O70209 (PDLI3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
PDZ and LIM domain protein 3

Alternative name(s):
Actinin-associated LIM protein
Alpha-actinin-2-associated LIM protein

Gene names

Name:

Pdlim3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in the organization of actin filament arrays within muscle cells By similarity.
Subunit structure	Interacts with ACTN2 By similarity.
Subcellular location	Cytoplasm › myofibril › sarcomere › Z line By similarity. Note: Localizes to myofiber Z-lines By similarity.
Developmental stage	At E15 highly expressed in skeletal muscle and heart. Ref.1
Sequence similarities	Contains 1 LIM zinc-binding domain. Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	LIM domain
Ligand	Metal-binding Zinc
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Inferred from direct assay PubMed 11329061. Source: MGI heart development Inferred from mutant phenotype PubMed 11329061. Source: MGI
Cellular_component	Z disc Traceable author statement PubMed 11238905. Source: MGI actin cytoskeleton Inferred from physical interaction PubMed 11329061. Source: MGI
Molecular_function	structural constituent of muscle Inferred from direct assay PubMed 11238905. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 316

316

PDZ and LIM domain protein 3

PRO_0000075868

Regions

Domain

1 – 84

84

PDZ

Domain

244 – 303

60

LIM zinc-binding

Secondary structure

1

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316

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Beta strand

18 – 20

3

Turn

21 – 24

4

Beta strand

25 – 28

4

Beta strand

34 – 36

3

Helix

39 – 41

3

Beta strand

48 – 52

5

Helix

62 – 69

8

Beta strand

74 – 77

4

Turn

84 – 87

4

Turn

247 – 249

3

Beta strand

258 – 262

5

Turn

267 – 269

3

Beta strand

273 – 275

3

Turn

279 – 281

3

Beta strand

285 – 287

3

Beta strand

290 – 292

3

Helix

294 – 300

7

Sequences

	Sequence		Length	Mass (Da)
	O70209 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: E59916D0BC430B6F	FASTA	316	34,300
	10 20 30 40 50 60 MPQNVVLPGP APWGFRLSGG IDFNQPLVIT RITPGSKAAA ANLCPGDVIL AIDGFGTESM 70 80 90 100 110 120 THADAQDRIK AASYQLCLKI DRAETRLWSP QVSEDGKAHP FKINLEAEPQ EFKPIGTAHN 130 140 150 160 170 180 RRAQPFVAAA NIDDKRQVVS ASYNSPIGLY STSNIQDALH GQLRGLIPGS LQNEPTASVP 190 200 210 220 230 240 PQSDVYRMLH DNRDDPAAPR QSGSFRVLQD LVNDGPDDRP AGTRSVRAPV TKVHGGAGSA 250 260 270 280 290 300 QRMPLCDKCG SGIVGAVVKA RDKYRHPECF VCADCNLNLK QKGYFFVEGE LYCETHARAR 310 TRPPEGYDTV TLYPKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs." Xia H., Winokur S.T., Kuo W.-L., Altherr M.R., Bredt D.S. J. Cell Biol. 139:507-515(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE. Tissue: Skeletal muscle.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Wolffian duct.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	"Solution structure of PDZ and LIM domains of mouse alpha-actinin-2 associated LIM protein." RIKEN structural genomics initiative (RSGI) Submitted (MAY-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 4-93, OF 226-301 IN COMPLEX WITH ZINC IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF002283 mRNA. Translation: AAC16673.1.
AK078421 mRNA. Translation: BAC37266.1.
BC070418 mRNA. Translation: AAH70418.1.

IPI

IPI00116347.

RefSeq

NP_058078.1. NM_016798.3.

UniGene

Mm.282900.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V5L	NMR	-	A	4-93	[»]
1X64	NMR	-	A	226-301	[»]

ProteinModelPortal

O70209.

SMR

O70209. Positions 4-93, 221-304.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000034053.

PTM databases

PhosphoSite

O70209.

2D gel databases

REPRODUCTION-2DPAGE

IPI00116347.

Proteomic databases

PaxDb

O70209.

PRIDE

O70209.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034053; ENSMUSP00000034053; ENSMUSG00000031636.

GeneID

53318.

KEGG

mmu:53318.

UCSC

uc009lpl.1. mouse.

Organism-specific databases

CTD

27295.

MGI

MGI:1859274. Pdlim3.

Phylogenomic databases

eggNOG

NOG258467.

GeneTree

ENSGT00590000082980.

HOGENOM

HOG000290704.

HOVERGEN

HBG061371.

InParanoid

O70209.

OMA

SMSEPTA.

OrthoDB

EOG4DR9CT.

Gene expression databases

Bgee

O70209.

CleanEx

MM_PDLIM3.

Genevestigator

O70209.

GermOnline

ENSMUSG00000031636. Mus musculus.

Family and domain databases

Gene3D

2.10.110.10. 1 hit.

InterPro

IPR001478. PDZ.
IPR006643. ZASP.
IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]

SMART

SM00132. LIM. 1 hit.
SM00228. PDZ. 1 hit.
SM00735. ZM. 1 hit.
[Graphical view]

SUPFAM

SSF50156. PDZ. 1 hit.

PROSITE

PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O70209.

NextBio

310113.

SOURCE

Search...

Entry information

Entry name

PDLI3_MOUSE

Accession

Primary (citable) accession number: O70209

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	August 1, 1998
Last modified:	April 3, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program