ID   ARD17_CAEEL             Reviewed;         426 AA.
AC   O45782;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Arrestin domain-containing protein 17 {ECO:0000305};
DE   AltName: Full=Calcineurin-interacting protein 1 {ECO:0000303|PubMed:22300764};
GN   Name=arrd-17 {ECO:0000312|WormBase:T12D8.4};
GN   Synonyms=cnp-1 {ECO:0000312|WormBase:T12D8.4};
GN   ORFNames=T12D8.4 {ECO:0000312|WormBase:T12D8.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH TAX-6, TISSUE SPECIFICITY, PHOSPHORYLATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=22300764; DOI=10.1016/j.jmb.2012.01.012;
RA   Jee C., Choi T.W., Kalichamy K., Yee J.Z., Song H.O., Ji Y.J., Lee J.,
RA   Lee J.I., L'Etoile N.D., Ahnn J., Lee S.K.;
RT   "CNP-1 (ARRD-17), a novel substrate of calcineurin, is critical for
RT   modulation of egg-laying and locomotion in response to food and lysine
RT   sensation in Caenorhabditis elegans.";
RL   J. Mol. Biol. 417:165-178(2012).
CC   -!- FUNCTION: Involved in several behavioral responses including chemotaxis
CC       towards lysine and adaptation to repeated osmotic stress. In addition,
CC       plays a role in resuming egg-laying and locomotion after starvation.
CC       {ECO:0000269|PubMed:22300764}.
CC   -!- SUBUNIT: Interacts with tax-6. {ECO:0000269|PubMed:22300764}.
CC   -!- TISSUE SPECIFICITY: Expressed from the comma stage to adulthood in the
CC       nervous system, including sensory neurons and interneurons posterior to
CC       the nerve ring, dorsal and ventral nerve cords, tail ganglia and, CEP,
CC       HSN, ASK, ADL, ASH and ASJ neurons. {ECO:0000269|PubMed:22300764}.
CC   -!- PTM: Phosphorylated. Dephosphorylated by tax-6 in vitro.
CC       {ECO:0000269|PubMed:22300764}.
CC   -!- DISRUPTION PHENOTYPE: Viable. Shows defects in several behavioral
CC       responses, including abnormal avoidance response to the chemoattractant
CC       lysine and impaired adaptability induced by prior exposure to high
CC       concentration of fructose. Delay in egg-laying upon refeeding after
CC       starvation. Slight decrease in brood size.
CC       {ECO:0000269|PubMed:22300764}.
CC   -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR   EMBL; BX284603; CAB03344.2; -; Genomic_DNA.
DR   PIR; T24860; T24860.
DR   RefSeq; NP_499816.2; NM_067415.4.
DR   AlphaFoldDB; O45782; -.
DR   SMR; O45782; -.
DR   STRING; 6239.T12D8.4; -.
DR   EPD; O45782; -.
DR   PaxDb; O45782; -.
DR   PeptideAtlas; O45782; -.
DR   EnsemblMetazoa; T12D8.4.1; T12D8.4.1; WBGene00011732.
DR   GeneID; 176799; -.
DR   KEGG; cel:CELE_T12D8.4; -.
DR   UCSC; T12D8.4; c. elegans.
DR   CTD; 176799; -.
DR   WormBase; T12D8.4; CE33831; WBGene00011732; arrd-17.
DR   eggNOG; KOG3780; Eukaryota.
DR   HOGENOM; CLU_039221_0_1_1; -.
DR   InParanoid; O45782; -.
DR   OMA; PRVKDPF; -.
DR   OrthoDB; 817924at2759; -.
DR   PhylomeDB; O45782; -.
DR   PRO; PR:O45782; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00011732; Expressed in larva and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IPI:WormBase.
DR   GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   Gene3D; 2.60.40.640; -; 2.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR011022; Arrestin_C-like.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   SMART; SM01017; Arrestin_C; 1.
DR   SUPFAM; SSF81296; SSF81296; 2.
PE   1: Evidence at protein level;
KW   Behavior; Phosphoprotein; Reference proteome.
FT   CHAIN           1..426
FT                   /note="Arrestin domain-containing protein 17"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436779"
FT   REGION          320..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  47637 MW;  891DC8B05D72CB8E CRC64;
     MVQLDRFEIL FNNPEQAYFA GQEISGKVII ENKEPKKVNE ILLELKGRAR TYWTKHSGKS
     RKHCSHSEPY FLEQFNPGYT HKFTVVKDGK EKERILPAGI HQVPFSYTLP KSLPSSFEGE
     FGHIRYTCKA ICERPWDFDI VSRKAFTVVG IEDINSDPKL NEPATCVESN HAVTFCCRSA
     GSVTGEIRIS KCGYTPGEKI DVSFKVINLS SKTRTTALRF VQQTTYKAKT FAGHEHIKNV
     VRVISKIDKG EVPGGSTTEW QEESITIPSL PPKLGKCKIL SVTYSVELEV EQTLTVPCPI
     VIGSIPQLSQ LLIHSKQSVQ SAGNGSLPKS SIKDSPPKWD SESCVQVTIT DESGQLVEEL
     GNEMEALLSA RKRVRMPSSI LSELYPTMPS PYYKESFFGA SDISEEKEQA QFGEASFAPK
     YPFYTD