P63168 (DYL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynein light chain 1, cytoplasmic

Alternative name(s):
8 kDa dynein light chain
Short name=DLC8
Dynein light chain LC8-type 1
Protein inhibitor of neuronal nitric oxide synthase
Short name=PIN
Short name=mPIN

Gene names

Name:	Dynll1
Synonyms:	Dlc1, Dncl1, Dnclc1

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	89 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures By similarity. Binds and inhibits the catalytic activity of neuronal nitric oxide synthase By similarity. Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1 By similarity. Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity By similarity.
Subunit structure	Homodimer. Monomer; the monomeric form is incapable of binding to target proteins. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with TXNDC17. Interacts with WWC1 and ESR1. The interaction with WWC1 is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin. Interacts with BCL2L11. Interacts with BCL2; the interaction is greatly enhanced in the nucleus and in mitochondria upon induction of apoptosis. Interacts with PAK1; the interaction requires dimeric DYNLL1 By similarity. Interacts with MYZAP By similarity. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGOL2 By similarity. Interacts with ATMIN; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN By similarity. Ref.4
Subcellular location	Cytoplasm › cytoskeleton By similarity. Nucleus By similarity. Mitochondrion By similarity.
Post-translational modification	Phosphorylation at Ser-88 appears to control the dimer-monomer transition By similarity.
Sequence similarities	Belongs to the dynein light chain family.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation Transport
Cellular component	Cytoplasm Cytoskeleton Dynein Microtubule Mitochondrion Nucleus
Molecular function	Activator Motor protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based movement Traceable author statement PubMed 8702622. Source: MGI negative regulation of phosphorylation Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara cytoplasmic dynein complex Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from direct assay PubMed 15136728. Source: MGI kinetochore Inferred from sequence or structural similarity. Source: UniProtKB membrane Inferred from direct assay PubMed 15136728. Source: MGI microtubule Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell mitotic spindle Inferred from sequence or structural similarity. Source: UniProtKB signalosome Inferred from electronic annotation. Source: Compara
Molecular_function	motor activity Inferred from electronic annotation. Source: UniProtKB-KW nitric-oxide synthase regulator activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAX6	P26367	3	EBI-349121,EBI-747278	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 89	89	Dynein light chain 1, cytoplasmic		PRO_0000195127
Regions
	Region	67 – 89	23	Interaction with ESR1 By similarity
Amino acid modifications
	Modified residue	36	1	N6-acetyllysine By similarity
	Modified residue	88	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P63168 [UniParc]. Last modified September 27, 2004. Version 1. Checksum: F5E7647D092BEB3A	FASTA	89	10,366
	10 20 30 40 50 60 MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR 70 80 NFGSYVTHET KHFIYFYLGQ VAILLFKSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Intra-renal localization of mPIN (Protein Inhibitor of Nitric oxide synthase)." Mount D.B. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[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: Hippocampus and Kidney.
[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: FVB/N. Tissue: Mammary tumor.
[4]	"Identification of a novel Bcl-2-interacting mediator of cell death (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in rapid ischemic tolerance-induced neuroprotection." Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P., Henshall D.C., Morris K.T., Simon R.P., Meller R. J. Biol. Chem. 286:19331-19339(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BCL2L11.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF020185 mRNA. Translation: AAD01643.1. AK002522 mRNA. Translation: BAB22160.1. AK010614 mRNA. Translation: BAB27063.1. AK010685 mRNA. Translation: BAB27117.1. AK013721 mRNA. Translation: BAB28970.1. AK082923 mRNA. Translation: BAC38691.1. AK147977 mRNA. Translation: BAE28262.1. BC008106 mRNA. Translation: AAH08106.1. BC034258 mRNA. Translation: AAH34258.1.
IPI	IPI00121623.
RefSeq	NP_062656.3. NM_019682.4.
UniGene	Mm.256858.
3D structure databases
ProteinModelPortal	P63168.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63168. 70 interactions.
MINT	MINT-1858885.
PTM databases
PhosphoSite	P63168.
Proteomic databases
PaxDb	P63168.
PRIDE	P63168.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000009157; ENSMUSP00000009157; ENSMUSG00000009013. ENSMUST00000112090; ENSMUSP00000107720; ENSMUSG00000009013.
GeneID	56455.
KEGG	mmu:56455.
UCSC	uc007kva.2. mouse.
Organism-specific databases
CTD	8655.
MGI	MGI:1861457. Dynll1.
Phylogenomic databases
eggNOG	NOG312371.
GeneTree	ENSGT00390000000378.
HOVERGEN	HBG002133.
InParanoid	P63168.
KO	K10418.
OMA	LAILIWK.
OrthoDB	EOG473PSW.
Gene expression databases
Bgee	P63168.
CleanEx	MM_DLC1. MM_DYNLL1.
Genevestigator	P63168.
GermOnline	ENSMUSG00000009013. Mus musculus.
Family and domain databases
Gene3D	3.30.740.10. 1 hit.
InterPro	IPR019763. Dynein_light_1/2_CS. IPR001372. Dynein_light_chain_typ-1/2. [Graphical view]
PANTHER	PTHR11886. PTHR11886. 1 hit.
Pfam	PF01221. Dynein_light. 1 hit. [Graphical view]
SUPFAM	SSF54648. Dynein_light_chain_typ-1/2. 1 hit.
PROSITE	PS01239. DYNEIN_LIGHT_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	312686.
SOURCE	Search...

Entry information

Entry name

DYL1_MOUSE

Accession

Primary (citable) accession number: P63168
Secondary accession number(s): Q15701, Q3UGE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	September 27, 2004
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program