ID   A7BFV9_RAT              Unreviewed;       897 AA.
AC   A7BFV9;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Epidermal growth factor receptor pathway substrate 15 {ECO:0000313|EMBL:BAF74783.1};
GN   Name=Eps15 {ECO:0000313|RGD:1305550};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:BAF74783.1};
RN   [1] {ECO:0000313|EMBL:BAF74783.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17626015; DOI=10.1074/jbc.M703815200;
RA   Uezu A., Horiuchi A., Kanda K., Kikuchi N., Umeda K., Tsujita K.,
RA   Suetsugu S., Araki N., Yamamoto H., Takenawa T., Nakanishi H.;
RT   "SGIP1alpha is an endocytic protein that directly interacts with
RT   phospholipids and Eps15.";
RL   J. Biol. Chem. 282:26481-26489(2007).
CC   -!- INTERACTION:
CC       A7BFV9; O14526: FCHO1; Xeno; NbExp=2; IntAct=EBI-6095043, EBI-719823;
CC       A7BFV9; Q3UQN2: Fcho2; Xeno; NbExp=2; IntAct=EBI-6095043, EBI-6094986;
CC       A7BFV9; Q8VD37: Sgip1; Xeno; NbExp=4; IntAct=EBI-6095043, EBI-776269;
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DR   EMBL; AB262963; BAF74783.1; -; mRNA.
DR   AlphaFoldDB; A7BFV9; -.
DR   IntAct; A7BFV9; 8.
DR   MINT; A7BFV9; -.
DR   iPTMnet; A7BFV9; -.
DR   PhosphoSitePlus; A7BFV9; -.
DR   AGR; RGD:1305550; -.
DR   RGD; 1305550; Eps15.
DR   GO; GO:0016235; C:aggresome; ISO:RGD.
DR   GO; GO:0030122; C:AP-2 adaptor complex; ISO:RGD.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
DR   GO; GO:0060170; C:ciliary membrane; ISO:RGD.
DR   GO; GO:0030132; C:clathrin coat of coated pit; ISO:RGD.
DR   GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR   GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:RGD.
DR   GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR   GO; GO:0048268; P:clathrin coat assembly; ISO:RGD.
DR   GO; GO:0032456; P:endocytic recycling; IMP:RGD.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   GO; GO:0006895; P:Golgi to endosome transport; ISO:RGD.
DR   GO; GO:0001921; P:positive regulation of receptor recycling; IMP:RGD.
DR   GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR   GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISO:RGD.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR   GO; GO:0070086; P:ubiquitin-dependent endocytosis; ISO:RGD.
DR   GO; GO:0046718; P:viral entry into host cell; ISO:RGD.
DR   CDD; cd00052; EH; 3.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 3.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000261; EH_dom.
DR   InterPro; IPR003903; UIM_dom.
DR   PANTHER; PTHR11216; EH DOMAIN; 1.
DR   PANTHER; PTHR11216:SF54; EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15; 1.
DR   Pfam; PF12763; EF-hand_4; 3.
DR   SMART; SM00054; EFh; 4.
DR   SMART; SM00027; EH; 3.
DR   SMART; SM00726; UIM; 2.
DR   SUPFAM; SSF47473; EF-hand; 3.
DR   SUPFAM; SSF90257; Myosin rod fragments; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS50031; EH; 3.
DR   PROSITE; PS50330; UIM; 2.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Receptor {ECO:0000313|EMBL:BAF74783.1}.
FT   DOMAIN          15..104
FT                   /note="EH"
FT                   /evidence="ECO:0000259|PROSITE:PS50031"
FT   DOMAIN          48..83
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          128..216
FT                   /note="EH"
FT                   /evidence="ECO:0000259|PROSITE:PS50031"
FT   DOMAIN          160..195
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          223..258
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          224..314
FT                   /note="EH"
FT                   /evidence="ECO:0000259|PROSITE:PS50031"
FT   REGION          536..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          335..474
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        536..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..791
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   897 AA;  98613 MW;  8AC00E465C9DB8D7 CRC64;
     MAAAAQLSLT QLSSGNPVYE KYYRQVEAGN TGRVLALDAA AFLKKSGLPD LILGKIWDLA
     DTDGKGVLNK QEFFIALRLV ACAQNGLEVS LSSLNLAVPP PRFHDSSSPL LTSGTSVAEL
     PWAVKSEDKA KYDAIFDSLS PVDGFLSGDK VKPVLLNSKL PVEILGRVWE LSDIDHDGKL
     DRDEFAVAMF LVYCALEKEP VPMSLPPALV PPSKRKTWVV SPAEKAKYDE IFLKTDKDMD
     GYVSGLEVRE TFLKTGLPST LLAHIWALCD TKNCGKLSKD QFALAFHLIN QKLIKGIDPP
     HSLTPEMIPP SDRSSLQKNT IGSSPVADFS AIKELDTLNN EIIDLQREKN NVEQDLKEKE
     DTVRQRTTEA QDLQDEVQRE SLNLQKLQAQ KQQVQELLDE LDEQKAQLEE QLKEVRKKCA
     EEAQLISSLK AEITSQESQI STYEEELSKA REELSRLQQE TAQLEESVES GKAQLEPLQQ
     HLQDSQQEIS SMQMRLAMKD LETDNNQSNW CSSPQSILVN GAADYCSLST SSSETANLNE
     HAEGQNNLES EPIHPESSVR SSPEIAPSDV TDESEVVTAA DIEKVSPRFD DDKHSKEEDP
     FNVESSSLTD AVADTNLDFF QSDPFVGSDP FKDDPFGKID PFGGDPFKGS DPFASDCFFK
     QTSTDPFATS STDPFSASSN SSNTSVETWK HNDPFAPGGT VVAATDSATD PFASVFGNES
     FGDGFADFST LSKVSNEDPF NPTISSSASS VVIPKPVLEE TPSKSEDVPP ALPPKTGTPT
     RPCPPPPGKR PINKLDSSDP FKLNDPFQPF PGNDSPKEKD PDMFCDPFTS SSTTANKEAE
     PSNFANFSAY PSEEDMIEWA KRESEREEEQ RLARLNQQEQ EDLELAIALS KSEISEA
//