ID   RIC3_XENTR              Reviewed;         375 AA.
AC   Q0VFF9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Protein RIC-3;
DE   Flags: Precursor;
GN   Name=ric3;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone which facilitates proper subunit assembly
CC       andsurface trafficking of alpha-7 (CHRNA7) and alpha-8 (CHRNA8)
CC       nicotinic acetylcholine receptors (By similarity). May also promote
CC       functional expression of homomeric serotoninergic 5-HT3 receptors, and
CC       of heteromeric acetylcholine receptors (By similarity).
CC       {ECO:0000250|UniProtKB:Q7Z5B4}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ric-3 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; BC118843; AAI18844.1; -; mRNA.
DR   RefSeq; NP_001072241.1; NM_001078773.1.
DR   AlphaFoldDB; Q0VFF9; -.
DR   SMR; Q0VFF9; -.
DR   STRING; 8364.ENSXETP00000042624; -.
DR   PaxDb; Q0VFF9; -.
DR   DNASU; 779690; -.
DR   Ensembl; ENSXETT00000042624; ENSXETP00000042624; ENSXETG00000019688.
DR   GeneID; 779690; -.
DR   KEGG; xtr:779690; -.
DR   CTD; 79608; -.
DR   Xenbase; XB-GENE-995825; ric3.
DR   eggNOG; ENOG502RZG3; Eukaryota.
DR   HOGENOM; CLU_062635_1_0_1; -.
DR   InParanoid; Q0VFF9; -.
DR   OMA; YPVYDNS; -.
DR   OrthoDB; 1096847at2759; -.
DR   PhylomeDB; Q0VFF9; -.
DR   TreeFam; TF333291; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000019688; Expressed in brain and 10 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISS:UniProtKB.
DR   GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR   InterPro; IPR026160; Ric3.
DR   InterPro; IPR032763; RIC3_N.
DR   PANTHER; PTHR21723; PTHR21723; 1.
DR   Pfam; PF15361; RIC3; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Coiled coil; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..375
FT                   /note="Protein RIC-3"
FT                   /id="PRO_0000302733"
FT   TOPO_DOM        30..90
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..375
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          38..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          135..165
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        305..320
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  40774 MW;  B14D3ED3A9362B54 CRC64;
     MALSAVQKVV LFSCLVLCVS LLLPRAYIAR GKPAAQEGNT GLFQSSGHHP KPTDGRPGGA
     HFPRSHMAEA MSKAKGGTGG GGGGGTRPSL VGQIIPIYGF GILLYILYIL FKLSSKGKST
     KQEPTTQPVA NGNLKRKITD YELSQLQDKL KETEEAMEKI ISRLGPNSER TDNVSSDEET
     DLLQRLKEIT RVMKEGKILD GISPEKEAEE APYMEDWNGY PEETYPVYDP SDCKRTQQTI
     LVDCSALNRP SAEQVAEQMG FDEEDDQENG SGNLAKEPDY KDSVGGDQQA QGTISAQGKV
     VGTGEDIEED EDEDEDPEVI AENAGFISDS CNEEEDPKES FMDLGNEKGP LGATLGSNRD
     ETGTLRKRNT KGIEY