AUXI_BOVIN
ID AUXI_BOVIN Reviewed; 910 AA.
AC Q27974;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Putative tyrosine-protein phosphatase auxilin {ECO:0000305|PubMed:7705342};
DE EC=3.1.3.48;
DE AltName: Full=DnaJ homolog subfamily C member 6 {ECO:0000250|UniProtKB:O75061};
GN Name=DNAJC6 {ECO:0000250|UniProtKB:O75061};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY,
RP AND PHOSPHORYLATION.
RC TISSUE=Brain;
RX PubMed=7705342; DOI=10.1111/j.1432-1033.1995.00297.x;
RA Schroeder S., Morris S.A., Knorr R., Plessmann U., Weber K., Vinh N.G.,
RA Ungewickell E.;
RT "Primary structure of the neuronal clathrin-associated protein auxilin and
RT its expression in bacteria.";
RL Eur. J. Biochem. 228:297-304(1995).
RN [2]
RP STRUCTURE BY NMR OF 713-910.
RX PubMed=10959640; DOI=10.1023/a:1008353226591;
RA Han C.J., Gruschus J.M., Greener T., Greene L.E., Ferretti J.,
RA Eisenberg E.;
RT "1H, 15N, and 13C NMR backbone assignments and secondary structure of the
RT C-terminal recombinant fragment of auxilin including the J-domain.";
RL J. Biomol. NMR 17:281-282(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 810-910, MUTAGENESIS OF LYS-847;
RP LYS-849 AND ASP-876, AND INTERACTION WITH HSPA8.
RX PubMed=12741832; DOI=10.1021/bi034270g;
RA Jiang J., Taylor A.B., Prasad K., Ishikawa-Brush Y., Hart P.J., Lafer E.M.,
RA Sousa R.;
RT "Structure-function analysis of the auxilin J-domain reveals an extended
RT Hsc70 interaction interface.";
RL Biochemistry 42:5748-5753(2003).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF 797-910 IN COMPLEX
RP WITH CLATHRIN COATS, AND FUNCTION.
RX PubMed=15502813; DOI=10.1038/nature03078;
RA Fotin A., Cheng Y., Grigorieff N., Walz T., Harrison S.C., Kirchhausen T.;
RT "Structure of an auxilin-bound clathrin coat and its implications for the
RT mechanism of uncoating.";
RL Nature 432:649-653(2004).
CC -!- FUNCTION: Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes
CC uncoating of clathrin-coated vesicles (PubMed:15502813). Plays a role
CC in clathrin-mediated endocytosis in neurons (By similarity).
CC {ECO:0000250|UniProtKB:Q80TZ3, ECO:0000269|PubMed:15502813}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- SUBUNIT: Interacts with HSPA8/HSC70. Interacts with clathrin heavy
CC chains. {ECO:0000269|PubMed:12741832}.
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:7705342}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7705342}.
CC -!- PTM: Target for coat-associated casein kinase II in vitro.
CC {ECO:0000305|PubMed:7705342}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U09237; AAA79037.1; -; mRNA.
DR PIR; S68983; S68983.
DR RefSeq; NP_777261.1; NM_174836.2.
DR PDB; 1N4C; NMR; -; A=737-910.
DR PDB; 1NZ6; X-ray; 2.50 A; A/B=810-910.
DR PDB; 1XI5; EM; 12.00 A; J/K/L/M/N/O/P/Q/R=797-910.
DR PDB; 2QWN; X-ray; 2.40 A; B=812-905.
DR PDB; 2QWO; X-ray; 1.70 A; B=813-904.
DR PDB; 2QWP; X-ray; 1.75 A; B=813-904.
DR PDB; 2QWQ; X-ray; 2.21 A; B=813-904.
DR PDB; 2QWR; X-ray; 2.21 A; B=813-904.
DR PDB; 3N0A; X-ray; 2.20 A; A=40-400.
DR PDBsum; 1N4C; -.
DR PDBsum; 1NZ6; -.
DR PDBsum; 1XI5; -.
DR PDBsum; 2QWN; -.
DR PDBsum; 2QWO; -.
DR PDBsum; 2QWP; -.
DR PDBsum; 2QWQ; -.
DR PDBsum; 2QWR; -.
DR PDBsum; 3N0A; -.
DR AlphaFoldDB; Q27974; -.
DR BMRB; Q27974; -.
DR SMR; Q27974; -.
DR DIP; DIP-41952N; -.
DR ELM; Q27974; -.
DR IntAct; Q27974; 1.
DR MINT; Q27974; -.
DR STRING; 9913.ENSBTAP00000041032; -.
DR PaxDb; Q27974; -.
DR PRIDE; Q27974; -.
DR GeneID; 317659; -.
DR KEGG; bta:317659; -.
DR CTD; 9829; -.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR InParanoid; Q27974; -.
DR OrthoDB; 826336at2759; -.
DR EvolutionaryTrace; Q27974; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IPI:CAFA.
DR GO; GO:0032050; F:clathrin heavy chain binding; IPI:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0072318; P:clathrin coat disassembly; IMP:CAFA.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR DisProt; DP00351; -.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Hydrolase;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
KW SH3-binding.
FT CHAIN 1..910
FT /note="Putative tyrosine-protein phosphatase auxilin"
FT /id="PRO_0000215902"
FT REPEAT 33..36
FT /note="1"
FT REPEAT 37..40
FT /note="2"
FT REPEAT 41..44
FT /note="3"
FT DOMAIN 52..219
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 225..363
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 846..910
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 33..44
FT /note="3 X 4 AA approximate tandem repeats"
FT REGION 448..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 406..414
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 450..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75061"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TZ3"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TZ3"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75061"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75061"
FT MUTAGEN 847
FT /note="K->C: Strongly reduces interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12741832"
FT MUTAGEN 849
FT /note="K->C: Slightly reduces interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12741832"
FT MUTAGEN 876
FT /note="D->A: Loss of interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:12741832"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 291..304
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 310..323
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:3N0A"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:3N0A"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:1N4C"
FT STRAND 751..754
FT /evidence="ECO:0007829|PDB:1N4C"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:1N4C"
FT HELIX 781..783
FT /evidence="ECO:0007829|PDB:1N4C"
FT STRAND 786..789
FT /evidence="ECO:0007829|PDB:1N4C"
FT HELIX 801..809
FT /evidence="ECO:0007829|PDB:1N4C"
FT HELIX 814..826
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 830..836
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 837..839
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 853..855
FT /evidence="ECO:0007829|PDB:2QWO"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 859..872
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 875..878
FT /evidence="ECO:0007829|PDB:2QWO"
FT HELIX 884..903
FT /evidence="ECO:0007829|PDB:2QWO"
SQ SEQUENCE 910 AA; 99512 MW; BC156DC1CF3487FD CRC64;
MDSSGASSPD MEPSYGGGLF DMVKGGAGRL FSNLKDNLKD TLKDTSSRVI QSVTSYTKGD
LDFTYVTSRI IVMSFPLDSV DIGFRNQVDD IRSFLDSRHL DHYTVYNLSP KSYRTAKFHS
RVSECSWPIR QAPSLHNLFA VCRNMYNWLL QNPKNVCVVH CLDGRAASSI LVGAMFIFCN
LYSTPGPAVR LLYAKRPGIG LSPSHRRYLG YMCDLLADKP YRPHFKPLTI KSITVSPVPF
FNKQRNGCRP YCDVLIGETK IYTTCADFER MKEYRVQDGK IFIPLSITVQ GDVVVSMYHL
RSTIGSRLQA KVTNTQIFQL QFHTGFIPLD TTVLKFTKPE LDACDVPEKY PQLFQVTLDV
ELQPHDKVME LTPPWEHYCT KDVNPSILFS SHQEHQDTLV LGGQAPIDIP PDNPRHFGQG
GFFSTLCWQD QKSEKSFCEE DHAALVNQES EQSDDELLTL SSPHGNANGD KPHAARKPSK
KQQEPAAPAP PEDVDLLGLE GSAVSKNFSS PAAPPSNSEL LSDLFGGGGA AGPVQSGQSG
VDDVFHPSGP TSTQSTPRRS ATSTSASPTL RVGEGATFDP FGAPSKPSGQ DLLGSFLNTA
SASSDPFLQP TRSPSPTVHA SSTPAVNIQP DVSGAWDWHT KPGGFGMGSK SAATSPTGSS
HGTPTHQNKP QTLDPFADLG TLGGSSFASK PSTPTGLGGG FPPLSSPQKA SPQPMGGGWQ
QGGGYNWQQT QSKPQSSMPH SSPQNRPNYN VSFSSMPGGQ NERGKAAANL EGKQKAADFE
DLLSGQGFNA HKDKKGPRTI AEMRKEEMAK EMDPEKLKIL EWIEGKERNI RALLSTMHTV
LWAGETKWKP VGMADLVTPE QVKKVYRKAV LVVHPDKATG QPYEQYAKMI FMELNDAWSE
FENQGQKPLY
