ID A0A3P9MTX9_POERE Unreviewed; 534 AA.
AC A0A3P9MTX9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Paxillin-like {ECO:0000313|Ensembl:ENSPREP00000000793.1};
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:ENSPREP00000000793.1, 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:ENSPREP00000000793.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000000793.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the paxillin family.
CC {ECO:0000256|ARBA:ARBA00005813, ECO:0000256|PIRNR:PIRNR037881}.
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DR AlphaFoldDB; A0A3P9MTX9; -.
DR STRING; 8081.ENSPREP00000000793; -.
DR Ensembl; ENSPRET00000000829.1; ENSPREP00000000793.1; ENSPREG00000000565.1.
DR GeneTree; ENSGT00940000158897; -.
DR OMA; THYVQAN; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000000565; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd09336; LIM1_Paxillin_like; 1.
DR CDD; cd09338; LIM3_Paxillin_like; 1.
DR CDD; cd09411; LIM4_Paxillin; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR InterPro; IPR001904; Paxillin_Lim_dom4.
DR InterPro; IPR047075; Paxillin_TGFB1I1_LIM_dom1.
DR InterPro; IPR017305; Tgfb1i1/Leupaxin/TGFB1I1.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24216; PAXILLIN-RELATED; 1.
DR PANTHER; PTHR24216:SF8; PAXILLIN-RELATED; 1.
DR Pfam; PF00412; LIM; 4.
DR Pfam; PF03535; Paxillin; 1.
DR PIRSF; PIRSF037881; Leupaxin; 2.
DR SMART; SM00132; LIM; 4.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 5.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PIRNR:PIRNR037881};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 299..358
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 359..416
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 417..476
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 477..534
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 86..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 58943 MW; C93EC750ADEB3D33 CRC64;
MQNIFDKCFD NVFLLDDVNK NSTTSHISKC SLFLSDEAAY SLPVGGQDQK DICSPPERSL
NGVDDSEVNE HALYVSLCSS KAVATKLESS SPNQPSGEED HVYSFPNKQK TSESSSSPAA
MNSSLGSNLS ELDRLLLELN AVQQSTPAFP TEAPPLPASS TIRHIQQNGL SAPGKIPPPT
LEKPKHVIAA RGIQDARPSV ESLLDELESS VPTPIPLVVS DEPNDRQAET LSQQQARMSA
SSATRELDEL MASLSDFKIQ SQGIQSTSAP AKPANKLDNM LGNLQSDLNK LGVQTNAKGV
CGACKKPIAG QVVTAMGRTW HPEHFVCTHC QEEIGSRNFF ERDGQPYCEK DYHNLFSPRC
HYCNGPILDK VVTALDKTWH PEHFFCAQCG SFFGPEGFHE KDGKAFCRKD YFDMFAPKCG
GCTRAILENY ISALNSLWHP ECFVCRECFT PFINGSFFDH DGQPYCEAHY HERRGSLCSG
CQKPITGRCI TAMGKKFHPE HFVCAFCLKQ LNKGTFKEQN DKPYCHGCFV KLFS
//
