Q3TJD7 (PDLI7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
PDZ and LIM domain protein 7

Alternative name(s):
LIM mineralization protein
Short name=LMP
Protein enigma

Gene names

Name:	Pdlim7
Synonyms:	Enigma

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation e.g (embryonic flat bones mandible and cranium), and endochondral bone formation e.g (embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway By similarity.
Subunit structure	Specifically binds via its LIM zinc-binding 3 domain (LIM 3) domain to endocytic codes of INSR, but not with those of IGF1R, LDLR, TFRC, or EGFR. Interacts with various PKC isoforms through the LIM zinc-binding domains. Binds to RET in a phosphorylation-independent manner via its LIM zinc-binding domain 2 (LIM 2). Probably part of a complex with SHC and the RET dimer. Interacts with TPM2, TBX4 and TBX5 By similarity.
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity. Note: Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Co-localizes with TBX4 and TBX5 to actin filaments By similarity.
Developmental stage	At E13.5 expressed in epaxial, intercostal, and other skeletal muscles at the brachial level, including the latissimus dorsi muscle. Expressed in the intrinsic and extrinsic muscle mass of the tongue. At E15 expressed in mesenchymal tissue surrounding the cartilaginous anlage of immature bones, and in the future joint spaces. As endochondral ossification progresses, and the hypertrophic cartilage zone is replaced by mineralized bone, expression appears in the mineralizing portion of the bone. Expressed in mesoderm derived bones of the skull base and neural crest-derived endochondral bones such as the proximal mandible. Ref.3 Ref.4
Domain	The LIM zinc-binding 2 domain (LIM 2) interacts with TBX4 By similarity. The LIM zinc-binding 3 domain (LIM 3) provides the structural basis for recognition of tyrosine-containing tight turn structures. This domain is necessary and sufficient for interaction with TBX5 By similarity. Anchored to cell periphery via its N-terminal PDZ domain By similarity.
Sequence similarities	Contains 3 LIM zinc-binding domains. Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Biological process	Differentiation Osteogenesis
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from physical interaction. Source: MGI cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW ossification Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: MGI ruffle Inferred from direct assay. Source: MGI stress fiber Inferred from direct assay. Source: MGI
Molecular function	protein binding Inferred from physical interaction. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q3TJD7-1)

Also known as: LMP-1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q3TJD7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     94-133: ALTPPADPPRYTFAPSASLNKTARPFGAPPPTDSTLRQNG → VQTSDK
     191-222: SQVPRTEAPAPASTIPQESWPGPTTPSPTSRP → REKYVLELQSPRYTRLRDWHHQRSAHVLNVQS
     223-457: Missing.

Isoform 3 (identifier: Q3TJD7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     134-153: QLLRQPVPDASKQRLMEDTE → CRPLTNSCSDSRSPMPASSG
     154-457: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 457	457	PDZ and LIM domain protein 7		PRO_0000075882
Regions
	Domain	1 – 85	85	PDZ
	Domain	280 – 338	59	LIM zinc-binding 1
	Domain	339 – 398	60	LIM zinc-binding 2
	Domain	399 – 457	59	LIM zinc-binding 3
Amino acid modifications
	Modified residue	247	1	Phosphoserine By similarity
	Modified residue	251	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	94 – 133	40	ALTPP…LRQNG → VQTSDK in isoform 2.		VSP_016517
	Alternative sequence	134 – 153	20	QLLRQ…MEDTE → CRPLTNSCSDSRSPMPASSG in isoform 3.		VSP_016518
	Alternative sequence	154 – 457	304	Missing in isoform 3.		VSP_016519
	Alternative sequence	191 – 222	32	SQVPR…PTSRP → REKYVLELQSPRYTRLRDWH HQRSAHVLNVQS in isoform 2.		VSP_016520
	Alternative sequence	223 – 457	235	Missing in isoform 2.		VSP_016521
Experimental info
	Sequence conflict	85	1	Q → P in BAB22725. Ref.1
	Sequence conflict	151	1	D → G in AAH49565. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LMP-1) [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 8556AEBF1077D7F7	FASTA	457	50,119
	10 20 30 40 50 60 MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LNIDGENAGS 70 80 90 100 110 120 LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKALTPPAD PPRYTFAPSA SLNKTARPFG 130 140 150 160 170 180 APPPTDSTLR QNGQLLRQPV PDASKQRLME DTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ 190 200 210 220 230 240 DPDEEFMKKS SQVPRTEAPA PASTIPQESW PGPTTPSPTS RPPWAVDPAF AERYAPDKTS 250 260 270 280 290 300 TVLTRHSQPA TPTPLQNRTS IVQAAAGGGT GGGSNNGKTP VCHQCHKIIR GRYLVALGHA 310 320 330 340 350 360 YHPEEFVCSQ CGKVLEEGGF FEEKGAIFCP SCYDVRYAPN CAKCKKKITG EIMHALKMTW 370 380 390 400 410 420 HVHCFTCAAC KTPIRNRAFY MEEGAPYCER DYEKMFGTKC RGCDFKIDAG DRFLEALGFS 430 440 450 WHDTCFVCAI CQINLEGKTF YSKKDKPLCK SHAFSHV
	Isoform 2 [UniParc]. Checksum: 0AF16D8F9CBAADA0	FASTA	188	21,155
	10 20 30 40 50 60 MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LNIDGENAGS 70 80 90 100 110 120 LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKVQTSDKQ LLRQPVPDAS KQRLMEDTED 130 140 150 160 170 180 WRPRPGTGQS RSFRILAHLT GTEFMQDPDE EFMKKSREKY VLELQSPRYT RLRDWHHQRS AHVLNVQS
	Isoform 3 [UniParc]. Checksum: 07F1A40AC2B568BE	FASTA	153	16,036
	10 20 30 40 50 60 MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LNIDGENAGS 70 80 90 100 110 120 LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKALTPPAD PPRYTFAPSA SLNKTARPFG 130 140 150 APPPTDSTLR QNGCRPLTNS CSDSRSPMPA SSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-457 (ISOFORM 1). Strain: FVB/N. Tissue: Brain and Colon.
[3]	"LMP-1, a LIM-domain protein, mediates BMP-6 effects on bone formation." Boden S.D., Liu Y., Hair G.A., Helms J.A., Hu D., Racine M., Nanes M.S., Titus L. Endocrinology 139:5125-5134(1998) [PubMed: 9832452] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[4]	"The PDZ domain of the LIM protein enigma binds to beta-tropomyosin." Guy P.M., Kenny D.A., Gill G.N. Mol. Biol. Cell 10:1973-1984(1999) [PubMed: 10359609] [Abstract] Cited for: DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK003338 mRNA. Translation: BAB22725.1. AK010141 mRNA. Translation: BAB26726.1. AK003019 mRNA. Translation: BAC25017.1. AK167476 mRNA. Translation: BAE39558.1. BC045528 mRNA. Translation: AAH45528.1. BC049565 mRNA. Translation: AAH49565.1.
IPI	IPI00130607. IPI00315878. IPI00404528.
RefSeq	NP_001107559.1. NM_001114087.1. NP_001107560.1. NM_001114088.1. NP_080407.3. NM_026131.3.
UniGene	Mm.275648.
3D structure databases
ProteinModelPortal	Q3TJD7.
SMR	Q3TJD7. Positions 1-84, 274-455.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3TJD7.
PTM databases
PhosphoSite	Q3TJD7.
Proteomic databases
PRIDE	Q3TJD7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000046246; ENSMUSP00000047173; ENSMUSG00000021493. ENSMUST00000069929; ENSMUSP00000064219; ENSMUSG00000021493. ENSMUST00000109909; ENSMUSP00000105535; ENSMUSG00000021493. ENSMUST00000155098; ENSMUSP00000120465; ENSMUSG00000021493.
GeneID	67399.
KEGG	mmu:67399.
Organism-specific databases
CTD	9260.
MGI	MGI:1914649. Pdlim7.
Phylogenomic databases
eggNOG	roNOG16727.
GeneTree	ENSGT00600000084390.
HOGENOM	HBG505271.
HOVERGEN	HBG051478.
InParanoid	Q3TJD7.
OMA	RPLCKSH.
Gene expression databases
ArrayExpress	Q3TJD7.
Bgee	Q3TJD7.
CleanEx	MM_PDLIM7.
Genevestigator	Q3TJD7.
GermOnline	ENSMUSG00000021493. Mus musculus.
Family and domain databases
InterPro	IPR001478. PDZ/DHR/GLGF. IPR001781. Znf_LIM. [Graphical view]
Gene3D	G3DSA:2.10.110.10. Znf_LIM. 3 hits.
Pfam	PF00412. LIM. 3 hits. PF00595. PDZ. 1 hit. [Graphical view]
SMART	SM00132. LIM. 3 hits. SM00228. PDZ. 1 hit. [Graphical view]
SUPFAM	SSF50156. PDZ. 1 hit.
PROSITE	PS00478. LIM_DOMAIN_1. 2 hits. PS50023. LIM_DOMAIN_2. 3 hits. PS50106. PDZ. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	324470.
SOURCE	Search...

Entry information

Entry name

PDLI7_MOUSE

Accession

Primary (citable) accession number: Q3TJD7
Secondary accession number(s): Q80ZY6 , Q810S3, Q8C1S4, Q9CRA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	October 11, 2005
Last modified:	September 21, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program