EFCB6_PONAB
ID EFCB6_PONAB Reviewed; 1013 AA.
AC Q5RE62;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=EF-hand calcium-binding domain-containing protein 6;
DE AltName: Full=DJ-1-binding protein;
DE Short=DJBP;
GN Name=EFCAB6; Synonyms=DJBP;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Negatively regulates the androgen receptor by recruiting
CC histone deacetylase complex, and protein DJ-1 antagonizes this
CC inhibition by abrogation of this complex. Microtubule inner protein
CC (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia
CC axoneme, which is required for motile cilia beating.
CC {ECO:0000250|UniProtKB:Q5THR3}.
CC -!- SUBUNIT: Binds PARK7. Part of a ternary complex containing PARK7,
CC EFCAB6/DJBP and AR (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5THR3}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q5THR3}.
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DR EMBL; CR857675; CAH89945.1; -; Transcribed_RNA.
DR AlphaFoldDB; Q5RE62; -.
DR STRING; 9601.ENSPPYP00000013297; -.
DR eggNOG; KOG0027; Eukaryota.
DR InParanoid; Q5RE62; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 9.
DR SUPFAM; SSF47473; SSF47473; 5.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 11.
PE 3: Inferred from homology;
KW Calcium; Cell projection; Cytoplasm; Cytoskeleton; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1013
FT /note="EF-hand calcium-binding domain-containing protein 6"
FT /id="PRO_0000246027"
FT DOMAIN 20..55
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 145..180
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 251..286
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 287..322
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 352..387
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 482..517
FT /note="EF-hand 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 589..624
FT /note="EF-hand 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 695..730
FT /note="EF-hand 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 731..766
FT /note="EF-hand 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 812..847
FT /note="EF-hand 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 917..952
FT /note="EF-hand 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 441..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 602
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 604
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 606
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 613
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1E8"
SQ SEQUENCE 1013 AA; 117761 MW; 5C1E8DB93920AB42 CRC64;
MNCCRTLREL EIQVGEKVFK NIKTVMKAFK LIDVNKTGLV RPQELRRVLE TFCLKLRDEE
YEKFSKHYNI HNDTAVDYNV FLKNLSINND LNLRYCMGNQ EVSLENQQAR NSKKERLLGS
ASSEDIWRNY SLDDIERNFC LELSKSYEKI EKALSAGDPC KGGYVSFNYL KIVLDTFIYQ
IPRRIFIQLM KRFGLKATTK INWKQFLTSF HEPQGLQVSN KGPLTKRNSI NSRSESRKEN
IITKLFRCTE DRSASLKKAL LIINTKPDGP ITREEFRYIL NCVAIKLSDS EFKELMQILD
PGDTGVVNTS MFIDLIEENC RMRKTSPCTD AKTPFLLAWD SVEEIVHDTI ARNLQAFYNM
LRSYDLGDTG LIGRNNFKKI MHVFCPFLTN AHFIKLCSKI QDIGSGRILY KKLLACIGID
GPPTVSPVLV PKDQLLSEHL QKDEQQQPDL SERTKPTEDK TTLTKKMTTE EVIEKFRKYI
QQQDPAFKKR FLDFSKEPNG KINVHDFRKI LEDTGMPMDD DQYALLTTKI GFEKEGMSYL
DFAAGFEDPP MRGLETTPPQ PPTPSKSYVN SHLITAEECL KLFPRRLKES FRDPYSAFFK
TDVDRDGIIN MHDLHRLLLH LLLNLKDDEF ERFLGLLGLR LSVTLNFREF QNLCEKRPWR
TDEAPQRLIR PKQKVADSEL ACEQAHQYLV TKAKNRWSDL SKNFLETDNE GNGILRRRDI
KNALYGFDIP LTPREFEKLW ARYNTEGKGH ITYQEFLQKL GINYSPAVHQ PCAEDYFNFM
GHFTKPQQLQ EEMKELQQST EKAMAARDKL MDLHQDISKA FTKIDKSKTN YISICKMQKV
LEECGCSLTE GELTHLLNSW GVSRHENAIN YLDFLRAVEN SKSTGAQPKE KEESMPISFA
TLNPQEVVRK IQEVVESSQL ALSTAFSALD KEDTGFVKAT EFGQVLKDFC YKLMDNQYHY
FLRKLRIHLT PYINWKYFLQ NFSCFLEEVR ISAAHKHLFE NELKLVFTKW IID
