PDLI3_RAT
ID PDLI3_RAT Reviewed; 362 AA.
AC Q66HS7; O70208;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=PDZ and LIM domain protein 3;
DE AltName: Full=Actinin-associated LIM protein;
DE AltName: Full=Alpha-actinin-2-associated LIM protein;
DE AltName: Full=SK-2;
GN Name=Pdlim3; Synonyms=Alp {ECO:0000303|PubMed:9334352};
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), SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND INTERACTION WITH ACTN2.
RC TISSUE=Skeletal muscle;
RX PubMed=9334352; DOI=10.1083/jcb.139.2.507;
RA Xia H., Winokur S.T., Kuo W.-L., Altherr M.R., Bredt D.S.;
RT "Actinin-associated LIM protein: identification of a domain interaction
RT between PDZ and spectrin-like repeat motifs.";
RL J. Cell Biol. 139:507-515(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-263, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 play a role in the organization of actin filament arrays
CC within muscle cells. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ACTN2 (PubMed:9334352). Forms a heterodimer
CC with PDLIM4 (via LIM domain) (By similarity).
CC {ECO:0000250|UniProtKB:O70209, ECO:0000269|PubMed:9334352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:9334352}. Note=Localizes to myofiber Z-lines.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66HS7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66HS7-2; Sequence=VSP_016503, VSP_016504;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and at low
CC levels in the heart. {ECO:0000269|PubMed:9334352}.
CC -!- DEVELOPMENTAL STAGE: At E15 highly expressed in developing skeletal
CC muscles, tongue, sternocephalic and tail. Weaker expression is seen in
CC the heart atrium and ventricle. Expressed in a circular pattern in the
CC intestine.
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DR EMBL; AF002281; AAC16671.1; -; mRNA.
DR EMBL; BC081703; AAH81703.1; -; mRNA.
DR RefSeq; NP_446102.1; NM_053650.1.
DR RefSeq; XP_006253181.1; XM_006253119.3.
DR AlphaFoldDB; Q66HS7; -.
DR SMR; Q66HS7; -.
DR STRING; 10116.ENSRNOP00000017054; -.
DR iPTMnet; Q66HS7; -.
DR PhosphoSitePlus; Q66HS7; -.
DR PaxDb; Q66HS7; -.
DR PeptideAtlas; Q66HS7; -.
DR PRIDE; Q66HS7; -.
DR GeneID; 114108; -.
DR KEGG; rno:114108; -.
DR CTD; 27295; -.
DR RGD; 620427; Pdlim3.
DR eggNOG; KOG1703; Eukaryota.
DR InParanoid; Q66HS7; -.
DR OrthoDB; 840552at2759; -.
DR PRO; PR:Q66HS7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0042805; F:actinin binding; IDA:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
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:0008307; F:structural constituent of muscle; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
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; Cytoplasm; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..362
FT /note="PDZ and LIM domain protein 3"
FT /id="PRO_0000075870"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 290..349
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 261..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53GG5"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 110..173
FT /note="DVNYFEHKHNIRPKPFIIPGRTSGCSTPSGIDCGSGRSTPSSVSTVSTICPG
FT DLKVAAKMAPNI -> EFKPIGTAHNRRAQPFVAAANIDDKRQVVSASYNSPIGLYSTS
FT NIRDALHGQLRGLIPSSPQN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9334352"
FT /id="VSP_016503"
FT VAR_SEQ 174..220
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9334352"
FT /id="VSP_016504"
FT CONFLICT 12
FT /note="P -> S (in Ref. 1; AAC16671)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="V -> M (in Ref. 1; AAC16671)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..90
FT /note="CPA -> WSPQ (in Ref. 2; AAH81703)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="R -> RA (in Ref. 2; AAH81703)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="T -> A (in Ref. 1; AAC16671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 39106 MW; 02D4174590F5DD78 CRC64;
MPQNVVLPGP APWGFRLSGG IDFNQPLVIT RITPGSKAEA ANLCPGDVIL AIDGFGTESM
THADAQDRIK AASYQLCLKI DRAETRLCPA VSEDGKAHPF KINLEAEPQD VNYFEHKHNI
RPKPFIIPGR TSGCSTPSGI DCGSGRSTPS SVSTVSTICP GDLKVAAKMA PNIPLEMELP
GVKIVHAQFN TPMQLYSDDN IMETLQGQVS TALGETPSMS EPTASVPPQS DVYRMLHDNR
DEPAAPRQSG SFRVLQELVN DGSDDRPAGT RSVRPVTKVH GGAGGAQRMP LCDKCGSGIV
GAVVKARDKY RHPECFVCAD CNLNLKQKGY FFVEGELYCE MHARARTRPP EGYDTVTLYP
KA
