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Database: UniProt
Entry: A0A093H491_DRYPU
LinkDB: A0A093H491_DRYPU
Original site: A0A093H491_DRYPU 
ID   A0A093H491_DRYPU        Unreviewed;       588 AA.
AC   A0A093H491;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Ankyrin repeat domain-containing protein 13A {ECO:0000313|EMBL:KFV77358.1};
GN   ORFNames=N307_00962 {ECO:0000313|EMBL:KFV77358.1};
OS   Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX   NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV77358.1, ECO:0000313|Proteomes:UP000053875};
RN   [1] {ECO:0000313|EMBL:KFV77358.1, ECO:0000313|Proteomes:UP000053875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV77358.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL217402; KFV77358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093H491; -.
DR   STRING; 118200.A0A093H491; -.
DR   Proteomes; UP000053875; Unassembled WGS sequence.
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:SF4; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 13A; 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; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50330; UIM; 2.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053875}.
FT   REPEAT          40..72
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          73..96
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ   SEQUENCE   588 AA;  66919 MW;  B9361959FF3BAB2D CRC64;
     MSSPGRASSD YPLHVLVWNN DYRRLDVELQ DKDVDQRDPR GRTLLHLAVS LGYIESAKVL
     LQHKADVTKE NGQGWTVLHE AVSTGDPEMV QMILQHRDYQ QTAMTLGGVP ELLQKINETP
     DFYVEMKWEF TSWAPSASPP RAVFQSSPQL CCLSLDTFKL GFENMSWERG RRSLIFKGED
     AGGWAELIEI NHDEKFVTTE RFEISQHMKR LTLGSMTPKR KDVERRLTSP IINTCLDTKN
     IAFERTTSGF WVWKTERAEG VNGYEAKVYF ANNVNVVTKI RTEHLTEEEK KRYKADRSPL
     ESFLGTVEHE YGAQSTTKTT EYAASNNPTA ITLEEYFDPG FDLRGRDIGR PKEVTIRTQK
     FKATLWMSEE FPLSLMEQVT PIIDLMARTS AHFARLRDFI TLEFPPGFPV KIEIPLFHVL
     NARITFENVN GCRTADKTSS QAVGAAQCES GANFEVDQSV FEIPKSYHVQ DDGRNIHVQD
     EDNEIMQFAI QQSLLESGGS KDLGVHSNGA VAYSQDFNIQ YQRALQESLL TSSGTSLCST
     PSEPSSFEKD LQLAMELSVR EQEERERQRR EEEDAELQQA LQLSLVEK
//
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