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Database: UniProt
Entry: A0A452S640_URSAM
LinkDB: A0A452S640_URSAM
Original site: A0A452S640_URSAM 
ID   A0A452S640_URSAM        Unreviewed;       761 AA.
AC   A0A452S640;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=LIM domain and actin binding 1 {ECO:0000313|Ensembl:ENSUAMP00000027583.1};
GN   Name=LIMA1 {ECO:0000313|Ensembl:ENSUAMP00000027583.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000027583.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000027583.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A452S640; -.
DR   STRING; 9643.ENSUAMP00000027583; -.
DR   Ensembl; ENSUAMT00000030824.1; ENSUAMP00000027583.1; ENSUAMG00000021327.1.
DR   GeneTree; ENSGT00940000158313; -.
DR   OMA; NQQVFHV; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0032154; C:cleavage furrow; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR   GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR   GO; GO:0003785; F:actin monomer binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051017; P:actin filament bundle assembly; IEA:Ensembl.
DR   GO; GO:0030835; P:negative regulation of actin filament depolymerization; IEA:Ensembl.
DR   GO; GO:0031529; P:ruffle organization; IEA:Ensembl.
DR   CDD; cd09485; LIM_Eplin_alpha_beta; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR   InterPro; IPR028740; EPLIN_Lim_dom.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24206:SF57; LIM DOMAIN AND ACTIN-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR24206; OS06G0237300 PROTEIN; 1.
DR   Pfam; PF00412; LIM; 1.
DR   SMART; SM00132; LIM; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   4: Predicted;
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          388..448
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          79..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..586
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..676
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  84838 MW;  51F9A41F2C71E78C CRC64;
     MESAPFNRRQ WTSVSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEEANM EKRRSNTENL
     PQHCRRGVLT VLKKKWENPA LGTESHTDSL RNGSAEVGHG GNQPAGEVAR SSASEAEADQ
     EERAHPRPRF GSPPEALTQC PYPRTEGSER PKDHLKERKK MENCLGESRH EVGKPEISEN
     TEAANKIEKY NVPLNRLKMM FEKGEPTQTK ILRSQSRSTG GRRISENSCS LDDLEIGPGQ
     SSSSPFNAEK SESRRNLDFP RLSETSIKDR MAKYQAAVSK QSSSTNSTND LRANGGEIRT
     HKLEQKENVP PDPEVCISHQ VGEKVSATEN SLAVRSTPAE DESRNSQVKS EVQQPVHPKP
     LNPDARASSL SESSPPKAVK KFQAPARETC VECQKTVYPM ERLLANQQVF HVSCFRCSYC
     NNKLTLGTYA SLHGRIYCKP HFNQLFKAKG NYDEGFGHRP HKDLWASKNE NEGILERPAQ
     LPNAGETPQS PGVEDAPIAK VGVLTASMEA KASSQPEKED KPAETKKLKI AWPPPTELGS
     SGSILEEGIK VSKPKWPPED EISKPEAPED VDLDLKKLRR SSSLKERSRP FTVAASFRTT
     SVKSPKISSP PIRKGWSMSE QSEEFTGGMT AERKQVENAN TFEKNGSVGK TTWQNQESGG
     GETGRRSKED HGFEMGSENL TENGANLDED DRNLNQQSPL EPTPTNWSSF ADNTSPKEFT
     TQNQESEDVG FWEGEVVQEL SVEEQIKRNR YYDEEEEEDE E
//
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