ABLM2_RAT
ID ABLM2_RAT Reviewed; 612 AA.
AC Q6KC51; Q6KC50;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Actin-binding LIM protein 2;
DE Short=abLIM-2;
DE AltName: Full=Actin-binding LIM protein family member 2;
GN Name=Ablim2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Wistar;
RA Klimov E.A., Rakhmanaliev E.R., Rudco O.I.;
RT "Structure and transcriptional activity of the ABLIM2 gene of human, mouse
RT and rat.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282; SER-365; SER-453;
RP SER-477 AND SER-579, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May act as scaffold protein. May stimulate ABRA activity and
CC ABRA-dependent SRF transcriptional activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with F-actin and ABRA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In skeletal muscle, sarcomeric or
CC cosarcomeric localization. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6KC51-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6KC51-2; Sequence=VSP_012125;
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DR EMBL; AJ703892; CAG28314.1; -; mRNA.
DR EMBL; AJ703893; CAG28315.1; -; mRNA.
DR RefSeq; NP_001001514.1; NM_001001514.2. [Q6KC51-2]
DR RefSeq; NP_001171166.1; NM_001177695.1. [Q6KC51-1]
DR AlphaFoldDB; Q6KC51; -.
DR BMRB; Q6KC51; -.
DR SMR; Q6KC51; -.
DR BioGRID; 262329; 1.
DR IntAct; Q6KC51; 1.
DR MINT; Q6KC51; -.
DR STRING; 10116.ENSRNOP00000055116; -.
DR iPTMnet; Q6KC51; -.
DR PhosphoSitePlus; Q6KC51; -.
DR SwissPalm; Q6KC51; -.
DR PaxDb; Q6KC51; -.
DR PRIDE; Q6KC51; -.
DR Ensembl; ENSRNOT00000058315; ENSRNOP00000055116; ENSRNOG00000007882. [Q6KC51-1]
DR GeneID; 360958; -.
DR KEGG; rno:360958; -.
DR CTD; 84448; -.
DR RGD; 1303094; Ablim2.
DR eggNOG; KOG1044; Eukaryota.
DR GeneTree; ENSGT00950000182850; -.
DR HOGENOM; CLU_001357_12_3_1; -.
DR InParanoid; Q6KC51; -.
DR OrthoDB; 192350at2759; -.
DR PRO; PR:Q6KC51; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Genevisible; Q6KC51; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0030032; P:lamellipodium assembly; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.950.10; -; 1.
DR InterPro; IPR028450; ABLIM2.
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:SF6; PTHR24213:SF6; 2.
DR Pfam; PF16182; AbLIM_anchor; 2.
DR Pfam; PF00412; LIM; 4.
DR Pfam; PF02209; VHP; 1.
DR SMART; SM00132; LIM; 4.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR PROSITE; PS51089; HP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..612
FT /note="Actin-binding LIM protein 2"
FT /id="PRO_0000075701"
FT DOMAIN 22..81
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 81..141
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 151..210
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 210..270
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 544..612
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 269..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL65"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL65"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 473
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL65"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 507..546
FT /note="RFPYSKPDTLPGPRKDGLDLRNANLAPCGADPDASWGTRE -> Q (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_012125"
SQ SEQUENCE 612 AA; 68010 MW; B6B6E27365D00B26 CRC64;
MSAVSQPQAA HAPLEKPAST AILCNTCGNV CKGEVLRVQN KHFHIRCFVC KACGCDLAEG
GFFVRQGEHI CTRDYQRLYG TRCFSCDCFI EGEVVSALGK TYHPDCFVCA VCRLPFPPGD
RVTFNGKDCM CQKCSPPTLV GNSAHVAQGL RSCGGCGLEI KNGQALVALD KHWHLGCFKC
KTCGKLLNAE YISKDGLPYC EADYHTKFGI RCDGCEKYIT GRVLEAGEKH YHPSCALCVR
CGQMFSEGEE MYLQGSSIWH PACRQAARTE DKSKETRTSS ESIVSVPASS TSGSPSRVIY
AKLGDEILDY RDLAALPKNK AIYNIDRPDM ISYSPYISHS AVGDRQSYGE GDQDDRSYKQ
CRTSSPSSAG SVSLGHYTPT SRSPQHYSRP GSESGRSTPS LSVHSDSRPP SSTYQQAPRH
FHVPDTGVKD NIYRKPPIYK QHAARRLDVE DSSFDQDSRK KTTWLLLKGD ADTRTNSPDL
DSQSLSLSSG ADQEPLQRMP GDSLYSRFPY SKPDTLPGPR KDGLDLRNAN LAPCGADPDA
SWGTREYKIY PYDSLIVTNR IRVKLPKDVD RTRLERHLSP EEFQEVFGMS IEEFDRLALW
KRNDLKKKAL LF
