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   24-JAN-2024, entry version 182.
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,
RC   Spleen, 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   GlyGen; O70400; 6 sites, 1 O-linked glycan (6 sites).
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; 10090-ENSMUSP00000064545; -.
DR   PeptideAtlas; O70400; -.
DR   ProteomicsDB; 288023; -.
DR   Pumba; O70400; -.
DR   Antibodypedia; 1897; 457 antibodies from 40 providers.
DR   DNASU; 54132; -.
DR   Ensembl; ENSMUST00000068439.13; ENSMUSP00000064545.6; ENSMUSG00000055044.13.
DR   GeneID; 54132; -.
DR   KEGG; mmu:54132; -.
DR   UCSC; uc008hkk.2; mouse.
DR   AGR; MGI:1860611; -.
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; QIYCETH; -.
DR   OrthoDB; 370973at2759; -.
DR   PhylomeDB; O70400; -.
DR   TreeFam; TF106408; -.
DR   BioGRID-ORCS; 54132; 3 hits in 77 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 108 other cell types or tissues.
DR   ExpressionAtlas; O70400; baseline and differential.
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   CDD; cd09448; LIM_CLP36; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR   InterPro; IPR031847; PDLI1-4/Zasp-like_mid.
DR   InterPro; IPR028537; PDLIM1_LIM.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR006643; Zasp-like_motif.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24214:SF5; PDZ AND LIM DOMAIN PROTEIN 1; 1.
DR   PANTHER; PTHR24214; PDZ AND LIM DOMAIN PROTEIN ZASP; 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   Genevisible; O70400; MM.
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
//