ID   RIC1_SCHPO              Reviewed;        1052 AA.
AC   O42656; Q9US18;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Guanine nucleotide exchange factor subunit ric1 {ECO:0000305};
DE   AltName: Full=Protein ric1 {ECO:0000250|UniProtKB:P40395};
GN   Name=ric1; ORFNames=SPAC1851.04c, SPAC27D7.01c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-293, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Probable component of a guanine nucleotide exchange factor
CC       (GEF) that may be required for efficient fusion of endosome-derived
CC       vesicles with the Golgi. {ECO:0000250|UniProtKB:P40395}.
CC   -!- SUBUNIT: Component of a guanine nucleotide exchange factor (GEF)
CC       complex. {ECO:0000250|UniProtKB:P40395}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RIC1 family. {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; CU329670; CAB62430.1; -; Genomic_DNA.
DR   PIR; T50127; T50127.
DR   RefSeq; NP_594607.2; NM_001020035.2.
DR   AlphaFoldDB; O42656; -.
DR   BioGRID; 278968; 4.
DR   STRING; 4896.SPAC1851.04c.1; -.
DR   iPTMnet; O42656; -.
DR   MaxQB; O42656; -.
DR   PaxDb; O42656; -.
DR   PRIDE; O42656; -.
DR   EnsemblFungi; SPAC1851.04c.1; SPAC1851.04c.1:pep; SPAC1851.04c.
DR   GeneID; 2542510; -.
DR   KEGG; spo:SPAC1851.04c; -.
DR   PomBase; SPAC1851.04c; ric1.
DR   VEuPathDB; FungiDB:SPAC1851.04c; -.
DR   eggNOG; KOG2006; Eukaryota.
DR   HOGENOM; CLU_002060_1_0_1; -.
DR   InParanoid; O42656; -.
DR   OMA; MVYDRAM; -.
DR   PhylomeDB; O42656; -.
DR   Reactome; R-SPO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   Reactome; R-SPO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:O42656; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; EXP:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:1904515; P:positive regulation of TORC2 signaling; IMP:PomBase.
DR   GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
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; 2.
PE   1: Evidence at protein level;
KW   Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..1052
FT                   /note="Guanine nucleotide exchange factor subunit ric1"
FT                   /id="PRO_0000116843"
FT   TRANSMEM        661..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         293
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1052 AA;  119589 MW;  A0029ECCD47F54FA CRC64;
     MYFLHGTPQR IQLSSRAIQI CRIPKVSFFV VLTETEILIY QIRPLTLISK ITKSQNLFER
     HGKNKKIAVN SEYGIIAVAT EKNYVAVYHF TLNASKPVLT PSPYLTRYDD GPGEIFGPIK
     CEIQYKLAMR YGGGLKCLEI QRDSIVYAAD SAPIIQVSTL ETTDPNKLWK VSSKQYDLRE
     VTWFLDHSSL ISRLYFDVKI DTFFWMSTDG RVYANIGVSS NTNTKSLFGL CVHNPVDLNK
     SDNDKDINED LESKLREKKA TVLSTNARFS LLYVGTADGT VYAYEIRDFG RQYVQTHSFK
     YSASSGKVNH IATTGDGHQV MVGYDDGWAT LSPYLNLCCA SSETEYFNFG LSCGFWDRDS
     SSFYGLGSKN FSSTGEAEGT GLSTPIIAES LKENDEFFAM EKENVDIQYL SQNDNTNDVL
     YSITDSKQFI STIYILPFLK STIVSSVQST LQVCGAQTSD RLYISKSYEF CSSVKNNFGI
     DFWDQVEYPQ PYVASEWPIR YVSIKDDGSL IAIAGLHGLA IYVCSKKTWF LYKDANMEQL
     ISVTCPMIWC SQFLLAGVVC ESNFELHLYK AKGPLDDREN LAKLSFTSTI VTMSVCDEYS
     LVVYTADNFL HHIRFDINEL GRLELDYLTS VNFAPIFTTP SRVRSITLLL PKDLANIQPS
     DLLFYAVLLV LINGKLVLLS LKKQHSKELL YQCSMLAGDV EFYFINGSQE IPSLFHSIWI
     MTGKGLKLWL SFSEILSSVL INTKNLIDGL PKFLNTSKRV SLENFHRLSV EDLRSPSFVY
     KNGVDCNFDN THLAKLIKNV NISEKFQKEC IDLESQGCLL TVLSNYGLLL TAYTQGHKNL
     VNKMEYAHIQ IGVYPFLPEI VRALLLLDKR EQAIDLVKTY GHLHYINFVL EKLLSSSLLT
     YNSSQRDKLL YEVSLLFKDL QEFTTFKIVL GCLRKTEAEY WPMIFKYFGE PKDLMKKCLE
     TEDVKSAAEC LIIWQIHQGS ASCASTFLSI YEMALKIKNW DVCTELSSYL VSLDPEKRLL
     KTALELLDEG PDSKDIRLYD QFNNLMKEVD KY