PDLI3_HUMAN
ID PDLI3_HUMAN Reviewed; 364 AA.
AC Q53GG5; B2R866; O43590; O60439; O60440; Q8N6Y6; Q9BVP4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 154.
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;
GN Name=PDLIM3; Synonyms=ALP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
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 [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=10063829; DOI=10.1016/s0960-8966(98)00087-x;
RA Bouju S., Pietu G., Le Cunff M., Cros N., Malzac P., Pellissier J.-F.,
RA Pons F., Leger J.-J., Auffray C., Dechesne C.A.;
RT "Exclusion of muscle specific actinin-associated LIM protein (ALP) gene
RT from 4q35 facioscapulohumeral muscular dystrophy (FSHD) candidate genes.";
RL Neuromuscul. Disord. 9:3-10(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Lung, and Skin;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play a role in the organization of actin filament arrays
CC within muscle cells. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ACTN2 (By similarity). Forms a heterodimer with
CC PDLIM4 (via LIM domain) (By similarity). {ECO:0000250|UniProtKB:O70209,
CC ECO:0000250|UniProtKB:Q66HS7}.
CC -!- INTERACTION:
CC Q53GG5; P35609: ACTN2; NbExp=6; IntAct=EBI-5658852, EBI-77797;
CC Q53GG5; P49792: RANBP2; NbExp=3; IntAct=EBI-5658852, EBI-973138;
CC Q53GG5-2; P35609: ACTN2; NbExp=3; IntAct=EBI-12702438, EBI-77797;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:10063829}. Note=Localizes to myofiber Z-lines.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ALP-SK;
CC IsoId=Q53GG5-1; Sequence=Displayed;
CC Name=2; Synonyms=ALP-H;
CC IsoId=Q53GG5-2; Sequence=VSP_016501;
CC Name=3;
CC IsoId=Q53GG5-3; Sequence=VSP_016500, VSP_016502;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in differentiated
CC skeletal muscle. Isoform 2 is heart-specific.
CC {ECO:0000269|PubMed:9334352}.
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DR EMBL; AF002280; AAC16670.1; -; mRNA.
DR EMBL; AF002282; AAC16672.1; -; mRNA.
DR EMBL; AF039018; AAB96665.1; -; mRNA.
DR EMBL; AK313253; BAG36063.1; -; mRNA.
DR EMBL; BT007341; AAP36005.1; -; mRNA.
DR EMBL; AK222966; BAD96686.1; -; mRNA.
DR EMBL; CH471056; EAX04641.1; -; Genomic_DNA.
DR EMBL; BC001017; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC027870; AAH27870.1; -; mRNA.
DR CCDS; CCDS3844.1; -. [Q53GG5-1]
DR CCDS; CCDS47172.1; -. [Q53GG5-2]
DR RefSeq; NP_001107579.1; NM_001114107.4. [Q53GG5-2]
DR RefSeq; NP_055291.2; NM_014476.5. [Q53GG5-1]
DR AlphaFoldDB; Q53GG5; -.
DR BMRB; Q53GG5; -.
DR SMR; Q53GG5; -.
DR BioGRID; 118119; 23.
DR IntAct; Q53GG5; 10.
DR STRING; 9606.ENSP00000284770; -.
DR iPTMnet; Q53GG5; -.
DR PhosphoSitePlus; Q53GG5; -.
DR BioMuta; PDLIM3; -.
DR DMDM; 74740479; -.
DR EPD; Q53GG5; -.
DR jPOST; Q53GG5; -.
DR MassIVE; Q53GG5; -.
DR MaxQB; Q53GG5; -.
DR PaxDb; Q53GG5; -.
DR PeptideAtlas; Q53GG5; -.
DR PRIDE; Q53GG5; -.
DR ProteomicsDB; 62479; -. [Q53GG5-1]
DR ProteomicsDB; 62480; -. [Q53GG5-2]
DR ProteomicsDB; 62481; -. [Q53GG5-3]
DR Antibodypedia; 1500; 188 antibodies from 24 providers.
DR DNASU; 27295; -.
DR Ensembl; ENST00000284767.12; ENSP00000284767.8; ENSG00000154553.16. [Q53GG5-1]
DR Ensembl; ENST00000284771.7; ENSP00000284771.6; ENSG00000154553.16. [Q53GG5-2]
DR GeneID; 27295; -.
DR KEGG; hsa:27295; -.
DR MANE-Select; ENST00000284767.12; ENSP00000284767.8; NM_014476.6; NP_055291.2.
DR UCSC; uc003ixw.5; human. [Q53GG5-1]
DR CTD; 27295; -.
DR DisGeNET; 27295; -.
DR GeneCards; PDLIM3; -.
DR HGNC; HGNC:20767; PDLIM3.
DR HPA; ENSG00000154553; Group enriched (skeletal muscle, tongue).
DR MIM; 605889; gene.
DR neXtProt; NX_Q53GG5; -.
DR OpenTargets; ENSG00000154553; -.
DR PharmGKB; PA134970631; -.
DR VEuPathDB; HostDB:ENSG00000154553; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000156741; -.
DR InParanoid; Q53GG5; -.
DR OMA; IHAQFNT; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; Q53GG5; -.
DR TreeFam; TF106408; -.
DR PathwayCommons; Q53GG5; -.
DR SignaLink; Q53GG5; -.
DR BioGRID-ORCS; 27295; 5 hits in 1065 CRISPR screens.
DR ChiTaRS; PDLIM3; human.
DR GeneWiki; PDLIM3; -.
DR GenomeRNAi; 27295; -.
DR Pharos; Q53GG5; Tbio.
DR PRO; PR:Q53GG5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q53GG5; protein.
DR Bgee; ENSG00000154553; Expressed in skeletal muscle tissue of biceps brachii and 177 other tissues.
DR ExpressionAtlas; Q53GG5; baseline and differential.
DR Genevisible; Q53GG5; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
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 DisProt; DP01782; -.
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..364
FT /note="PDZ and LIM domain protein 3"
FT /id="PRO_0000075867"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 292..351
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HS7"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HS7"
FT VAR_SEQ 111..233
FT /note="DGNYFEHKHNIRPKPFVIPGRSSGCSTPSGIDCGSGRSTPSSVSTVSTICPG
FT DLKVAAKLAPNIPLEMELPGVKIVHAQFNTPMQLYSDDNIMETLQGQVSTALGETPLMS
FT EPTASVPPESDV -> EFKPIGTAHNRRAQPFVAAANIDDKRQVVSASYNSPIGLYSTS
FT NIQDALHGQLRGLIPSSPQKTGTTLNTSIIFGPNLS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_016500"
FT VAR_SEQ 111..224
FT /note="DGNYFEHKHNIRPKPFVIPGRSSGCSTPSGIDCGSGRSTPSSVSTVSTICPG
FT DLKVAAKLAPNIPLEMELPGVKIVHAQFNTPMQLYSDDNIMETLQGQVSTALGETPLMS
FT EPT -> EFKPIGTAHNRRAQPFVAAANIDDKRQVVSASYNSPIGLYSTSNIQDALHGQ
FT LRGLIPSSPQNEPT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9334352"
FT /id="VSP_016501"
FT VAR_SEQ 234..364
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_016502"
FT VARIANT 127
FT /note="V -> M (in dbSNP:rs11944325)"
FT /id="VAR_050166"
FT CONFLICT 12
FT /note="P -> A (in Ref. 1; AAC16670/AAC16672)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="A -> G (in Ref. 1; AAC16670/AAC16672)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="T -> I (in Ref. 1; AAC16670)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="S -> N (in Ref. 2; AAB96665)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="E -> R (in Ref. 1; AAC16670/AAC16672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39232 MW; 083802DF22D7A237 CRC64;
MPQTVILPGP APWGFRLSGG IDFNQPLVIT RITPGSKAAA ANLCPGDVIL AIDGFGTESM
THADAQDRIK AAAHQLCLKI DRGETHLWSP QVSEDGKAHP FKINLESEPQ DGNYFEHKHN
IRPKPFVIPG RSSGCSTPSG IDCGSGRSTP SSVSTVSTIC PGDLKVAAKL APNIPLEMEL
PGVKIVHAQF NTPMQLYSDD NIMETLQGQV STALGETPLM SEPTASVPPE SDVYRMLHDN
RNEPTQPRQS GSFRVLQGMV DDGSDDRPAG TRSVRAPVTK VHGGSGGAQR MPLCDKCGSG
IVGAVVKARD KYRHPECFVC ADCNLNLKQK GYFFIEGELY CETHARARTK PPEGYDTVTL
YPKA
