ID A0A3P9Q6J7_POERE Unreviewed; 640 AA.
AC A0A3P9Q6J7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Actin binding LIM protein family member 3 {ECO:0000313|Ensembl:ENSPREP00000029811.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000029811.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000029811.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000029811.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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 AlphaFoldDB; A0A3P9Q6J7; -.
DR Ensembl; ENSPRET00000030150.1; ENSPREP00000029811.1; ENSPREG00000020058.1.
DR GeneTree; ENSGT00950000182850; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000020058; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR CDD; cd09327; LIM1_abLIM; 1.
DR CDD; cd09328; LIM2_abLIM; 1.
DR CDD; cd09329; LIM3_abLIM; 1.
DR CDD; cd09330; LIM4_abLIM; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR Gene3D; 1.10.950.10; Villin headpiece domain; 1.
DR InterPro; IPR032402; AbLIM_anchor.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24213; ACTIN-BINDING LIM PROTEIN; 1.
DR PANTHER; PTHR24213:SF0; ACTIN-BINDING LIM PROTEIN 3; 1.
DR Pfam; PF16182; AbLIM_anchor; 2.
DR Pfam; PF00412; LIM; 4.
DR Pfam; PF02209; VHP; 1.
DR SMART; SM00132; LIM; 4.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 6.
DR SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR PROSITE; PS51089; HP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 20..79
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 80..139
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 149..208
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 572..640
FT /note="HP"
FT /evidence="ECO:0000259|PROSITE:PS51089"
FT REGION 404..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 72543 MW; 679B9855BF9D0E07 CRC64;
MSSSAHRQVS TRSERGSEPI RCQRCREVCK GEVVRVQDTH FHVKCFTCTV CNCDLARSGF
FQKKGEYICT ADYQRLYGTR CDRCGNFITG EVVSALGRTY HPKCFVCSMC SKPFPIGDRV
TFSGKDCVCQ QCSHTLVKSN EPIKIHGPSH CAGCGAEIKQ GQSLLALEKQ WHVSCFRCRT
CNMVLTGEYI SKDGAPYCEA DYHAQYGVKC ETCNRYISGR VLEAGGKHYH PTCARCARCN
TMFKEGEEMY LTGCEVWHPL CKQAARAERR LRHRRLSETS ISPPGSSIGS PSRVICARVE
NEIFDYKDLA ALPKVKAIYE VQQPDLISSS YQPFHRYTSD ERLDTFTYGE SLGNLSPYSQ
DYDHPDAKQL RCPIQGYIDS PTYSRQGMSP IMPRSPQHFV YPATKSRTSE DILRSSSLST
YSPEPYTQSE SDYYPYTSSP RAYRAPRRRF STGGDEESWS QGLQRIGSGI GRMILKEEMK
ARSGSYDNDP WGSARNSRCG SKETLNTTGY GTTAYNNTIN GSPRSQYSAD SDFGCKSASL
PGYRRNGIQR PQSADCYQYQ YDDGSEVNWG SRAEYKVYPY DSLIVTTRGR NKLPKDVDRA
RLERHLSPEE FVQVFGMTVE DFDRLALWKR NELKKQARLF
//
