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O88487 (DC1I2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic dynein 1 intermediate chain 2
Alternative name(s):
Cytoplasmic dynein intermediate chain 2
Dynein intermediate chain 2, cytosolic
Short name=DH IC-2
Gene names
Name:Dync1i2
Synonyms:Dnci2, Dncic2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length612 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCNT1. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes By similarity.

Subunit structure

Homodimer By similarity. 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 DYNLT1 and DYNLT3. Interacts with DCNT1 By similarity.

Subcellular location

Cytoplasmcytoskeleton By similarity.

Post-translational modification

The phosphorylation status of Ser-84 appears to be involved in dynactin-dependent target binding By similarity.

Sequence similarities

Belongs to the dynein intermediate chain family.

Contains 7 WD repeats.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Cytoskeleton
Dynein
Microtubule
   DomainRepeat
WD repeat
   Molecular functionMotor protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmicrotubule-based movement

Inferred from electronic annotation. Source: InterPro

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasmic dynein complex

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmotor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 612611Cytoplasmic dynein 1 intermediate chain 2
PRO_0000114656

Regions

Repeat251 – 30050WD 1
Repeat304 – 34441WD 2
Repeat353 – 39442WD 3
Repeat403 – 44341WD 4
Repeat448 – 49346WD 5
Repeat496 – 53641WD 6
Repeat542 – 58140WD 7

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue841Phosphoserine By similarity
Modified residue911Phosphoserine By similarity
Modified residue951Phosphoserine By similarity
Modified residue981Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O88487 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 1D14CEECF62A5E33

FASTA61268,394
        10         20         30         40         50         60 
MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAAVSVQEE SDLEKKRREA 

        70         80         90        100        110        120 
EALLQSMGLT TDSPIVPPPM SPSSKSVSTP SEAGSQDSGD GAVGSRRGPI KLGMAKITQV 

       130        140        150        160        170        180 
DFPPREIVTY TKETQTPVTA QPKEDEEEED DVATPKPPVE PEEEKTLKKD EENDSKAPPH 

       190        200        210        220        230        240 
ELTEEEKQQI LHSEEFLSFF DHSTRIVERA LSEQINIFFD YSGRDLEDKE GEIQAGAKLS 

       250        260        270        280        290        300 
LNRQFFDERW SKHRVVSCLD WSSQYPELLV ASYNNNEEAP HEPDGVALVW NMKYKKTTPE 

       310        320        330        340        350        360 
YVFHCQSAVM SATFAKFHPN LVVGGTYSGQ IVLWDNRSNK RTPVQRTPLS AAAHTHPVYC 

       370        380        390        400        410        420 
VNVVGTQNAH NLISISTDGK ICSWSLDMLS HPQDSMELVH KQSKAVAVTS MSFPVGDVNN 

       430        440        450        460        470        480 
FVVGSEEGSV YTACRHGSKA GISEMFEGHQ GPITGIHCHA AVGAVDFSHL FVTSSFDWTV 

       490        500        510        520        530        540 
KLWTTKNNKP LYSFEDNSDY VYDVMWSPTH PALFACVDGM GRLDLWNLNN DTEVPTASIS 

       550        560        570        580        590        600 
VEGNPALNRV RWTHSGREIA VGDSEGQIVI YDVGEQIAVP RNDEWARFGR TLAEINANRA 

       610 
DAEEEAATRI PA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of two cytoplasmic dynein intermediate chain genes in mouse and human."
Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M., Rommens J.M., Scherer S.W., Tsui L.-C.
Genomics 55:257-267(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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 and NOD.
Tissue: Eye, Heart and Thymus.
[3]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF063231 mRNA. Translation: AAC33446.1.
AK088015 mRNA. Translation: BAC40097.1.
AK164437 mRNA. Translation: BAE37788.1.
AK168730 mRNA. Translation: BAE40571.1.
RefSeqNP_001185805.1. NM_001198876.1.
NP_001185806.1. NM_001198877.1.
NP_001185807.1. NM_001198878.1.
NP_034194.1. NM_010064.4.
UniGeneMm.249479.

3D structure databases

ProteinModelPortalO88487.
SMRO88487. Positions 110-138, 307-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199256. 7 interactions.
IntActO88487. 11 interactions.
MINTMINT-3088834.

PTM databases

PhosphoSiteO88487.

2D gel databases

REPRODUCTION-2DPAGEO88487.

Proteomic databases

PaxDbO88487.
PRIDEO88487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081710; ENSMUSP00000080410; ENSMUSG00000027012.
ENSMUST00000112138; ENSMUSP00000107766; ENSMUSG00000027012.
GeneID13427.
KEGGmmu:13427.
UCSCuc008kai.2. mouse.

Organism-specific databases

CTD1781.
MGIMGI:107750. Dync1i2.

Phylogenomic databases

eggNOGNOG308180.
GeneTreeENSGT00730000110228.
HOVERGENHBG004083.
KOK10415.
OrthoDBEOG7FR7FX.
TreeFamTF300553.

Gene expression databases

ArrayExpressO88487.
BgeeO88487.
CleanExMM_DYNC1I2.
GenevestigatorO88487.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR025956. Dynein_IC_1/2.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF11540. Dynein_IC2. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283847.
PROO88487.
SOURCESearch...

Entry information

Entry nameDC1I2_MOUSE
AccessionPrimary (citable) accession number: O88487
Secondary accession number(s): Q3TGH7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot