Reviewed, UniProtKB/Swiss-Prot Q27974 (AUXI_BOVIN)

Names and origin

Protein names

Recommended name:
    Putative tyrosine-protein phosphatase auxilin
    EC=3.1.3.48
Alternative name(s):
    DnaJ homolog subfamily C member 6

Gene names

Name:

DNAJC6

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	910 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Ref.4
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with HSPA8/HSC70. Interacts with clathrin heavy chains. Ref.3
Tissue specificity	Brain.
Post-translational modification	The N-terminus is blocked. Target for coat-associated casein kinase II in vitro.
Sequence similarities	Contains 1 C2 tensin-type domain. Contains 1 J domain. Contains 1 phosphatase tensin-type domain.

Ontologies

Keywords
Domain	Repeat SH3-binding
Molecular function	Chaperone Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW heat shock protein binding Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 910

910

Putative tyrosine-protein phosphatase auxilin

PRO_0000215902

Regions

Repeat

33 – 36

4

1

Repeat

37 – 40

4

2

Repeat

41 – 44

4

3

Domain

52 – 219

168

Phosphatase tensin-type

Domain

225 – 363

139

C2 tensin-type

Domain

846 – 910

65

J

Region

33 – 44

12

3 X 4 AA approximate tandem repeats

Motif

406 – 414

9

SH3-binding Potential

Compositional bias

463 – 757

295

Pro-rich

Compositional bias

526 – 529

4

Poly-Gly

Sites

Active site

161

1

Phosphocysteine intermediate Potential

Amino acid modifications

Modified residue

560

1

Phosphoserine By similarity

Modified residue

563

1

Phosphoserine By similarity

Modified residue

564

1

Phosphothreonine By similarity

Modified residue

567

1

Phosphoserine By similarity

Experimental info

Mutagenesis

847

1

K → C: Strongly reduces interaction with HSPA8. Ref.3

Mutagenesis

849

1

K → C: Slightly reduces interaction with HSPA8. Ref.3

Mutagenesis

876

1

D → A: Loss of interaction with HSPA8. Ref.3

Secondary structure

1

.

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.

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910

Helix Strand Turn

Details...

Beta strand

738 – 740

3

Beta strand

751 – 754

4

Beta strand

757 – 759

3

Helix

781 – 783

3

Beta strand

786 – 789

4

Helix

801 – 809

9

Helix

814 – 823

10

Turn

824 – 828

5

Helix

830 – 834

5

Helix

837 – 839

3

Helix

853 – 855

3

Helix

859 – 872

14

Helix

875 – 878

4

Helix

884 – 902

19

Turn

903 – 905

3

Sequences

	Sequence		Length	Mass (Da)
	Q27974-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: BC156DC1CF3487FD	FASTA	910	99,512
	10 20 30 40 50 60 MDSSGASSPD MEPSYGGGLF DMVKGGAGRL FSNLKDNLKD TLKDTSSRVI QSVTSYTKGD 70 80 90 100 110 120 LDFTYVTSRI IVMSFPLDSV DIGFRNQVDD IRSFLDSRHL DHYTVYNLSP KSYRTAKFHS 130 140 150 160 170 180 RVSECSWPIR QAPSLHNLFA VCRNMYNWLL QNPKNVCVVH CLDGRAASSI LVGAMFIFCN 190 200 210 220 230 240 LYSTPGPAVR LLYAKRPGIG LSPSHRRYLG YMCDLLADKP YRPHFKPLTI KSITVSPVPF 250 260 270 280 290 300 FNKQRNGCRP YCDVLIGETK IYTTCADFER MKEYRVQDGK IFIPLSITVQ GDVVVSMYHL 310 320 330 340 350 360 RSTIGSRLQA KVTNTQIFQL QFHTGFIPLD TTVLKFTKPE LDACDVPEKY PQLFQVTLDV 370 380 390 400 410 420 ELQPHDKVME LTPPWEHYCT KDVNPSILFS SHQEHQDTLV LGGQAPIDIP PDNPRHFGQG 430 440 450 460 470 480 GFFSTLCWQD QKSEKSFCEE DHAALVNQES EQSDDELLTL SSPHGNANGD KPHAARKPSK 490 500 510 520 530 540 KQQEPAAPAP PEDVDLLGLE GSAVSKNFSS PAAPPSNSEL LSDLFGGGGA AGPVQSGQSG 550 560 570 580 590 600 VDDVFHPSGP TSTQSTPRRS ATSTSASPTL RVGEGATFDP FGAPSKPSGQ DLLGSFLNTA 610 620 630 640 650 660 SASSDPFLQP TRSPSPTVHA SSTPAVNIQP DVSGAWDWHT KPGGFGMGSK SAATSPTGSS 670 680 690 700 710 720 HGTPTHQNKP QTLDPFADLG TLGGSSFASK PSTPTGLGGG FPPLSSPQKA SPQPMGGGWQ 730 740 750 760 770 780 QGGGYNWQQT QSKPQSSMPH SSPQNRPNYN VSFSSMPGGQ NERGKAAANL EGKQKAADFE 790 800 810 820 830 840 DLLSGQGFNA HKDKKGPRTI AEMRKEEMAK EMDPEKLKIL EWIEGKERNI RALLSTMHTV 850 860 870 880 890 900 LWAGETKWKP VGMADLVTPE QVKKVYRKAV LVVHPDKATG QPYEQYAKMI FMELNDAWSE 910 FENQGQKPLY

References

[1]	"Primary structure of the neuronal clathrin-associated protein auxilin and its expression in bacteria." Schroeder S., Morris S.A., Knorr R., Plessmann U., Weber K., Vinh N.G., Ungewickell E. Eur. J. Biochem. 228:297-304(1995) [PubMed: 7705342] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[2]	"1H, 15N, and 13C NMR backbone assignments and secondary structure of the C-terminal recombinant fragment of auxilin including the J-domain." Han C.J., Gruschus J.M., Greener T., Greene L.E., Ferretti J., Eisenberg E. J. Biomol. NMR 17:281-282(2000) [PubMed: 10959640] [Abstract] Cited for: STRUCTURE BY NMR OF 713-910.
[3]	"Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface." Jiang J., Taylor A.B., Prasad K., Ishikawa-Brush Y., Hart P.J., Lafer E.M., Sousa R. Biochemistry 42:5748-5753(2003) [PubMed: 12741832] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 810-910, MUTAGENESIS OF LYS-847; LYS-849 AND ASP-876, INTERACTION WITH HSPA8.
[4]	"Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating." Fotin A., Cheng Y., Grigorieff N., Walz T., Harrison S.C., Kirchhausen T. Nature 432:649-653(2004) [PubMed: 15502813] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF 797-910 IN COMPLEX WITH CLATHRIN COATS, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U09237 mRNA. Translation: AAA79037.1.

IPI

IPI00707709.

PIR

S68983.

RefSeq

NP_777261.1.

UniGene

Bt.65042

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N4C	NMR	-	A	737-910	[»]
1NZ6	X-ray	2.50	A/B	810-910	[»]
1Q2G	model	-	A	776-910	[»]
1XI5	electron microscopy	12.00	J/K/L/M/N/O/P/Q/R	797-910	[»]
2QWN	X-ray	2.40	B	812-905	[»]
2QWO	X-ray	1.70	B	813-904	[»]
2QWP	X-ray	1.75	B	813-904	[»]
2QWQ	X-ray	2.21	B	813-904	[»]
2QWR	X-ray	2.21	B	813-904	[»]

DisProt

DP00351.

ModBase

Search...

Genome annotation databases

Ensembl

ENSBTAG00000016410. Bos taurus. [Contig view]

GeneID

317659.

KEGG

bta:317659.

Phylogenomic databases

HOVERGEN

Q27974.

Enzyme and pathway databases

BRENDA

3.1.3.48. 251.

Family and domain databases

InterPro

IPR001623. DnaJ_N.
IPR018253. Heat_shock_DnaJ_CS.
IPR014019. Phosphatase_tensin-typ.
IPR014020. Tensin_phosphatase_C2-dom.
[Graphical view]

Gene3D

G3DSA:1.10.287.110. DnaJ_N. 1 hit.

Pfam

PF00226. DnaJ. 1 hit.
PF10409. PTEN_C2. 1 hit.
[Graphical view]

SMART

SM00271. DnaJ. 1 hit.
[Graphical view]

PROSITE

PS51182. C2_TENSIN. 1 hit.
PS00636. DNAJ_1. False negative.
PS50076. DNAJ_2. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AUXI_BOVIN

Accession

Primary (citable) accession number: Q27974

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 5, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)