| General information | | DisProt: | DP00360 | | Name: | Cytoplasmic dynein 1 intermediate chain 1 [Isoform 1] | | Synonym(s): | DC1I1_HUMAN
Cytoplasmic dynein intermediate chain 1
Dynein intermediate chain 1, cytosolic
DH IC-1
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | O14576-1 | | UniGene: | Hs.440364 | | SwissProt: | DC1I1_HUMAN | | TrEMBL: | | | NCBI (GI): | 6647481 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 645 | | Percent disordered: | 45% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVQDDS DLDRKRRETE - 60
ALLQSIGISP EPPLVQPLHF LTWDTCYFHY LVPTPMSPSS KSVSTPSEAG SQDSGDLGPL - 120
TRTLQWDTDP SVLQLQSDSE LGRRLHKLGV SKVTQVDFLP REVVSYSKET QTPLATHQSE - 180
EDEEDEEMVE SKVGQDSELE NQDKKQEVKE APPRELTEEE KQQILHSEEF LIFFDRTIRV - 240
IERALAEDSD IFFDYSGREL EEKDGDVQAG ANLSFNRQFY DEHWSKHRVV TCMDWSLQYP - 300
ELMVASYNNN EDAPHEPDGV ALVWNMKFKK TTPEYVFHCQ SSVMSVCFAR FHPNLVVGGT - 360
YSGQIVLWDN RSHRRTPVQR TPLSAAAHTH PVYCVNVVGT QNAHNLITVS TDGKMCSWSL - 420
DMLSTPQESM ELVYNKSKPV AVTGMAFPTG DVNNFVVGSE EGTVYTACRH GSKAGIGEVF - 480
EGHQGPVTGI NCHMAVGPID FSHLFVTSSF DWTVKLWTTK HNKPLYSFED NADYVYDVMW - 540
SPVHPALFAC VDGMGRLDLW NLNNDTEVPT ASVAIEGASA LNRVRWAQAG KEVAVGDSEG - 600
RIWVYDVGEL AVPHNDEWTR FARTLVEIRA NRADSEEEGT VELSA
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| Functional narrative |
Cytoplasmic dynein from vertebrates contains two heavy chains (HCs), two intermediate chains (ICs), two to four light intermediate chains (LICs), and four to five light chains (LCs). The HC contains the motor domain. The accessory chains are important for mediating the functions performed by HC. In Caenorhabditis elegans and cultured vertebrate cells, loss of IC or LIC function shows defects in cytoplasmic dynein function.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 289 | | Length: | 289 | | Region sequence: |
MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRETE
ALLQSIGISPEPPLVQPLHFLTWDTCYFHYLVPTPMSPSSKSVSTPSEAGSQDSGDLGPL
TRTLQWDTDPSVLQLQSDSELGRRLHKLGVSKVTQVDFLPREVVSYSKETQTPLATHQSE
EDEEDEEMVESKVGQDSELENQDKKQEVKEAPPRELTEEEKQQILHSEEFLIFFDRTIRV
IERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRV | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
Relationship to function unknown
| | Functional classes: | | | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
- Fluorescence, intrinsic
- Size exclusion/gel filtration chromatography
- Sensitivity to proteolysis
| References:
- Barbar E, Hare M. "Characterization of the cargo attachment complex of cytoplasmic dynein using NMR and mass spectrometry." Methods Enzymol. 2004; 380: 219-41. PubMed: 15051340
- Makokha M, Hare M, Li M, Hays T, Barbar E. "Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74." Biochemistry. 2002; 41(13): 4302-11. PubMed: 11914076
- Nyarko A, Hare M, Hays TS, Barbar E. "The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8." Biochemistry. 2004; 43(49): 15595-603. PubMed: 15581372
| Comments:
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| References |
- King SM. "The dynein microtubule motor." Biochim Biophys Acta. 2000; 1496(1): 60-75. PubMed: 10722877
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