ID A0A401RVJ7_CHIPU Unreviewed; 387 AA.
AC A0A401RVJ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Arrestin-C {ECO:0000256|ARBA:ARBA00017730};
DE AltName: Full=Cone arrestin {ECO:0000256|ARBA:ARBA00031498};
GN ORFNames=chiPu_0000536 {ECO:0000313|EMBL:GCC22151.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC22151.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC22151.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- FUNCTION: May play a role in an as yet undefined retina-specific signal
CC transduction. Could bind to photoactivated-phosphorylated red/green
CC opsins. {ECO:0000256|ARBA:ARBA00024976}.
CC -!- SIMILARITY: Belongs to the arrestin family.
CC {ECO:0000256|ARBA:ARBA00005298}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC22151.1}.
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DR EMBL; BEZZ01000007; GCC22151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RVJ7; -.
DR STRING; 137246.A0A401RVJ7; -.
DR OMA; MCVKGTE; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.640; -; 1.
DR Gene3D; 2.60.40.840; -; 1.
DR InterPro; IPR000698; Arrestin.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR011022; Arrestin_C-like.
DR InterPro; IPR017864; Arrestin_CS.
DR InterPro; IPR014753; Arrestin_N.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11792; ARRESTIN; 1.
DR PANTHER; PTHR11792:SF19; ARRESTIN-C; 1.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR PRINTS; PR00309; ARRESTIN.
DR SMART; SM01017; Arrestin_C; 1.
DR SUPFAM; SSF81296; E set domains; 2.
DR PROSITE; PS00295; ARRESTINS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00023305};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT DOMAIN 217..380
FT /note="Arrestin C-terminal-like"
FT /evidence="ECO:0000259|SMART:SM01017"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 43629 MW; 076316DD5B83365D CRC64;
MQHYPPVKSK KNSSRSSYSS TSISMTQKSG QVFKKTSPNA KLSLYLGKRD FVDHVDTVDP
VDGMLLLDPD YLKDRRAYVM LTCAFRYGRE DLDVMGLSFR KDIYCETIQV YPPVSDNKKP
LTPLQEQLAN KLKENCYPFL FQIPPNLPCS ITLQPGPEDH GKACGVDFEV KGFCADNLEE
KIHKRNSVKL IIRKVQYAPE KSTVQPKAEI TRQFLMSDKP LQLEALLGKE MYYHGEPIQV
TVHINNNTSK VVKKIKLSVD QITDVVLYQL DKYAKTVCSE EPNDTVAPNS TFTKVYSLTP
TLANNRQKRG LALDGKLKHQ DTNLASSTVL RPQLDKEVLG ILVSYLLRVK VIVSRGGILG
DLTSSEVSVE IPFYLMHPKP SEVLETL
//
