ID A0A3B3TUQ8_9TELE Unreviewed; 1203 AA.
AC A0A3B3TUQ8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Vigilin {ECO:0000256|ARBA:ARBA00039270};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000004302.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000004302.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR AlphaFoldDB; A0A3B3TUQ8; -.
DR STRING; 48699.ENSPLAP00000004302; -.
DR Ensembl; ENSPLAT00000009865.1; ENSPLAP00000004302.1; ENSPLAG00000006033.1.
DR GeneTree; ENSGT00900000141059; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd22405; KH-I_Vigilin_rpt1; 1.
DR CDD; cd22413; KH-I_Vigilin_rpt10; 1.
DR CDD; cd22414; KH-I_Vigilin_rpt11; 1.
DR CDD; cd22415; KH-I_Vigilin_rpt12; 1.
DR CDD; cd22416; KH-I_Vigilin_rpt13; 1.
DR CDD; cd22417; KH-I_Vigilin_rpt14; 1.
DR CDD; cd22418; KH-I_Vigilin_rpt15; 1.
DR CDD; cd22406; KH-I_Vigilin_rpt2; 1.
DR CDD; cd22407; KH-I_Vigilin_rpt3; 1.
DR CDD; cd22408; KH-I_Vigilin_rpt4; 1.
DR CDD; cd22409; KH-I_Vigilin_rpt5; 1.
DR CDD; cd02394; KH-I_Vigilin_rpt6; 1.
DR CDD; cd22410; KH-I_Vigilin_rpt7; 1.
DR CDD; cd22411; KH-I_Vigilin_rpt8; 1.
DR CDD; cd22412; KH-I_Vigilin_rpt9; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 14.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR PANTHER; PTHR10627; SCP160; 1.
DR PANTHER; PTHR10627:SF34; VIGILIN; 1.
DR Pfam; PF00013; KH_1; 14.
DR SMART; SM00322; KH; 14.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 12.
DR PROSITE; PS50084; KH_TYPE_1; 14.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT DOMAIN 151..219
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 223..291
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 296..364
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 365..431
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 436..504
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 508..577
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 582..650
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 654..723
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 728..797
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 801..870
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 874..973
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 974..1040
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1052..1121
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1125..1194
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 15..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 778..805
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1203 AA; 134081 MW; C9192CF95426F569 CRC64;
MSSVAVLTQE SFIEHRSGLL PEQSGAAGGP SAGEDEEELP TYKDAFPPLP EKAATPEGTQ
ETANAWTSKI RPLKSSIITQ VFHVPLEERK YKDINQFGEG EQAKVCVDIM HKTGAHLELS
LAKDQGLSIM VSGKLDAVMK ARKEIVSRLQ TQASATVAIP KEHHRFVIGK NGEKLQELEL
KTATKIQIPR PDDPSNQIKI SGTKEGLEKA KHEILLISAE QDKRAVERVN IDKVYHPFIT
GAYNKIVGEM MQETGARINV PPPSVNKNEI VITGEKEQVA LAVTLIKKIH EEKKKSTTTI
AVEVKKSQHK YVVGPKGNTL QEILDRTGVS VEIPPSDNSS ETVILRGEPD RLGQALTEVY
AKANSYTVSS VSAPSWLHRF IIGKKGQNLA KITQQMPKVH IEFTEGEDKI TLEGPTKDVQ
MVQSQIQAIV TDLVSRMDYA EITVDPKFHR HLIGKGGVNI NRIKELHKVT VRIPPDNEKS
NLIRIEGDPQ GVQEAKKELL ELASRMENER TKDLIIEHRL HRAIIGQKGE KIKEVRDKFP
EVIINFPDPA QKSDIVQLRG PRNEVEKCSK FMQKMVAEMV ENSQTLSVPI FKQFHRNIIG
KGGANIKKIR EETNTKIDLP AENSNSEMIV ITGKKANCEA ARNRILAIQK ELANITEMDV
SIPSKLHNLL IGSKGRLVRS IMEECGGVHI HFPTEGSGID KVTIRGPVEE VEKAKQQLLA
LAEEKQIKSF TAELHAKPEY HKFLIGKGGG NIRKVRDSTG ARIIFPTSED KDQELITVVG
TEEAVRTAQK ELEELIKSLD NIVEDTMNVD PKHHRYFVAR RGQVLRDLAD EYGGVMVSFP
RTASQSDKVT LKGAKECVEA AKKRMQEIVE DLEAQVTIEC VISQKFHRSI MGPKGSRIQQ
ITRDHNVQIK FPEREDPQAA PPAEAAVQEN GEANGEVKEP VDPNAPKKCD VILISGRKER
CEAAVEALKV LVPVTIEVEV PFELHRYIIG QKGSGIRKMM DEFEVNIQVP PPDQQSDKIA
ITGLASHLDR AKEGLFERVK ELQAEQADRA LKSFKLTITV DPKYHPKIIG RKGAIITNIR
TEHDVNIQFP EKNDENQDQI TITGYEQNAI AAREAIQAIV DELEEMISEN ITLDSRVHAR
IIGARGKGIR KIMDEFKIDL RFPQSGAADP NLVAVIGRPE HVDEAIDHLL NLEEEYLSDV
VEN
//