ID   H9FTV6_MACMU            Unreviewed;       605 AA.
AC   H9FTV6;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Ankyrin repeat domain-containing protein 13D {ECO:0000313|EMBL:AFE78065.1};
GN   Name=ANKRD13D {ECO:0000313|EMBL:AFE78065.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE78065.1};
RN   [1] {ECO:0000313|EMBL:AFE78065.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE78065.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH29341.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
CC   -!- FUNCTION: Ubiquitin-binding protein that specifically recognizes and
CC       binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked
CC       ubiquitin. Positively regulates the internalization of ligand-activated
CC       EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell
CC       membrane. {ECO:0000256|ARBA:ARBA00024956}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Endosome {ECO:0000256|ARBA:ARBA00004177}. Late endosome
CC       {ECO:0000256|ARBA:ARBA00004603}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
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DR   EMBL; JU334312; AFE78065.1; -; mRNA.
DR   EMBL; JU472537; AFH29341.1; -; mRNA.
DR   AlphaFoldDB; H9FTV6; -.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR021832; ANKRD13.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR003903; UIM_dom.
DR   PANTHER; PTHR12447; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 13; 1.
DR   PANTHER; PTHR12447:SF2; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 13D; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF11904; GPCR_chapero_1; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00726; UIM; 4.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50330; UIM; 2.
PE   2: Evidence at transcript level;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023}.
FT   REPEAT          39..71
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          279..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..564
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..605
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  68204 MW;  870CCED1BCAA81B8 CRC64;
     MASPCPTFPL HRLVWANRHR ELEAALHSHQ HDIEQEDPRG RTPLELAVSL GNLESVRVLL
     RHNANVGKEN RQGWAVLQEA VSTGDPEMVQ LVLQYRDYQR ATQRLAGIPE LLNKLRQAPD
     FYVEMKWEFT SWVPLVSKMC PSDVYRVWKR GESLRVDTSL LGFEHMTWQR GRRSFIFKGQ
     EAGALVMEVD HDRQVVHAET LGLALQEPEA LLAAMRPSEE HVASRLTSPI VSTHLDTRNV
     AFERNKCGIW GWRSEKMETV SGYEAKVYSA TNVELVTRTR TEHLSDQDKS RSKGGKTPFQ
     SFLGMAQQHS SHTGAPVQQA ASPTNPTAIS PEEYFDPNFS LESRNIGRPI EMSSKVQRFK
     ATLWLSEEHP LSLGDQVTPI IDLMAISNAH FAKLRDFITL RLPPGFPVKI EIPLFHVLNA
     RITFSNLCGC DEPLSSVWVP APSSAVATSG NPFPCEVDPT VFEVPEGYSV LGTERSEPLR
     DEDDDLLQFA IQQSLLEAGT EAEQVTVWEA LTNTRPGARP PPQATVYEEQ LQLERALQES
     LRLSTEPRGP ASPPRTPPAP GPPSFEEQLR LALELSSREQ EERERRGQQE EEDLQRILRL
     SLTEH
//