PDLI1_MOUSE
ID PDLI1_MOUSE Reviewed; 327 AA.
AC O70400; Q99K93;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=PDZ and LIM domain protein 1;
DE AltName: Full=C-terminal LIM domain protein 1;
DE AltName: Full=Elfin;
DE AltName: Full=LIM domain protein CLP-36;
GN Name=Pdlim1; Synonyms=Clim1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11596114; DOI=10.1002/jcb.1244;
RA Kotaka M., Lau Y.-M., Cheung K.-K., Lee S.M.Y., Li H.-Y., Chan W.-Y.,
RA Fung K.-P., Lee C.-Y., Waye M.M.Y., Tsui S.K.W.;
RT "Elfin is expressed during early heart development.";
RL J. Cell. Biochem. 83:463-472(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD; TISSUE=Skin, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-130, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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, cytoskeleton
CC {ECO:0000269|PubMed:11596114}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:O00151}. Note=Associates with the actin stress
CC fibers (PubMed:11596114).
CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, spleen, testis and
CC skeletal muscle. {ECO:0000269|PubMed:11596114}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout the developing heart.
CC {ECO:0000269|PubMed:11596114}.
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DR EMBL; AF053367; AAC08436.1; -; mRNA.
DR EMBL; AK076285; BAC36288.1; -; mRNA.
DR EMBL; AK088089; BAC40138.1; -; mRNA.
DR EMBL; AK146225; BAE26993.1; -; mRNA.
DR EMBL; BC004809; AAH04809.1; -; mRNA.
DR CCDS; CCDS37977.1; -.
DR RefSeq; NP_058557.2; NM_016861.4.
DR AlphaFoldDB; O70400; -.
DR SMR; O70400; -.
DR BioGRID; 207571; 6.
DR CORUM; O70400; -.
DR STRING; 10090.ENSMUSP00000064545; -.
DR iPTMnet; O70400; -.
DR PhosphoSitePlus; O70400; -.
DR SwissPalm; O70400; -.
DR CPTAC; non-CPTAC-3992; -.
DR EPD; O70400; -.
DR jPOST; O70400; -.
DR MaxQB; O70400; -.
DR PaxDb; O70400; -.
DR PeptideAtlas; O70400; -.
DR PRIDE; O70400; -.
DR ProteomicsDB; 288023; -.
DR Antibodypedia; 1897; 413 antibodies from 40 providers.
DR DNASU; 54132; -.
DR Ensembl; ENSMUST00000068439; ENSMUSP00000064545; ENSMUSG00000055044.
DR GeneID; 54132; -.
DR KEGG; mmu:54132; -.
DR UCSC; uc008hkk.2; mouse.
DR CTD; 9124; -.
DR MGI; MGI:1860611; Pdlim1.
DR VEuPathDB; HostDB:ENSMUSG00000055044; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000155525; -.
DR HOGENOM; CLU_038114_1_1_1; -.
DR InParanoid; O70400; -.
DR OMA; EPQEVKH; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; O70400; -.
DR TreeFam; TF106408; -.
DR BioGRID-ORCS; 54132; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Pdlim1; mouse.
DR PRO; PR:O70400; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O70400; protein.
DR Bgee; ENSMUSG00000055044; Expressed in ileum and 105 other tissues.
DR ExpressionAtlas; O70400; baseline and differential.
DR Genevisible; O70400; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
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:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISO:MGI.
DR GO; GO:0010761; P:fibroblast migration; ISO:MGI.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0030011; P:maintenance of cell polarity; ISO:MGI.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0043149; P:stress fiber assembly; ISO:MGI.
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 1: Evidence at protein 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..327
FT /note="PDZ and LIM domain protein 1"
FT /id="PRO_0000075860"
FT DOMAIN 3..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 256..315
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 161..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 308
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:0007744|PubMed:21183079"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT MOD_RES 319
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00151"
FT CONFLICT 21
FT /note="Missing (in Ref. 1; AAC08436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 35774 MW; 8A5EDA47F2E90C03 CRC64;
MTTQQIVLQG PGPWGFRLVG GKDFEQPLAI SRVTPGSKAA IANLCIGDLI TAIDGEDTSS
MTHLEAQNKI KGCADNMTLT VSRSEQKIWS PLVTEEGKRH PYKMNLASEP QEVLHIGSAH
NRSAMPFTAS PAPSTRVITN QYNSPTGLYS SENISNFNNA VESKTSASGE EANSRPVVQP
HPSGSLIIDK DSEVYKMLQE KQELNEPPKQ STSFLVLQEI LESDGKGDPN KPSGFRSVKA
PVTKVAASVG NAQKLPICDK CGTGIVGVFV KLRDHHRHPE CYVCTDCGIN LKQKGHFFVE
DQIYCEKHAR ERVTPPEGYD VVTVFRE
