RIC1_MOUSE
ID RIC1_MOUSE Reviewed; 1422 AA.
AC Q69ZJ7; A4GZ02; Q3U0Q6; Q3UWK1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Guanine nucleotide exchange factor subunit RIC1 {ECO:0000305};
DE AltName: Full=Protein RIC1 homolog {ECO:0000250|UniProtKB:P40395};
DE AltName: Full=RAB6A-GEF complex partner protein 1 {ECO:0000312|MGI:MGI:1924893};
GN Name=Ric1 {ECO:0000312|MGI:MGI:1924893}; Synonyms=Kiaa1432;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 980-1422 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-1422.
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-991; THR-995 AND SER-1171,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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).
RN [5]
RP TISSUE SPECIFICITY.
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).
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. The RIC1-RGP1 complex
CC participates in the recycling of mannose-6-phosphate receptors.
CC Required for phosphorylation and localization of GJA1. Is a regulator
CC of procollagen transport and secretion, and is required for correct
CC cartilage morphogenesis and development of the craniofacial skeleton.
CC {ECO:0000250|UniProtKB:Q4ADV7}.
CC -!- SUBUNIT: Forms a complex with RGP1; the interaction enhances RAB6A
CC GTPase activity. Interacts (via central domain) with RGP1. Interacts
CC with RAB6A; the interaction is direct with a preference for RAB6A-GDP.
CC Interacts (via C-terminus domain) with RAB33B; the interaction is
CC direct with a preference for RAB33B-GTP. Interacts with GJA1.
CC {ECO:0000250|UniProtKB:Q4ADV7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q4ADV7}. Membrane
CC {ECO:0000250|UniProtKB:Q4ADV7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q69ZJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZJ7-2; Sequence=VSP_031710, VSP_031711;
CC Name=3;
CC IsoId=Q69ZJ7-3; Sequence=VSP_031708, VSP_031709;
CC -!- TISSUE SPECIFICITY: Expressed in the eye lens.
CC {ECO:0000269|PubMed:27878435}.
CC -!- SIMILARITY: Belongs to the RIC1 family. {ECO:0000305}.
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DR EMBL; AK136285; BAE22914.1; -; mRNA.
DR EMBL; AK156653; BAE33795.1; -; mRNA.
DR EMBL; AK048394; BAC33322.1; -; mRNA.
DR EMBL; BC132346; AAI32347.2; -; mRNA.
DR EMBL; AK173171; BAD32449.1; -; mRNA.
DR CCDS; CCDS37951.1; -. [Q69ZJ7-1]
DR AlphaFoldDB; Q69ZJ7; -.
DR IntAct; Q69ZJ7; 1.
DR STRING; 10090.ENSMUSP00000043437; -.
DR iPTMnet; Q69ZJ7; -.
DR PhosphoSitePlus; Q69ZJ7; -.
DR jPOST; Q69ZJ7; -.
DR MaxQB; Q69ZJ7; -.
DR PaxDb; Q69ZJ7; -.
DR PeptideAtlas; Q69ZJ7; -.
DR PRIDE; Q69ZJ7; -.
DR ProteomicsDB; 253126; -. [Q69ZJ7-1]
DR ProteomicsDB; 253127; -. [Q69ZJ7-2]
DR ProteomicsDB; 253128; -. [Q69ZJ7-3]
DR UCSC; uc008hdq.1; mouse. [Q69ZJ7-3]
DR UCSC; uc008hdr.1; mouse. [Q69ZJ7-2]
DR MGI; MGI:1924893; Ric1.
DR eggNOG; KOG2006; Eukaryota.
DR HOGENOM; CLU_1677280_0_0_1; -.
DR InParanoid; Q69ZJ7; -.
DR PhylomeDB; Q69ZJ7; -.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR ChiTaRS; Ric1; mouse.
DR PRO; PR:Q69ZJ7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q69ZJ7; protein.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:1904888; P:cranial skeletal system development; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0003330; P:regulation of extracellular matrix constituent secretion; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR009771; Ribosome_control_1.
DR InterPro; IPR040096; Ric1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22746; PTHR22746; 1.
DR Pfam; PF07064; RIC1; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Guanine-nucleotide releasing factor;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1422
FT /note="Guanine nucleotide exchange factor subunit RIC1"
FT /id="PRO_0000320663"
FT REPEAT 64..103
FT /note="WD 1"
FT REPEAT 304..343
FT /note="WD 2"
FT REGION 442..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 991
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 995
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4ADV7"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4ADV7"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4ADV7"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4ADV7"
FT MOD_RES 1171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 147..157
FT /note="SLQSVLEDLLV -> RYGMLVKFEIF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031708"
FT VAR_SEQ 158..1422
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031709"
FT VAR_SEQ 485..541
FT /note="ISSTYLESNWPIRFSAIDKLGQNIAVAGKFGFAHYSLLTKKWKLFGNITQEQ
FT NMIVT -> VSVHLLTAADSLIRNGSLGRFLIIFIAISLSMLWFLSLPFFFPFDRVYSK
FT SYFFFPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031710"
FT VAR_SEQ 542..1422
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031711"
SQ SEQUENCE 1422 AA; 158829 MW; A04A6F728116351E CRC64;
MYFLSGWPKR LLCAPRSPAE APLHVQSDPR RAFFAVLAPA RLSIWYSRPS VLIVTYKEPA
KSSTQFGSYK QAEWRPDSTM IAVSTANGYI LFFHITSSRG DKYLYEPVYP KGSPQMKGIP
HFKEEHCAPA LNLEMKKILD LQAPIMSLQS VLEDLLVATS DGLLHLIHWE GMTNGRKAIN
LSTVPFSVDL QSSRVGSFLG FADVHIKDME YCATLDGFAV VFNDGKVGFI TPVSSRFTAE
QLHGVWPQDV IDGTCVAVNN KYRLMAFGCA SGCVQVYTID NTTGAMLLSH KLELTAKQYP
DIWNKTGAVK LIRWSPDNSA VIVTWEYGGL SLWSVFGAQL ICTLGGDFAY RSDGTKKDPL
KINSMSWGAE GYHLWVISGL GSQHTQIETD LRSTVKEPSI LLFQFIKSVL TVNPCMSNQE
QVLLQGEDRL YLNCGEASQA QNPKYSSARA ERMPRHEKSP FADGGLEAPG LSTLLGHRHW
HVVQISSTYL ESNWPIRFSA IDKLGQNIAV AGKFGFAHYS LLTKKWKLFG NITQEQNMIV
TGGLAWWDDF MVLACYNLSD CQEELRIYLR TSNLDNAFAH VTKAPMETLL LSVFRDMVVV
FRADCSICLY SIERKSDGSN TTASVQVLQE VSMSRYIPHP FLVVSVTLTS VSTENGISLK
MPQQARDAES IMLNLAGQLI MMQRDRSGPQ IREKDSHPNQ RKLLPFCPPV VLAQSVENVW
TTCRANKQKR HLLEALWLSC GGAGMKVWLP LFPRDHRKPH SFLSQRIMLP FHINIYPLAV
LFEDALVLGA VNDTLLYDSL YTRSSAREQL EVLFPFCVVE RTSQIYLHHI LRQLLVRNLG
EQALLLAQSC AALPYFPHVL ELMLHEVLEE EATSREPIPD PLLPTVAKFI TEFPLFLQTV
VHCARKTEYA LWNYLFAAVG NPKDLFEECL MAQDLDTAAS YLIILQNMEV PAVSRQHATL
LFNTALEQGK WDLCRHMIRF LKAIGSGESE TPPSTPTSQE PSSSGGFEFF RNRSISLSQS
AENVPPGKFG LQKTLSMPTG PSGKRWSKDS ECAENMYIDM MLWRHARRLL EEVRLKDLGC
FAAQLGFELI SWLCKERTRA ARVDNFVVAL KRLHKDFLWP LPIIPASSIS SPFKNGKCRA
VGEQMLKSQS ADPFITPEMD AGISNIQRSQ SWLSNIGPTH RDTDRASSPG PQMQDAFLSP
LSNKGDECSI GSATDLTESS SVVDGDWTMV DENFSTLSLT QSELEHISME LASKGPHKSQ
VQLRYLLHIF MEAGCLDWCV VIGLILRESS VVSQLLGIAQ SSEMDGEMLQ NIKSGLQAVD
RWASTDCPGY KPFLNIIKPQ LQKLSEITEE LVQPDTFQPV TVGKTPEQTS PRAEENRGSC
SHGSISQSEP GSNNVVSRKE EDTTQADEEE PLQDGAYDCS VS
