ES8L2_PONAB
ID ES8L2_PONAB Reviewed; 716 AA.
AC Q5RC07;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Epidermal growth factor receptor kinase substrate 8-like protein 2;
DE Short=EPS8-like protein 2;
DE AltName: Full=Epidermal growth factor receptor pathway substrate 8-related protein 2;
DE Short=EPS8-related protein 2;
GN Name=EPS8L2; Synonyms=EPS8R2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role
CC in membrane ruffling and remodeling of the actin cytoskeleton (By
CC similarity). In the cochlea, is required for stereocilia maintenance in
CC adult hair cells (By similarity). {ECO:0000250|UniProtKB:Q99K30,
CC ECO:0000250|UniProtKB:Q9H6S3}.
CC -!- SUBUNIT: Interacts with ABI1. Part of a complex that contains SOS1,
CC ABI1 and EPS8L2. Associates with F-actin (By similarity).
CC {ECO:0000250|UniProtKB:Q9H6S3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H6S3}. Cell
CC projection, stereocilium {ECO:0000250|UniProtKB:Q99K30}. Note=Localizes
CC at the tips of the stereocilia of the inner and outer hair cells.
CC {ECO:0000250|UniProtKB:Q99K30}.
CC -!- SIMILARITY: Belongs to the EPS8 family. {ECO:0000305}.
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DR EMBL; CR858475; CAH90703.1; -; mRNA.
DR RefSeq; NP_001125388.1; NM_001131916.1.
DR AlphaFoldDB; Q5RC07; -.
DR SMR; Q5RC07; -.
DR STRING; 9601.ENSPPYP00000023859; -.
DR GeneID; 100172293; -.
DR KEGG; pon:100172293; -.
DR CTD; 64787; -.
DR eggNOG; KOG0825; Eukaryota.
DR eggNOG; KOG3557; Eukaryota.
DR InParanoid; Q5RC07; -.
DR OrthoDB; 218804at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032421; C:stereocilium bundle; ISS:UniProtKB.
DR GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR CDD; cd01210; PTB_EPS8; 1.
DR CDD; cd11764; SH3_Eps8; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 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; PTHR12287; 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; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..716
FT /note="Epidermal growth factor receptor kinase substrate 8-
FT like protein 2"
FT /id="PRO_0000239086"
FT DOMAIN 46..202
FT /note="PID"
FT DOMAIN 493..552
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6S3"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99K30"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6S3"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6S3"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6S3"
SQ SEQUENCE 716 AA; 80812 MW; 2A2A4747ED160CE5 CRC64;
MSQSGTMSCC PGATNGSLGR SDGVAKMSPK DLFEQRKKYS NSNVIMHETS QYHVQHLATF
IMDKSEAITS VDDAIRKLVQ LSSKEKIWTQ EMLLQVNDQS LRLLDIESQE ELENFPLPTV
QRSQTVLNQL RYPSVLLLVC QDSEQSKPDV HFFHCDEVEA ELVHEDIESA LADCRLGKKM
RPQTLKGHQE KIRQRQSILP PPQGPAPIPF QHRGGDSPQA KNRVGPQVPL SEPGFRRRES
QEEEPRALLA QKIEKETQIL NCALDDIEWF VARLQKAAEA FKQLNQRKKG KKKGKKAPAE
GVLTLRARPP SEGEFIDCFQ KTKLAINLLA KLQKHIQNPS AAELVHFLFG PLDLIVNTCG
GPDIARSVSC PLLSRDAVDF LRGHLVPKEM SLWESLGESW MRPRSEWPWE PQVPLYVPKF
HSGWEPPMDV LQEAPWEVEG LASAPIEEVS PVSRQSIRNS QKHSPTSEPT PPGDALPPVS
SPHTHRGYQP TPAMAKYVKI LYDFTARNAN ELSVLKDEVL EVLEDGRQWW KLRSRSGQAG
YVPCNILGEA RPEDAGAPFE QAGQKYWGPA SPTHKLPPSF PGNKDELMQH MDEVNDELIR
KISNIRAQPQ RHFRVERSQP VSQPLTYESG PDEVRAWLEA KAFSPRIVEN LGILTGPQLF
SLNKEELKKV CGEEGVRVYS QLTVQKAFLE KQQSGSELEE LMNKFHSMNQ RRGEDS
