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Database: UniProt
Entry: A0A091DID3_FUKDA
LinkDB: A0A091DID3_FUKDA
Original site: A0A091DID3_FUKDA 
ID   A0A091DID3_FUKDA        Unreviewed;       111 AA.
AC   A0A091DID3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=TYRO protein tyrosine kinase-binding protein {ECO:0000256|ARBA:ARBA00022356};
DE   AltName: Full=DNAX-activation protein 12 {ECO:0000256|ARBA:ARBA00031252};
GN   ORFNames=H920_08560 {ECO:0000313|EMBL:KFO30050.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO30050.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO30050.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO30050.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TYROBP family.
CC       {ECO:0000256|ARBA:ARBA00009791}.
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DR   EMBL; KN122516; KFO30050.1; -; Genomic_DNA.
DR   RefSeq; XP_010630173.1; XM_010631871.1.
DR   AlphaFoldDB; A0A091DID3; -.
DR   STRING; 885580.ENSFDAP00000003617; -.
DR   Ensembl; ENSFDAT00000017256; ENSFDAP00000003617; ENSFDAG00000013023.
DR   GeneID; 104867497; -.
DR   CTD; 7305; -.
DR   eggNOG; ENOG502SCVI; Eukaryota.
DR   OMA; FPECNCS; -.
DR   OrthoDB; 4557845at2759; -.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:InterPro.
DR   GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR   Gene3D; 1.10.287.770; YojJ-like; 1.
DR   InterPro; IPR009861; HCST.
DR   InterPro; IPR026200; Tyrobp.
DR   PANTHER; PTHR17554; TYRO PROTEIN TYROSINE KINASE-BINDING PROTEIN; 1.
DR   PANTHER; PTHR17554:SF2; TYRO PROTEIN TYROSINE KINASE-BINDING PROTEIN; 1.
DR   Pfam; PF07213; DAP10; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:KFO30050.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:KFO30050.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..111
FT                   /note="TYRO protein tyrosine kinase-binding protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001871703"
FT   TRANSMEM        37..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          70..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   111 AA;  12062 MW;  F6253F593D819B73 CRC64;
     MGGLEPFWQL LLLPLLLTVA GVSPVQAQSG CNCTPMSAGV LAGIVLGDLV LTLLIALAVY
     SLGRLVPRGR KTAQMARKQP ITETESPYQE LQGTRSDIYS DLNTQRQPYY K
//
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