GenomeNet

Database: UniProt
Entry: L5KKX3_PTEAL
LinkDB: L5KKX3_PTEAL
Original site: L5KKX3_PTEAL 
ID   L5KKX3_PTEAL            Unreviewed;       848 AA.
AC   L5KKX3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Epidermal growth factor receptor kinase substrate 8 {ECO:0000313|EMBL:ELK11972.1};
GN   ORFNames=PAL_GLEAN10015648 {ECO:0000313|EMBL:ELK11972.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK11972.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the EPS8 family.
CC       {ECO:0000256|ARBA:ARBA00006197}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KB030666; ELK11972.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KKX3; -.
DR   STRING; 9402.L5KKX3; -.
DR   eggNOG; KOG3557; Eukaryota.
DR   InParanoid; L5KKX3; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01210; PTB_EPS8; 1.
DR   CDD; cd09540; SAM_EPS8-like; 1.
DR   CDD; cd11764; SH3_Eps8; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR039801; EPS8-like.
DR   InterPro; IPR033928; EPS8_PTB.
DR   InterPro; IPR035462; Eps8_SH3.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041418; SAM_3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12287:SF21; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE 8; 1.
DR   PANTHER; PTHR12287; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE EPS8-RELATED PROTEIN; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF18016; SAM_3; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:ELK11972.1};
KW   Receptor {ECO:0000313|EMBL:ELK11972.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:ELK11972.1}.
FT   DOMAIN          557..616
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          229..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..672
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   848 AA;  94729 MW;  6D45EC8D364FB541 CRC64;
     MAFLVSLSVN SFGVDFSPRN IWVKVTMNGH ISNHPSGFGI YPSQMNGYGT SSTFSQMDRE
     HSSKPSAKAL YEQRKNYARD SISSVSNTTH YHVEHLTTFV LDRKDAMITI DDGIRKLKLL
     DAKGKVWTQD MLLQVDDRAV SLIDLESKNE LENFPFNTIQ HCQAVMHSCN YDSILALVCK
     EPTQNKPDLH LFQCDEVKAN LISEDIESAI SDSKGGKQKR RPDALRVISN ADHGIPPPPR
     APAPVPPGTV TQVDVRSRVA AWSAWAADQG DFEKQRQYHG HEETPEMMAA RIDRDVQILN
     HILDDIEFFI TKLQKAAEAF SELSKRKKTK KGKRKGPGEG VLTLRAKPPP PDEFIDCFQK
     FKHGFNLLAK LKSHIQNPSA ADLVHFLFTP LNMVIQATGG SELASSVLSP LLTKDTIDFL
     NYTVNTDERQ LWMSLGETWM KPRAEWPKEQ FIPPYVPRFR NGWEPPMLNF MGAPVEQDIY
     QLVGSVAGAA EQHRHETKRY ATEQSSVLEY APPPPDGYAF NNIYTRGTHL DQGEAAVAFK
     PAPNRHVDRN YDPLITQPKK YAKSKYDFVA RNGSELSVLK DDILEILDDR KQWWKVRNAS
     GNSGFVPNNI LDIVRPTESG VGRADPPYTH TIQKQRMEYG PRSTDPPSAP SPPPTPAPVP
     VPLPPSIPAP VPVSKVPANV TRQNSSSSDS GGSTVRDSQR HKQLPVDRRK SQMEEVQDEL
     IHRLTIGRSA AQKKFHVPRQ NVPVVNITYD STPEDVKTWL QSKGFNPMTV NSLGVLNGAQ
     LFSLNKDELK TVCPEGARVF NQITVQKAAL EDISGSSELQ EIMRRRQEKI SAAASDSGVE
     SFDEGSSH
//
DBGET integrated database retrieval system