF07064; RIC1; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR Genevisible; Q4ADV7; HS. 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; FT loss-of-function variant affecting procollagen secretion; FT dbSNP:rs763515150)" 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 FT P-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 //