ID F1RUX4_PIG Unreviewed; 604 AA.
AC F1RUX4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Ankyrin repeat domain 13D {ECO:0000313|Ensembl:ENSSSCP00000013734.3};
GN Name=ANKRD13D {ECO:0000313|Ensembl:ENSSSCP00000013734.3,
GN ECO:0000313|VGNC:VGNC:85327};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000013734.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000013734.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000013734.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000013734.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; F1RUX4; -.
DR PaxDb; 9823-ENSSSCP00000013734; -.
DR Ensembl; ENSSSCT00000014120.5; ENSSSCP00000013734.3; ENSSSCG00000012917.5.
DR VGNC; VGNC:85327; ANKRD13D.
DR eggNOG; KOG0522; Eukaryota.
DR GeneTree; ENSGT00950000182928; -.
DR HOGENOM; CLU_026137_2_0_1; -.
DR OMA; KGQHDIE; -.
DR TreeFam; TF314176; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Bgee; ENSSSCG00000012917; Expressed in blood and 44 other cell types or tissues.
DR ExpressionAtlas; F1RUX4; baseline and differential.
DR Genevisible; F1RUX4; SS.
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; 3.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
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 540..604
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 571..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 67789 MW; 8798FF093C1A043C CRC64;
MAGPGPTFPL HRLVWANRHR ELEAALHSRQ HDIEQEDPRG RTPLELAVSL GNLESVRVLL
RHNANVGKES CQGWAVLQEA VSTGDPEMVQ LVLQYRDYQR ATQRLAGIPE LLHKLRQAPD
FYVEMKWEFT SWVPLVSKMC PSDVYRVWKR GESLRVDTSL LGFEHMTWQR GRRSFIFKGQ
EVGALVMEVD HDRQVVHTET LGLALHEPEA LLAAMRPSEE HVASRLTSPI VSTHLDTRNV
AFERNKCGIW GWRSEKMETV SGYEAKVYSA TNVELVTRTR TEHLSDQDKS RSKGGKTPFQ
SFLGMAQQHS SHNGAPVQQA ASPTNPTAIS PDEYFDPNFS LESRNIGRPI EMSSKVQRFK
ATLWLSEEHP LSLGDQVTPI IDLMAISNAH FAKLRDFITL RLPPGFPVKI EIPLFHVLNA
RITFGNLCGC DEPLSSVWAP APGSAVAASG SPFPCEVDPA VFEVPEGYSV LGTERSEPLR
DEDDDLLQFA IQQSLLEAGT EAEQVTVWEA LSNTRPGTHL PQGTAFEEQL QLERALQESL
RMSTETGGPG SPHRTPPALA PPSFEEQLRL ALELSSREQE ERERRGQQEE EDLQRILQLS
LTEH
//
