General information | DisProt: | DP00351 | Name: | Putative tyrosine-protein phosphatase auxilin | Synonym(s): | AUXI_BOVIN
EC=3.1.3.48
DnaJ homolog subfamily C member 6
| First appeared in release: | Release 3.0 (02/17/2006) | UniProt: | Q27974 | UniGene: | Bt.65042 | SwissProt: | AUXI_BOVIN | TrEMBL: | | NCBI (GI): | 2498170 | Source organism: | Bos taurus (Bovine) | Sequence length: | 910 | Percent disordered: | 29% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MDSSGASSPD MEPSYGGGLF DMVKGGAGRL FSNLKDNLKD TLKDTSSRVI QSVTSYTKGD - 60 LDFTYVTSRI IVMSFPLDSV DIGFRNQVDD IRSFLDSRHL DHYTVYNLSP KSYRTAKFHS - 120 RVSECSWPIR QAPSLHNLFA VCRNMYNWLL QNPKNVCVVH CLDGRAASSI LVGAMFIFCN - 180 LYSTPGPAVR LLYAKRPGIG LSPSHRRYLG YMCDLLADKP YRPHFKPLTI KSITVSPVPF - 240 FNKQRNGCRP YCDVLIGETK IYTTCADFER MKEYRVQDGK IFIPLSITVQ GDVVVSMYHL - 300 RSTIGSRLQA KVTNTQIFQL QFHTGFIPLD TTVLKFTKPE LDACDVPEKY PQLFQVTLDV - 360 ELQPHDKVME LTPPWEHYCT KDVNPSILFS SHQEHQDTLV LGGQAPIDIP PDNPRHFGQG - 420 GFFSTLCWQD QKSEKSFCEE DHAALVNQES EQSDDELLTL SSPHGNANGD KPHAARKPSK - 480 KQQEPAAPAP PEDVDLLGLE GSAVSKNFSS PAAPPSNSEL LSDLFGGGGA AGPVQSGQSG - 540 VDDVFHPSGP TSTQSTPRRS ATSTSASPTL RVGEGATFDP FGAPSKPSGQ DLLGSFLNTA - 600 SASSDPFLQP TRSPSPTVHA SSTPAVNIQP DVSGAWDWHT KPGGFGMGSK SAATSPTGSS - 660 HGTPTHQNKP QTLDPFADLG TLGGSSFASK PSTPTGLGGG FPPLSSPQKA SPQPMGGGWQ - 720 QGGGYNWQQT QSKPQSSMPH SSPQNRPNYN VSFSSMPGGQ NERGKAAANL EGKQKAADFE - 780 DLLSGQGFNA HKDKKGPRTI AEMRKEEMAK EMDPEKLKIL EWIEGKERNI RALLSTMHTV - 840 LWAGETKWKP VGMADLVTPE QVKKVYRKAV LVVHPDKATG QPYEQYAKMI FMELNDAWSE - 900 FENQGQKPLY
|
Functional narrative |
The J-domain protein auxilin is a neuron-specific protein involved in the removal of the clathrin coat from endocytosed synaptic vesicle membranes. Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles.
|
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.
|
Region 1 | Type: | Disordered | Name: | Clathrin binding domain | Location: | 547 - 813 | Length: | 267 | Region sequence: |
PSGPTSTQSTPRRSATSTSASPTLRVGEGATFDPFGAPSKPSGQDLLGSFLNTASASSDP FLQPTRSPSPTVHASSTPAVNIQPDVSGAWDWHTKPGGFGMGSKSAATSPTGSSHGTPTH QNKPQTLDPFADLGTLGGSSFASKPSTPTGLGGGFPPLSSPQKASPQPMGGGWQQGGGYN WQQTQSKPQSSMPHSSPQNRPNYNVSFSSMPGGQNERGKAAANLEGKQKAADFEDLLSGQ GFNAHKDKKGPRTIAEMRKEEMAKEMD | Modification type: | Native
| PDB: | | Structural/functional type: | | Functional classes: | | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (75 K; PBS)
| References:
- Scheele U, Alves J, Frank R, Düwel M, Kalthoff C, Ungewickell E.
Scheele U, Alves J, Frank R, Düwel M, Kalthoff C, Ungewickell E. "Molecular and functional characterization of clathrin- and AP-2 binding determinants within a disordered domain of auxilin." J Biol Chem. 2003; 278(28): 25357-25368. PubMed: 12732633
| Comments:
|
References |
- Morgan JR, Prasad K, Jin S, Augustine GJ, Lafer EM. "Uncoating of clathrin-coated vesicles in presynaptic terminals: roles for Hsc70 and auxilin." Neuron. 2001; 32(2): 289-300. PubMed: 11683998
|
If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|