PDLI3_CHICK
ID PDLI3_CHICK Reviewed; 315 AA.
AC Q9PU47; Q9PU46;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=PDZ and LIM domain protein 3;
DE AltName: Full=Alpha-actinin-associated LIM protein;
GN Name=PDLIM3; Synonyms=ALP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-250
RP (ISOFORM 2), PROTEIN SEQUENCE OF 1-31; 87-97; 103-135; 137-163; 165-181;
RP 207-222 AND 300-315, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH ALPHA-ACTININ.
RX PubMed=10506181; DOI=10.1074/jbc.274.41.29242;
RA Pomies P., Macalma T., Beckerle M.C.;
RT "Purification and characterization of an alpha-actinin-binding PDZ-LIM
RT protein that is up-regulated during muscle differentiation.";
RL J. Biol. Chem. 274:29242-29250(1999).
CC -!- FUNCTION: May play a role in the organization of actin filament arrays
CC within muscle cells. {ECO:0000269|PubMed:10506181}.
CC -!- SUBUNIT: Interacts with alpha-actinin. {ECO:0000269|PubMed:10506181}.
CC -!- SUBCELLULAR LOCATION: Note=Isoform 1 colocalizes with alpha-actinin
CC along actin stress fibers and lammellipodia of spreading fibroblasts.
CC Isoform 2 colocalizes with alpha-actinin at the Z-lines of myotubes.
CC {ECO:0000269|PubMed:10506181}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton. Cell
CC projection, lamellipodium. Note=Isoform 1 colocalizes with alpha-
CC actinin along actin stress fibers and lammellipodia of spreading
CC fibroblasts.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton. Cytoplasm,
CC myofibril, sarcomere, Z line. Note=Isoform 2 colocalizes with alpha-
CC actinin at the Z-lines of myotubes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=p36-ALP, SmALP;
CC IsoId=Q9PU47-1; Sequence=Displayed;
CC Name=2; Synonyms=p40-ALP, SkALP;
CC IsoId=Q9PU47-2; Sequence=VSP_016505;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in heart and in tissues
CC enriched in smooth muscle including arteries, stomach, gizzard,
CC intestine, and lung. Isoform 2 is skeletal muscle-specific. Isoform 1
CC and isoform 2 are up-regulated during myogenic differentiation.
CC {ECO:0000269|PubMed:10506181}.
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DR EMBL; AJ249218; CAB53970.1; -; mRNA.
DR EMBL; AJ249219; CAB53971.1; -; mRNA.
DR RefSeq; NP_001001764.1; NM_001001764.1. [Q9PU47-1]
DR AlphaFoldDB; Q9PU47; -.
DR SMR; Q9PU47; -.
DR GeneID; 414873; -.
DR KEGG; gga:414873; -.
DR CTD; 27295; -.
DR VEuPathDB; HostDB:geneid_414873; -.
DR eggNOG; KOG1703; Eukaryota.
DR InParanoid; Q9PU47; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; Q9PU47; -.
DR PRO; PR:Q9PU47; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:AgBase.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:AgBase.
DR GO; GO:0030027; C:lamellipodium; IDA:AgBase.
DR GO; GO:0001725; C:stress fiber; IDA:AgBase.
DR GO; GO:0030018; C:Z disc; IDA:AgBase.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0051393; F:alpha-actinin binding; IPI:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR006643; Zasp-like_motif.
DR InterPro; IPR001781; Znf_LIM.
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 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; LIM domain; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..315
FT /note="PDZ and LIM domain protein 3"
FT /id="PRO_0000075871"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 243..302
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT VAR_SEQ 111..173
FT /note="EFKPIGTAHNRRAQPFVAAANIDDKRQVVSSSYNSPIGLYSSGNIQDALHGQ
FT LRSLIPNASQN -> DINYFEHRHNIRPKPFILPGRSSGCSTPSGIDCGSGRSTPSSIS
FT TVSSICPTELKAVSRMAPNVPLEMELPGVKIVHAQFNTPMQLYSDDNIMETLQGQVSTA
FT LGETPVMS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10506181"
FT /id="VSP_016505"
FT CONFLICT 81
FT /note="E -> K (in Ref. 1; CAB53971)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="A -> T (in Ref. 1; CAB53971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 34365 MW; 86414A80A89BCA35 CRC64;
MPQNVILPGP APWGFRLSGG IDFNQPLIIT RITPGSKAST ANLCPGDIIV AINGLSTENM
THNDAQERIK AAAHQLSLRI ERAETKLWSP QVSEDGKANP YKINLEAEPQ EFKPIGTAHN
RRAQPFVAAA NIDDKRQVVS SSYNSPIGLY SSGNIQDALH GQLRSLIPNA SQNDPAPAAV
PQSDVYRMLH SNQEEPSQPR QSGSFKVLQN LVSEEDGRPV GTRSVKAPVT KIPTGLPGAQ
KVPQCDKCGS GILGTVVKAR DKYRHPECFV CSDCNLNLKQ KGYFFVEGQL YCEAHARARM
RPPEGYEAVT VYPKC
