ID A0A3B4AM59_9GOBI Unreviewed; 453 AA.
AC A0A3B4AM59;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=LIM zinc-binding domain-containing protein {ECO:0000259|PROSITE:PS50023};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000017775.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000017775.1}
RP IDENTIFICATION.
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; A0A3B4AM59; -.
DR STRING; 409849.ENSPMGP00000017775; -.
DR Ensembl; ENSPMGT00000018966.1; ENSPMGP00000017775.1; ENSPMGG00000014545.1.
DR Proteomes; UP000261520; Unplaced.
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; cd09409; LIM3_Paxillin; 1.
DR CDD; cd09339; LIM4_Paxillin_like; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR InterPro; IPR047075; Paxillin_TGFB1I1_LIM_dom1.
DR InterPro; IPR017305; Tgfb1i1/Leupaxin/TGFB1I1.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24205; FOUR AND A HALF LIM DOMAINS PROTEIN; 1.
DR PANTHER; PTHR24205:SF4; LIM DOMAIN FAMILY; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 218..276
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 277..336
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 337..395
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 396..453
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 50121 MW; 4CEB9343F9EA44FC CRC64;
MEDLDALLAD LENTSSPLSR CPVLLTSEPP LNADSTSQDT AQVRPPPPAY TPQQTVSAAM
KSSQNSNADK LYSTVNKPRS PRAADPPPAF SSSSLLGGGL SELDHLLQEL NATQFNITDE
ILAQFPSPKK DDKPKDRTIS STKPSATSAT LELDKLMASL SDFRVQSTCL YNKMLNYIPF
LQPVAPVTPG SSGGSLDSML GLLQSDLTRQ GVHTSSKGTC TACQKPVVGQ VVTALGKVWH
PEHFVCTECE IELGSRNFFE KDSRPYCESD YFTLFSPHCA QCNKPILNKM VTALDKNWHP
ECFCCVKCTR AFGEEGFHDR EGQQYCQQCF LTLFASRCQG CSQPILENYI SALNSLWHPQ
CFVCRECYSP FVNGSFFEHD GKPLCEAHYH QSRGSMCQAC QQPILGRCVT AMGAKFHPHH
LVCHFCLKPL SKGCFKEQEN KPYCHPCFIK LFG
//
