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Database: UniProt
Entry: A0A2Y9R2A2_TRIMA
LinkDB: A0A2Y9R2A2_TRIMA
Original site: A0A2Y9R2A2_TRIMA 
ID   A0A2Y9R2A2_TRIMA        Unreviewed;       656 AA.
AC   A0A2Y9R2A2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Actin-binding LIM protein 1 isoform X8 {ECO:0000313|RefSeq:XP_023585743.1};
GN   Name=LOC101347995 {ECO:0000313|RefSeq:XP_023585743.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023585743.1};
RN   [1] {ECO:0000313|RefSeq:XP_023585743.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   RefSeq; XP_023585743.1; XM_023729975.1.
DR   AlphaFoldDB; A0A2Y9R2A2; -.
DR   STRING; 127582.A0A2Y9R2A2; -.
DR   InParanoid; A0A2Y9R2A2; -.
DR   OrthoDB; 370973at2759; -.
DR   Proteomes; UP000248480; Unplaced.
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; 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; 3.
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:SF18; ACTIN-BINDING LIM PROTEIN 1; 1.
DR   Pfam; PF16182; AbLIM_anchor; 1.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00132; LIM; 3.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 5.
DR   SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR   PROSITE; PS51089; HP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
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:UP000248480};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          4..64
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          72..131
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          588..656
FT                   /note="HP"
FT                   /evidence="ECO:0000259|PROSITE:PS51089"
FT   REGION          217..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   656 AA;  73878 MW;  4EA03368BE034466 CRC64;
     MYGTCCHGCG EFVEGEVVTA LGKTYHPNCF ACTICKRPFP PGDRVTFNGR DCLCQLCAQP
     MSSSPKEATC SSNCAGCGRD IKNGQALLAL DKQWHLGCFK CKSCGKVLTG EYISKDGAPY
     CEKDYQGLFG VKCEACHQFI TGKVLEAGDK HYHPSCARCS RCNQMFTEGE EMYLQGSTVW
     HPDCKQSTKT EEKLRPPNLH RSSFDFFYPK SLIRRAGRSS SLQPTRTSSE SIYSRPGSSI
     PGSPGHTIYA KVDNEILDYK DLAAIPKVKA IYDIERPDLI TYEPFYTSGY DDKQERQSLG
     ESPRTLSPTP SAEGYQDVRD RMIHRSTSQG SINSPVYSRH SYTPTTSRSP QHFHRPGNEP
     SSGRNSPLPY RPDSRPLTPT YAQAPKHFHV PDQGINIYRK PPIYKQHDAA ALAAQSKSSE
     DIIKFSKFPA AQAPDHNEIP KIETDLWPGP PSVATIGTDM RRRSSGREED EEELLRRRQL
     QEEQLMKLNS GLGQLILKEE MEKESRERAS LSASRYDSPI NSASHAPSSK TSSLPGYGKN
     GLHRPVSTEF AQYNSYGDVS GGVRDYQTLP DGHMPGMRMD RGVSMPNMLE PKIFPYEMLM
     VTNRGRNKIL RDVDRTRLER HLSPEVFREI FGMSIQEFDR LPLWRRNDMK KKAKLF
//
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