ID   RIC1_DANRE              Reviewed;        1321 AA.
AC   A0A2R8QPS5;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 1.
DT   03-AUG-2022, entry version 18.
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 1;
GN   Name=ric1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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 be thereby 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 (By
CC       similarity). It is a regulator of procollagen transport and secretion,
CC       and is required for correct cartilage morphogenesis and development of
CC       the craniofacial skeleton (PubMed:31932796).
CC       {ECO:0000250|UniProtKB:Q4ADV7, ECO:0000269|PubMed:31932796}.
CC   -!- SUBUNIT: Forms a complex with rgp1; the interaction enhances rab6a
CC       GTPase activity. {ECO:0000250|UniProtKB:Q4ADV7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q4ADV7}. Membrane
CC       {ECO:0000250|UniProtKB:Q4ADV7}.
CC   -!- DISRUPTION PHENOTYPE: ric1-null mutant larvae show micrognathia, small
CC       head, shortened trunk, and short, kinked pectoral fins. Craniofacial
CC       cartilage elements and newly formed ossification centers are present
CC       but they are malformed and smaller than in wild-type controls.
CC       Chondrocytes of mutant fishes retain procollagen II intracellularly in
CC       large inclusions. {ECO:0000269|PubMed:31932796}.
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DR   AlphaFoldDB; A0A2R8QPS5; -.
DR   STRING; 7955.ENSDARP00000076812; -.
DR   Ensembl; ENSDART00000177459; ENSDARP00000157676; ENSDARG00000108298.
DR   GeneTree; ENSGT00390000002955; -.
DR   Reactome; R-DRE-6811438; Intra-Golgi traffic.
DR   PRO; PR:A0A2R8QPS5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   Bgee; ENSDARG00000108298; Expressed in early embryo and 20 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; IBA:GO_Central.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
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; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..1321
FT                   /note="Guanine nucleotide exchange factor subunit RIC1"
FT                   /id="PRO_0000450286"
FT   REPEAT          63..102
FT                   /note="WD 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q4ADV7"
FT   REPEAT          303..342
FT                   /note="WD 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q4ADV7"
FT   REGION          945..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..964
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1321 AA;  148264 MW;  FAA050339C31580D CRC64;
     MYFLSGWPRR LLCPLRSDER PFRIEPSAQR FYLAVLSETQ ISIWFSRPSV LIVSYIESGK
     AAAQFGFYQQ VEWKPDDSMI AVAAANGYVL LFDIIGGLDD KYLYEPVYPK GSARVKVTPG
     YKEEQCAPAL TLEMKKPVDL EAPISCLQSL AEDLLVATAD GFLHMLHWDS VSNGRRAVNL
     CTIPFSLDLQ SSRGGPCLDL DGVYIRDLEY CATLDGFAVV FDDGRIGFIT PTANRLATDQ
     LQGVWAADVT DGTCVAVNNK YRLMAFGCTS GSVLVYMIDS STGCMQLSHK LELTPKHYPD
     IWNKTGPVKM IRWSPDCSVA MVTWECGGLS LWSVFGAHLI CTLGEDFAYR SDGTKKDPLK
     ISSMSWGVEG YHLWVIRSSD STVTEEKQEK LQQNTILQFQ FIKSSNQEQV LLQGEDRLYV
     TCGDPTQTQT PGQCRSSSTA PLSQGLSTLL GHKHWQVVQI HSTYLETNWP IRVRNAHDRR
     RVTLIMLMLT DHYAVCEQNM TVTGGLAWWN DFVVVACYNF IDRQEELRLY VRSANLDNAF
     ASITKLHADT LLLNVFRNMV ILFRADCSIC LYSIERRHDG PSPSASVELL QEVSMSRYIP
     HPGLVVSVTL TSVRTESGIT LKAPQQACSA ESILLNLAGQ LIMLQRDRSG PQVREKDAPA
     NHSKLLPFCP PVVLAQCVES VWTSSRSNRK KRHLMEALWL SCGEAGMKVW LPLFPRDHRK
     PHSFLSRRIM LPFHINIYPL TVLFEDALIL GASNETVLFD GLSSSAEPLE ALFPYCTVER
     TSQIYLHHIL RQLLVRNLGE QALMLAQSCA SLPYFPHVLE LMVHVVLEEE ATSREPIPDP
     LLPTVAKFVT EFPLFLQTIV HCARKTEYAL WNYLFAAVGN PKDLFEECLM AQDLDTAASY
     LIILQNMEVP AVSRQHATLL FNTALEQGKW DLCRHMIRFL KAIGSGESET PPTTPTTQEQ
     SPSSGFEFFR NRSISLSQSA DSIAAGKFNL QKTMSMPTGP SSKSDSAENL YIDVMLWRHA
     RRLLEQVRLR DLGCFSAQLG FELIGWLCRE RTRVARVDDF VTALKCLHKD FLWPFPVIPA
     CTISSPLKNG RCRPVLSSRL LKSQSADSLL NSEMDTTPPQ VSTANHRWLD GLGAVSKELD
     SASSHGGPQT QEAFLSPLIS KGEQVSDIYL YFHPSIHPIH LSIHPSIVLF IHSSFYPSIH
     PSFHPSIHPS IVLSIHPSIH RSIYLSIHPS IHPSIHPSIV LFIHPSIVPS IHPSIHPSIH
     PLFYLSIHPS IHPSIHRSIH PSIHRSIYPS IHRSIHPSIH RSIYPFIHPS IVLSIHPSIH
     C