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Database: UniProt
Entry: A0A2Y9LTM8_DELLE
LinkDB: A0A2Y9LTM8_DELLE
Original site: A0A2Y9LTM8_DELLE 
ID   A0A2Y9LTM8_DELLE        Unreviewed;       758 AA.
AC   A0A2Y9LTM8;
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 2 isoform X15 {ECO:0000313|RefSeq:XP_022410442.1};
GN   Name=ABLIM2 {ECO:0000313|RefSeq:XP_022410442.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022410442.1};
RN   [1] {ECO:0000313|RefSeq:XP_022410442.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022410442.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   RefSeq; XP_022410442.1; XM_022554734.2.
DR   AlphaFoldDB; A0A2Y9LTM8; -.
DR   Proteomes; UP000248483; 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; 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:SF6; ACTIN-BINDING LIM PROTEIN 2; 1.
DR   Pfam; PF16182; AbLIM_anchor; 1.
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; 2.
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:UP000248483};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          175..234
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          235..294
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          304..363
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          690..758
FT                   /note="HP"
FT                   /evidence="ECO:0000259|PROSITE:PS51089"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   758 AA;  84091 MW;  D455D4E05AA006BE CRC64;
     MPAATRIWTG REGSSRRAQR EPCPADTWIS AQWYRLWTSG FQNCCLTSLC WFVTTATRNE
     YTSEQTTPKR RGRTRQSVFL AGGLRAGRGS ANQARLRGGG SAPSPTLLLG PAGGRSTVGQ
     REPPSAWTQN WNIVTSTRVP WPSQPHEPAQ RGDPGEVSEP QAARSAPEKP ASTAILCNTC
     GNVCRGEVLR VQSKYFHIQC FVCKECGCDL AEGGFFVRQG EYICTQDYQR LYGTRCFSCD
     QFIEGEVVSA LGKTYHPNCF VCAVCRLPFP PGDRVTFNGK ECMCQKCSLP TSAGSSVPLS
     QGLWSCKGCG VEIKNGQSLV ALEKHWHLGC FKCKTCGKQL NAEYISKDGL PYCEADYHSK
     FGIRCDGCEK YITGHVLEAG EKHFHPLCAL CVGCGRMFAE GEEMYLQGSS IWHPACRQAA
     RTEDKSKETR TSSESIISVP ASSTSGSPSR VIYAKLGDEI LDYRDLAALP KNKAIYSIDR
     PDMISYSPFI SHSVGDRQSC SEGYQDDRSY KQCRTSSPSS TGSVSLGRYT PTLRSPQHYS
     RPAGTLSVGT SSCLSLSQHP SPTSVFRHHY IPYFRGSESG RSTSSLSVLS DSKPPPSTYQ
     QAPRHFHVPD TGVKDNIYRK PPIYKQHAGR RSDGEDGSFD ADNRKKTNWL LLKGDGDTRT
     NSPDLDSQSL AHSSGTDRGP LQTMPGDNIY SQYKIYPYDA LIVTNRIRVK LPKDVDRTRL
     ERHLSPEEFQ EVFGMSMEEF DRLALWKRND LKKKALLF
//
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