Full text data of DYNLL2
DYNLL2
(DLC2)
[Confidence: low (only semi-automatic identification from reviews)]
Dynein light chain 2, cytoplasmic (8 kDa dynein light chain b; DLC8b; Dynein light chain LC8-type 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Dynein light chain 2, cytoplasmic (8 kDa dynein light chain b; DLC8b; Dynein light chain LC8-type 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96FJ2
ID DYL2_HUMAN Reviewed; 89 AA.
AC Q96FJ2; B2R5B4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Dynein light chain 2, cytoplasmic;
DE AltName: Full=8 kDa dynein light chain b;
DE Short=DLC8b;
DE AltName: Full=Dynein light chain LC8-type 2;
GN Name=DYNLL2; Synonyms=DLC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang H.L., Yu L., Yang J., Fu Q., Cui Y.Y., Zhao S.Y.;
RT "Cloning and sequencing of a novel human cDNA homologous to Rattus
RT norvegicus protein inhibitor of neuronal nitric oxide synthase (PIN)
RT mRNA.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory
CC components of the cytoplasmic dynein 1 complex that are thought to
CC be involved in linking dynein to cargos and to adapter proteins
CC that regulate dynein function. Cytoplasmic dynein 1 acts as a
CC motor for the intracellular retrograde motility of vesicles and
CC organelles along microtubules. May play a role in changing or
CC maintaining the spatial distribution of cytoskeletal structures
CC (By similarity).
CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of
CC two catalytic heavy chains (HCs) and a number of non-catalytic
CC subunits which present intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs); the composition
CC seems to vary in respect to the IC, LIC and LC composition. The
CC heavy chain homodimer serves as a scaffold for the probable
CC homodimeric assembly of the respective non-catalytic subunits.
CC Dynein ICs and LICs bind directly to the HC dimer and the LCs
CC assemble on the IC dimer. Interacts with DYNC1I1. Interacts with
CC BMF. Component of the myosin V motor complex. Interacts with
CC rabies virus phosphoprotein (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- SIMILARITY: Belongs to the dynein light chain family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF112997; AAP97230.1; -; mRNA.
DR EMBL; AK312125; BAG35061.1; -; mRNA.
DR EMBL; CH471109; EAW94484.1; -; Genomic_DNA.
DR EMBL; BC010744; AAH10744.1; -; mRNA.
DR RefSeq; NP_542408.1; NM_080677.2.
DR UniGene; Hs.720595; -.
DR PDB; 2XQQ; X-ray; 1.31 A; A/B/C/D=1-89.
DR PDB; 3P8M; X-ray; 2.90 A; A/B=1-89.
DR PDBsum; 2XQQ; -.
DR PDBsum; 3P8M; -.
DR ProteinModelPortal; Q96FJ2; -.
DR SMR; Q96FJ2; 1-89.
DR IntAct; Q96FJ2; 21.
DR MINT; MINT-1473886; -.
DR STRING; 9606.ENSP00000240343; -.
DR PhosphoSite; Q96FJ2; -.
DR DMDM; 56748850; -.
DR PaxDb; Q96FJ2; -.
DR PeptideAtlas; Q96FJ2; -.
DR PRIDE; Q96FJ2; -.
DR Ensembl; ENST00000240343; ENSP00000240343; ENSG00000121083.
DR GeneID; 140735; -.
DR KEGG; hsa:140735; -.
DR UCSC; uc010wnn.1; human.
DR CTD; 140735; -.
DR GeneCards; GC17P056160; -.
DR HGNC; HGNC:24596; DYNLL2.
DR MIM; 608942; gene.
DR neXtProt; NX_Q96FJ2; -.
DR PharmGKB; PA142671920; -.
DR eggNOG; NOG312371; -.
DR HOVERGEN; HBG002133; -.
DR InParanoid; Q96FJ2; -.
DR KO; K10418; -.
DR OMA; LAILIWK; -.
DR OrthoDB; EOG7BZVVQ; -.
DR PhylomeDB; Q96FJ2; -.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q96FJ2; -.
DR GeneWiki; DYNLL2; -.
DR GenomeRNAi; 140735; -.
DR NextBio; 84325; -.
DR PRO; PR:Q96FJ2; -.
DR Bgee; Q96FJ2; -.
DR CleanEx; HS_DYNLL2; -.
DR Genevestigator; Q96FJ2; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0008039; P:synaptic target recognition; IEA:Ensembl.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.740.10; -; 1.
DR InterPro; IPR019763; Dynein_light_1/2_CS.
DR InterPro; IPR001372; Dynein_light_chain_typ-1/2.
DR PANTHER; PTHR11886; PTHR11886; 1.
DR Pfam; PF01221; Dynein_light; 1.
DR PROSITE; PS01239; DYNEIN_LIGHT_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Cytoskeleton; Dynein;
KW Microtubule; Motor protein; Reference proteome; Transport.
FT CHAIN 1 89 Dynein light chain 2, cytoplasmic.
FT /FTId=PRO_0000195132.
FT SITE 41 41 Interaction with myosin V motor complex
FT (By similarity).
FT STRAND 6 13
FT HELIX 15 31
FT HELIX 35 50
FT STRAND 54 66
FT STRAND 72 78
FT STRAND 81 87
SQ SEQUENCE 89 AA; 10350 MW; 45364D32C0077F8E CRC64;
MSDRKAVIKN ADMSEDMQQD AVDCATQAME KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
//
ID DYL2_HUMAN Reviewed; 89 AA.
AC Q96FJ2; B2R5B4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Dynein light chain 2, cytoplasmic;
DE AltName: Full=8 kDa dynein light chain b;
DE Short=DLC8b;
DE AltName: Full=Dynein light chain LC8-type 2;
GN Name=DYNLL2; Synonyms=DLC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang H.L., Yu L., Yang J., Fu Q., Cui Y.Y., Zhao S.Y.;
RT "Cloning and sequencing of a novel human cDNA homologous to Rattus
RT norvegicus protein inhibitor of neuronal nitric oxide synthase (PIN)
RT mRNA.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory
CC components of the cytoplasmic dynein 1 complex that are thought to
CC be involved in linking dynein to cargos and to adapter proteins
CC that regulate dynein function. Cytoplasmic dynein 1 acts as a
CC motor for the intracellular retrograde motility of vesicles and
CC organelles along microtubules. May play a role in changing or
CC maintaining the spatial distribution of cytoskeletal structures
CC (By similarity).
CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of
CC two catalytic heavy chains (HCs) and a number of non-catalytic
CC subunits which present intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs); the composition
CC seems to vary in respect to the IC, LIC and LC composition. The
CC heavy chain homodimer serves as a scaffold for the probable
CC homodimeric assembly of the respective non-catalytic subunits.
CC Dynein ICs and LICs bind directly to the HC dimer and the LCs
CC assemble on the IC dimer. Interacts with DYNC1I1. Interacts with
CC BMF. Component of the myosin V motor complex. Interacts with
CC rabies virus phosphoprotein (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- SIMILARITY: Belongs to the dynein light chain family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF112997; AAP97230.1; -; mRNA.
DR EMBL; AK312125; BAG35061.1; -; mRNA.
DR EMBL; CH471109; EAW94484.1; -; Genomic_DNA.
DR EMBL; BC010744; AAH10744.1; -; mRNA.
DR RefSeq; NP_542408.1; NM_080677.2.
DR UniGene; Hs.720595; -.
DR PDB; 2XQQ; X-ray; 1.31 A; A/B/C/D=1-89.
DR PDB; 3P8M; X-ray; 2.90 A; A/B=1-89.
DR PDBsum; 2XQQ; -.
DR PDBsum; 3P8M; -.
DR ProteinModelPortal; Q96FJ2; -.
DR SMR; Q96FJ2; 1-89.
DR IntAct; Q96FJ2; 21.
DR MINT; MINT-1473886; -.
DR STRING; 9606.ENSP00000240343; -.
DR PhosphoSite; Q96FJ2; -.
DR DMDM; 56748850; -.
DR PaxDb; Q96FJ2; -.
DR PeptideAtlas; Q96FJ2; -.
DR PRIDE; Q96FJ2; -.
DR Ensembl; ENST00000240343; ENSP00000240343; ENSG00000121083.
DR GeneID; 140735; -.
DR KEGG; hsa:140735; -.
DR UCSC; uc010wnn.1; human.
DR CTD; 140735; -.
DR GeneCards; GC17P056160; -.
DR HGNC; HGNC:24596; DYNLL2.
DR MIM; 608942; gene.
DR neXtProt; NX_Q96FJ2; -.
DR PharmGKB; PA142671920; -.
DR eggNOG; NOG312371; -.
DR HOVERGEN; HBG002133; -.
DR InParanoid; Q96FJ2; -.
DR KO; K10418; -.
DR OMA; LAILIWK; -.
DR OrthoDB; EOG7BZVVQ; -.
DR PhylomeDB; Q96FJ2; -.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q96FJ2; -.
DR GeneWiki; DYNLL2; -.
DR GenomeRNAi; 140735; -.
DR NextBio; 84325; -.
DR PRO; PR:Q96FJ2; -.
DR Bgee; Q96FJ2; -.
DR CleanEx; HS_DYNLL2; -.
DR Genevestigator; Q96FJ2; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0008039; P:synaptic target recognition; IEA:Ensembl.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.740.10; -; 1.
DR InterPro; IPR019763; Dynein_light_1/2_CS.
DR InterPro; IPR001372; Dynein_light_chain_typ-1/2.
DR PANTHER; PTHR11886; PTHR11886; 1.
DR Pfam; PF01221; Dynein_light; 1.
DR PROSITE; PS01239; DYNEIN_LIGHT_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Cytoskeleton; Dynein;
KW Microtubule; Motor protein; Reference proteome; Transport.
FT CHAIN 1 89 Dynein light chain 2, cytoplasmic.
FT /FTId=PRO_0000195132.
FT SITE 41 41 Interaction with myosin V motor complex
FT (By similarity).
FT STRAND 6 13
FT HELIX 15 31
FT HELIX 35 50
FT STRAND 54 66
FT STRAND 72 78
FT STRAND 81 87
SQ SEQUENCE 89 AA; 10350 MW; 45364D32C0077F8E CRC64;
MSDRKAVIKN ADMSEDMQQD AVDCATQAME KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
//
MIM
608942
*RECORD*
*FIELD* NO
608942
*FIELD* TI
*608942 DYNEIN, LIGHT CHAIN, LC8 TYPE, 2; DYNLL2
;;DYNEIN LIGHT CHAIN 2; DLC2
*FIELD* TX
read more
CLONING
Using yeast 2-hybrid analysis with the postsynaptic scaffold protein
gephyrin (GPH; 603930) as bait, Fuhrmann et al. (2002) identified rat
dynein light chain-2 (Dlc2). Dlc2 encodes an 89-amino acid protein that
shows 93% and 100% identity to rat Dlc1 (DNCL1; 601562) and human DLC2,
respectively. Coimmunoprecipitation and GST pull-down assays confirmed
that Dlc2 binds with Gph, and yeast 2-hybrid analysis showed that Dlc2
binds to residues 181-243 of Gph, in the central linker domain.
GENE FUNCTION
Using immunofluorescence, Fuhrmann et al. (2002) showed that both
recombinant and endogenous Dlc2 colocalize with Gph in HEK293 cells. In
primary hippocampal neurons, Dlc2 localized to the cytoplasm in a
granular staining pattern and to the plasma membrane of dendrites and
cell bodies in a punctate staining pattern. The pattern of Dlc2 membrane
staining overlapped that of synaptophysin (313475) and partially
overlapped that of Gph. Electron microscopy of spinal cord neurons
showed that Dlc2 localizes to the edges of postsynaptic
differentiations, along cytoskeletal structures, and at the edge of the
Golgi apparatus. Wildtype Gph and Gph lacking the Dlc-binding domain
expressed in hippocampal neurons showed similar staining patterns,
suggesting that Dlc2 binding is not required for Gph localization.
MAPPING
By genomic sequence analysis, Pazour et al. (2006) mapped the DLC2 gene
to chromosome 17q23.2.
*FIELD* RF
1. Fuhrmann, J. C.; Kins, S.; Rostaing, P.; El Far, O.; Kirsch, J.;
Sheng, M.; Triller, A.; Betz, H.; Kneussel, M.: Gephyrin interacts
with dynein light chains 1 and 2, components of motor protein complexes. J.
Neurosci. 22: 5393-5402, 2002.
2. Pazour, G. J.; Agrin, N.; Walker, B. L.; Witman, G. B.: Identification
of predicted human outer dynein arm genes: candidates for primary
ciliary dyskinesia genes. (Letter) J. Med. Genet. 43: 62-73, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 4/19/2006
*FIELD* CD
Laura L. Baxter: 9/27/2004
*FIELD* ED
terry: 09/09/2010
mgross: 4/19/2006
alopez: 9/27/2004
*RECORD*
*FIELD* NO
608942
*FIELD* TI
*608942 DYNEIN, LIGHT CHAIN, LC8 TYPE, 2; DYNLL2
;;DYNEIN LIGHT CHAIN 2; DLC2
*FIELD* TX
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CLONING
Using yeast 2-hybrid analysis with the postsynaptic scaffold protein
gephyrin (GPH; 603930) as bait, Fuhrmann et al. (2002) identified rat
dynein light chain-2 (Dlc2). Dlc2 encodes an 89-amino acid protein that
shows 93% and 100% identity to rat Dlc1 (DNCL1; 601562) and human DLC2,
respectively. Coimmunoprecipitation and GST pull-down assays confirmed
that Dlc2 binds with Gph, and yeast 2-hybrid analysis showed that Dlc2
binds to residues 181-243 of Gph, in the central linker domain.
GENE FUNCTION
Using immunofluorescence, Fuhrmann et al. (2002) showed that both
recombinant and endogenous Dlc2 colocalize with Gph in HEK293 cells. In
primary hippocampal neurons, Dlc2 localized to the cytoplasm in a
granular staining pattern and to the plasma membrane of dendrites and
cell bodies in a punctate staining pattern. The pattern of Dlc2 membrane
staining overlapped that of synaptophysin (313475) and partially
overlapped that of Gph. Electron microscopy of spinal cord neurons
showed that Dlc2 localizes to the edges of postsynaptic
differentiations, along cytoskeletal structures, and at the edge of the
Golgi apparatus. Wildtype Gph and Gph lacking the Dlc-binding domain
expressed in hippocampal neurons showed similar staining patterns,
suggesting that Dlc2 binding is not required for Gph localization.
MAPPING
By genomic sequence analysis, Pazour et al. (2006) mapped the DLC2 gene
to chromosome 17q23.2.
*FIELD* RF
1. Fuhrmann, J. C.; Kins, S.; Rostaing, P.; El Far, O.; Kirsch, J.;
Sheng, M.; Triller, A.; Betz, H.; Kneussel, M.: Gephyrin interacts
with dynein light chains 1 and 2, components of motor protein complexes. J.
Neurosci. 22: 5393-5402, 2002.
2. Pazour, G. J.; Agrin, N.; Walker, B. L.; Witman, G. B.: Identification
of predicted human outer dynein arm genes: candidates for primary
ciliary dyskinesia genes. (Letter) J. Med. Genet. 43: 62-73, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 4/19/2006
*FIELD* CD
Laura L. Baxter: 9/27/2004
*FIELD* ED
terry: 09/09/2010
mgross: 4/19/2006
alopez: 9/27/2004