PDLI1_BOVIN
ID PDLI1_BOVIN Reviewed; 328 AA.
AC Q5E9E1;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=PDZ and LIM domain protein 1;
DE AltName: Full=Elfin;
GN Name=PDLIM1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Cytoskeletal protein that may act as an adapter that brings
CC other proteins (like kinases) to the cytoskeleton (By similarity).
CC Involved in assembly, disassembly and directioning of stress fibers in
CC fibroblasts. Required for the localization of ACTN1 and PALLD to stress
CC fibers. Required for cell migration and in maintaining cell polarity of
CC fibroblasts (By similarity). {ECO:0000250|UniProtKB:O00151,
CC ECO:0000250|UniProtKB:P52944}.
CC -!- SUBUNIT: Interacts with ACTN1, ACTN2 and ACTN4 (By similarity).
CC Interacts with PDLIM4 (By similarity). {ECO:0000250|UniProtKB:O00151,
CC ECO:0000250|UniProtKB:P52944}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O00151}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O00151}. Cytoplasm,
CC myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O00151}.
CC Note=Associates with the actin stress fibers.
CC {ECO:0000250|UniProtKB:O00151}.
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DR EMBL; BT020979; AAX08996.1; -; mRNA.
DR RefSeq; NP_001030532.1; NM_001035455.1.
DR AlphaFoldDB; Q5E9E1; -.
DR SMR; Q5E9E1; -.
DR STRING; 9913.ENSBTAP00000014850; -.
DR PaxDb; Q5E9E1; -.
DR PeptideAtlas; Q5E9E1; -.
DR GeneID; 614675; -.
DR KEGG; bta:614675; -.
DR CTD; 9124; -.
DR eggNOG; KOG1703; Eukaryota.
DR InParanoid; Q5E9E1; -.
DR OrthoDB; 840552at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; ISS:AgBase.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:AgBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:AgBase.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR028537; PDLIM1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR006643; Zasp-like_motif.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24214:SF5; PTHR24214:SF5; 1.
DR Pfam; PF15936; DUF4749; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00735; ZM; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT CHAIN 2..328
FT /note="PDZ and LIM domain protein 1"
FT /id="PRO_0000075858"
FT DOMAIN 3..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 257..316
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 144
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 320
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
SQ SEQUENCE 328 AA; 35881 MW; 945F8C801E63D15E CRC64;
MTTLQIVLQG PGPWGFRLVG GKDFEQPLAI SRVTPGSKAA IGNLCVGDVI TAIDGENTSN
MTHLEAQNKI KGCTDNMTLT VARSEQKIWS PLVTEEGKRH PYKMNLASEP QEALHIGSAH
NRSAVPFTAS PAFSSAPRVI TNQYNNPAGL YSSENISSFN NALESKTAAS GQENGRALDH
SQLPSGLVID KESEVYKMLQ EKQELNEPPK QSTSFLVLQE ILESEEKGDP NKPSGFRSVK
APVTKVAASI GNAQKLPMCD KCGTGIVGVF VKLRERHRHP ECYVCTDCGT NLKQKGHFFV
EDQIYCEKHA RERVTPPEGY DVITVFPK
