ID   A0A8M9QG43_DANRE        Unreviewed;       974 AA.
AC   A0A8M9QG43;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   10-JUN-2026, entry version 20.
DE   RecName: Full=Auxilin {ECO:0000256|ARBA:ARBA00069335};
DE   AltName: Full=DnaJ homolog subfamily C member 6 {ECO:0000256|ARBA:ARBA00075670};
GN   Name=dnajc6 {ECO:0000313|RefSeq:XP_021332835.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-080104-2};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_021332835.1};
RN   [1] {ECO:0000313|RefSeq:XP_021332835.1}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021332835.1};
RC   TISSUE=Fibroblasts and whole tissue
RC   {ECO:0000313|RefSeq:XP_021332835.1};
RG   RefSeq;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- SUBUNIT: Forms a complex composed of HSPA8, CLTC and DNAJC6. Interacts
CC       with HSPA8/HSC70 in an ATP-dependent manner; this interaction
CC       stimulates the HSPA8's ATPase activity. Interacts with CLTC; this
CC       interaction produces a local change in heavy-chain contacts, creating a
CC       detectable global distortion of the clathrin coat. Interacts with
CC       AP2A2. Interacts with DNM1(GTP-bound form); this interaction allows
CC       clathrin-coated vesicle (CCV) formation at the plasma membrane.
CC       {ECO:0000256|ARBA:ARBA00064305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       {ECO:0000256|ARBA:ARBA00004132}.
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DR   RefSeq; XP_021332835.1; XM_021477160.3.
DR   AlphaFoldDB; A0A8M9QG43; -.
DR   GeneID; 796345; -.
DR   AGR; ZFIN:ZDB-GENE-080104-2; -.
DR   CTD; 9829; -.
DR   ZFIN; ZDB-GENE-080104-2; dnajc6.
DR   Proteomes; UP000000437; Chromosome 6.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:UniProtKB-ARBA.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd14563; PTP_auxilin_N; 1.
DR   FunFam; 2.60.40.1110:FF:000001; cyclin-G-associated kinase isoform X2; 1.
DR   FunFam; 3.90.190.10:FF:000255; putative tyrosine-protein phosphatase auxilin; 1.
DR   FunFam; 1.10.287.110:FF:000002; putative tyrosine-protein phosphatase auxilin isoform X2; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR23172; AUXILIN/CYCLIN G-ASSOCIATED KINASE-RELATED; 1.
DR   PANTHER; PTHR23172:SF4; TYROSINE-PROTEIN PHOSPHATASE AUXILIN-RELATED; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
PE   4: Predicted;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          109..276
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          282..417
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   DOMAIN          910..974
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          464..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..491
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..503
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..594
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..703
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..729
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..746
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..791
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..830
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  104459 MW;  72B1960134AC1B5B CRC64;
     MSLLGGYKKK SSYDGYESLQ LVDSSGDFST GGRSGGGGGG GLTAVTLGSV KTGPARQDDY
     STMDSSDMDG NYGGGLLDMV KGGAGKFFSN IKDNLKDTIK DTSTKVMNQV ATYTKGELDI
     AYITSRIIVM SYPAETVEMG YRNHTEDIRS FLDSRHADHY TVFNLSQRNY RGAKFSNRVS
     ECNWPSRQAP SLHNLFAVCK NMYNWLKQNP KNVCVITCSD GRAPSGVLVC AMFCFCHLFA
     NPVPAMQLLS AKRPGSGLWP SHRRYIGYVC SLVSEKPTVP HSKPLVIKTV TISPVPCFNK
     QRSGCRPFCD VLIGETKIFS TAQEYERMRE HRIQEGKVVF PVGVSAQGDV VISVYHMRSH
     ALQAKVTNTQ IFQIQFHTGF IAPGSTVLKF MKTELDACDS PEKYPQLFHV LIDIEVESTE
     KQKDLTPPWE QFPTKDLSPN VLFSCHQEHQ DALAIADEME GLDLEDPAQG HSSCGGRVGP
     NEESEPSDDE MLSLSSQQSN ASNEKSKAAK RPEPQAAAPP PPAAEEVDLL GLDGDAAKIP
     PSSPQPPANN TTTDLLGDLF GAPPTPQPAS CPGSAQSTPR RSAQSSSPGP SPRSGNTFDP
     FGSGPAPAPK PQDFMGAFLG PGNMGQPDPF LHAARSPSPT MQNMGMGRSS PVPPSTPTVN
     IQQQNSTGAW EWNKPAAAGG GFGMGSKSAS TSPTSSAHGT PTHQTKPNTL DPFADLGNLG
     AGLGGGGSGF SSKPTTPTGT GGAFPPMGSP QRPAPSPQHT ASGGWHPNTG FPSWQAGGGA
     QWQPQAQGTP TKAPPASMPH TSPQNRPNYN VSFSAMSGAS PGAAGPKAQP NMGTRPKVSD
     ANFDDLLSGQ GFAGGKEKKG PKTIAEMRKE EMAKEMDPEK LKILDWIEGK ERNIRALLST
     MHTVLWEGET RWKPVGMADL VTPEQVKKVY RKAVLVVHPD KATGQPYEQY AKMIFMELND
     AWSEFESQGQ KALY
//