PDLI7_MOUSE
ID PDLI7_MOUSE Reviewed; 457 AA.
AC Q3TJD7; Q80ZY6; Q810S3; Q8C1S4; Q9CRA1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=PDZ and LIM domain protein 7;
DE AltName: Full=LIM mineralization protein;
DE Short=LMP;
DE AltName: Full=Protein enigma;
GN Name=Pdlim7; Synonyms=Enigma;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 305-457 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Brain, and Colon;
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 DEVELOPMENTAL STAGE.
RX PubMed=9832452; DOI=10.1210/endo.139.12.6392;
RA Boden S.D., Liu Y., Hair G.A., Helms J.A., Hu D., Racine M., Nanes M.S.,
RA Titus L.;
RT "LMP-1, a LIM-domain protein, mediates BMP-6 effects on bone formation.";
RL Endocrinology 139:5125-5134(1998).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=10359609; DOI=10.1091/mbc.10.6.1973;
RA Guy P.M., Kenny D.A., Gill G.N.;
RT "The PDZ domain of the LIM protein enigma binds to beta-tropomyosin.";
RL Mol. Biol. Cell 10:1973-1984(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: May function as a scaffold on which the coordinated assembly
CC of proteins can occur. May play a role as an adapter that, via its PDZ
CC domain, localizes LIM-binding proteins to actin filaments of both
CC skeletal muscle and nonmuscle tissues. Involved in both of the two
CC fundamental mechanisms of bone formation, direct bone formation (e.g.
CC embryonic flat bones mandible and cranium), and endochondral bone
CC formation (e.g. embryonic long bone development). Plays a role during
CC fracture repair. Involved in BMP6 signaling pathway (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Specifically binds via its LIM zinc-binding 3 domain (LIM 3)
CC domain to endocytic codes of INSR, but not with those of IGF1R, LDLR,
CC TFRC, or EGFR. Interacts with various PKC isoforms through the LIM
CC zinc-binding domains. Binds to RET in a phosphorylation-independent
CC manner via its LIM zinc-binding domain 2 (LIM 2). Probably part of a
CC complex with SHC and the RET dimer. Interacts with TPM2, TBX4 and TBX5
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Colocalizes with RET to the cell periphery and in
CC some cytoskeletal components. Colocalizes with TPM2 near the Z line in
CC muscle. Colocalizes with TBX4 and TBX5 to actin filaments (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=LMP-1;
CC IsoId=Q3TJD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TJD7-2; Sequence=VSP_016517, VSP_016520, VSP_016521;
CC Name=3;
CC IsoId=Q3TJD7-3; Sequence=VSP_016518, VSP_016519;
CC -!- DEVELOPMENTAL STAGE: At 13.5 dpc expressed in epaxial, intercostal, and
CC other skeletal muscles at the brachial level, including the latissimus
CC dorsi muscle. Expressed in the intrinsic and extrinsic muscle mass of
CC the tongue. At 15 dpc expressed in mesenchymal tissue surrounding the
CC cartilaginous anlage of immature bones, and in the future joint spaces.
CC As endochondral ossification progresses, and the hypertrophic cartilage
CC zone is replaced by mineralized bone, expression appears in the
CC mineralizing portion of the bone. Expressed in mesoderm derived bones
CC of the skull base and neural crest-derived endochondral bones such as
CC the proximal mandible. {ECO:0000269|PubMed:10359609,
CC ECO:0000269|PubMed:9832452}.
CC -!- DOMAIN: The LIM zinc-binding 2 domain (LIM 2) interacts with TBX4.
CC {ECO:0000250}.
CC -!- DOMAIN: The LIM zinc-binding 3 domain (LIM 3) provides the structural
CC basis for recognition of tyrosine-containing tight turn structures.
CC This domain is necessary and sufficient for interaction with TBX5 (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: Anchored to cell periphery via its N-terminal PDZ domain.
CC {ECO:0000250}.
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DR EMBL; AK003338; BAB22725.1; -; mRNA.
DR EMBL; AK010141; BAB26726.1; -; mRNA.
DR EMBL; AK003019; BAC25017.1; -; mRNA.
DR EMBL; AK167476; BAE39558.1; -; mRNA.
DR EMBL; BC045528; AAH45528.1; -; mRNA.
DR EMBL; BC049565; AAH49565.1; -; mRNA.
DR CCDS; CCDS26547.1; -. [Q3TJD7-2]
DR CCDS; CCDS49275.1; -. [Q3TJD7-1]
DR RefSeq; NP_001107560.1; NM_001114088.2. [Q3TJD7-1]
DR RefSeq; NP_080407.3; NM_026131.4. [Q3TJD7-2]
DR AlphaFoldDB; Q3TJD7; -.
DR BioGRID; 212162; 4.
DR STRING; 10090.ENSMUSP00000047173; -.
DR iPTMnet; Q3TJD7; -.
DR PhosphoSitePlus; Q3TJD7; -.
DR EPD; Q3TJD7; -.
DR jPOST; Q3TJD7; -.
DR MaxQB; Q3TJD7; -.
DR PaxDb; Q3TJD7; -.
DR PeptideAtlas; Q3TJD7; -.
DR PRIDE; Q3TJD7; -.
DR ProteomicsDB; 287992; -. [Q3TJD7-1]
DR ProteomicsDB; 287993; -. [Q3TJD7-2]
DR ProteomicsDB; 287994; -. [Q3TJD7-3]
DR Antibodypedia; 17442; 150 antibodies from 23 providers.
DR DNASU; 67399; -.
DR Ensembl; ENSMUST00000046246; ENSMUSP00000047173; ENSMUSG00000021493. [Q3TJD7-1]
DR Ensembl; ENSMUST00000069929; ENSMUSP00000064219; ENSMUSG00000021493. [Q3TJD7-2]
DR Ensembl; ENSMUST00000155098; ENSMUSP00000120465; ENSMUSG00000021493. [Q3TJD7-1]
DR GeneID; 67399; -.
DR KEGG; mmu:67399; -.
DR UCSC; uc007qrg.3; mouse. [Q3TJD7-1]
DR UCSC; uc007qri.3; mouse. [Q3TJD7-2]
DR CTD; 9260; -.
DR MGI; MGI:1914649; Pdlim7.
DR VEuPathDB; HostDB:ENSMUSG00000021493; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000159626; -.
DR HOGENOM; CLU_001357_8_1_1; -.
DR InParanoid; Q3TJD7; -.
DR OMA; ACKVPIR; -.
DR OrthoDB; 1013114at2759; -.
DR PhylomeDB; Q3TJD7; -.
DR TreeFam; TF106408; -.
DR Reactome; R-MMU-8853659; RET signaling.
DR BioGRID-ORCS; 67399; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Pdlim7; mouse.
DR PRO; PR:Q3TJD7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3TJD7; protein.
DR Bgee; ENSMUSG00000021493; Expressed in hindlimb stylopod muscle and 215 other tissues.
DR ExpressionAtlas; Q3TJD7; baseline and differential.
DR Genevisible; Q3TJD7; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
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; IPI:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; LIM domain; Metal-binding; Methylation; Osteogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..457
FT /note="PDZ and LIM domain protein 7"
FT /id="PRO_0000075882"
FT DOMAIN 1..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 280..338
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 339..398
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 399..457
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 82..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR12"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Z9"
FT MOD_RES 103
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR12"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR12"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 94..133
FT /note="ALTPPADPPRYTFAPSASLNKTARPFGAPPPTDSTLRQNG -> VQTSDK
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016517"
FT VAR_SEQ 134..153
FT /note="QLLRQPVPDASKQRLMEDTE -> CRPLTNSCSDSRSPMPASSG (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016518"
FT VAR_SEQ 154..457
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016519"
FT VAR_SEQ 191..222
FT /note="SQVPRTEAPAPASTIPQESWPGPTTPSPTSRP -> REKYVLELQSPRYTRL
FT RDWHHQRSAHVLNVQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016520"
FT VAR_SEQ 223..457
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016521"
FT CONFLICT 85
FT /note="Q -> P (in Ref. 1; BAB22725)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="D -> G (in Ref. 2; AAH49565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 50119 MW; 8556AEBF1077D7F7 CRC64;
MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LNIDGENAGS
LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKALTPPAD PPRYTFAPSA SLNKTARPFG
APPPTDSTLR QNGQLLRQPV PDASKQRLME DTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ
DPDEEFMKKS SQVPRTEAPA PASTIPQESW PGPTTPSPTS RPPWAVDPAF AERYAPDKTS
TVLTRHSQPA TPTPLQNRTS IVQAAAGGGT GGGSNNGKTP VCHQCHKIIR GRYLVALGHA
YHPEEFVCSQ CGKVLEEGGF FEEKGAIFCP SCYDVRYAPN CAKCKKKITG EIMHALKMTW
HVHCFTCAAC KTPIRNRAFY MEEGAPYCER DYEKMFGTKC RGCDFKIDAG DRFLEALGFS
WHDTCFVCAI CQINLEGKTF YSKKDKPLCK SHAFSHV
