PDLI7_RAT
ID PDLI7_RAT Reviewed; 457 AA.
AC Q9Z1Z9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
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, Lim1;
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], FUNCTION IN BONE FORMATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC TISSUE=Bone;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 INTERACTION WITH SIPA1L1, AND SUBCELLULAR LOCATION.
RX PubMed=19900557; DOI=10.1016/j.mcn.2009.10.009;
RA Herrick S., Evers D.M., Lee J.Y., Udagawa N., Pak D.T.;
RT "Postsynaptic PDLIM5/Enigma homolog binds SPAR and causes dendritic spine
RT shrinkage.";
RL Mol. Cell. Neurosci. 43:188-200(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96, AND IDENTIFICATION BY
RP 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 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.
CC {ECO:0000269|PubMed:9832452}.
CC -!- SUBUNIT: Binds via its LIM zinc-binding 3 domain (LIM 3) domain to
CC endocytic codes of INSR, but not with those of IGF1R, LDLR, TFRC, or
CC EGFR. Interacts with various PKC isoforms through the LIM zinc-binding
CC domains. Binds to RET in a phosphorylation-independent manner via its
CC LIM zinc-binding 2 domain (LIM 2). Probably part of a complex with SHC
CC and the RET dimer. Interacts with TPM2, TBX4 and TBX5 (By similarity).
CC Interacts (via LIM domains) with SIPA1L1. {ECO:0000250,
CC ECO:0000269|PubMed:19900557}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19900557}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with RET to the
CC cell periphery and in some cytoskeletal components. Colocalizes with
CC TPM2 near the Z line in muscle. Colocalizes with TBX4 and TBX5 to actin
CC filaments (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, heart, brain, lung, and
CC skeletal muscle. Overexpression results in the synthesis of an
CC unidentified soluble factor which acts on cells in the osteoblast
CC lineage causing them to differentiate and secrete BMP-2.
CC {ECO:0000269|PubMed:9832452}.
CC -!- DEVELOPMENTAL STAGE: At E14 expressed in mesenchymal tissue surrounding
CC the cartilaginous anlage of immature bones, and in the future joint
CC spaces. As endochondral ossification progresses, and the hypertrophic
CC cartilage zone is replaced by mineralized bone, expression appears in
CC the mineralizing portion of the bone. Expressed in mesoderm derived
CC bones of the skull base and neural crest-derived endochondral bones
CC such as the proximal mandible. {ECO:0000269|PubMed:9832452}.
CC -!- INDUCTION: Induced by glucocorticoid or BMP6.
CC -!- DOMAIN: The LIM zinc-binding 2 (LIM 2) interacts with TBX4.
CC {ECO:0000250}.
CC -!- DOMAIN: The LIM zinc-binding 3 (LIM 3) domain 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; AF095585; AAD13197.1; -; mRNA.
DR EMBL; BC078693; AAH78693.1; -; mRNA.
DR RefSeq; NP_775148.1; NM_173125.1.
DR RefSeq; XP_017455959.1; XM_017600470.1.
DR AlphaFoldDB; Q9Z1Z9; -.
DR IntAct; Q9Z1Z9; 1.
DR STRING; 10116.ENSRNOP00000018899; -.
DR iPTMnet; Q9Z1Z9; -.
DR PhosphoSitePlus; Q9Z1Z9; -.
DR jPOST; Q9Z1Z9; -.
DR PaxDb; Q9Z1Z9; -.
DR PRIDE; Q9Z1Z9; -.
DR GeneID; 286908; -.
DR KEGG; rno:286908; -.
DR UCSC; RGD:628769; rat.
DR CTD; 9260; -.
DR RGD; 628769; Pdlim7.
DR VEuPathDB; HostDB:ENSRNOG00000013653; -.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_001357_8_1_1; -.
DR InParanoid; Q9Z1Z9; -.
DR OMA; ACKVPIR; -.
DR OrthoDB; 1013114at2759; -.
DR PhylomeDB; Q9Z1Z9; -.
DR TreeFam; TF106408; -.
DR Reactome; R-RNO-8853659; RET signaling.
DR PRO; PR:Q9Z1Z9; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000013653; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; Q9Z1Z9; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
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; ISO:RGD.
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; IDA:RGD.
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 Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
KW LIM domain; Metal-binding; Methylation; Osteogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..457
FT /note="PDZ and LIM domain protein 7"
FT /id="PRO_0000075883"
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 81..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..226
FT /note="Disordered"
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:0007744|PubMed:22673903"
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:0000250|UniProtKB:Q9NR12"
SQ SEQUENCE 457 AA; 49913 MW; B4EE3142D5A90D72 CRC64;
MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGS
LTHIEAQNKI RACGERLSLG LSRAQPAQSK PQKALTPPAD PPRYTFAPSA SLNKTARPFG
APPPTDSALS QNGQLLRQLV PDASKQRLME NTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ
DPDEEFMKKS SQVPRTEAPA PASTIPQESW PGPTTPSPTS RPPWAVDPAF AERYAPDKTS
TVLTRHSQPA TPTPLQNRTS IVQAAAGGGT GGGSNNGKTP VCHQCHKIIR GRYLVALGHA
YHPEEFVCSQ CGKVLEEGGF FEEKGAIFCP SCYDVRYAPS CAKCKKKITG EIMHALKMTW
HVPCFTCAAC KTPIRNRAFY MEEGAPYCER DYEKMFGTKC RGCDFKIDAG DRFLEALGFS
WHDTCFVCAI CQINLEGKTF YSKKDKPLCK SHAFSHV
