ID A0A3Q3AKP4_KRYMA Unreviewed; 591 AA.
AC A0A3Q3AKP4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Epsin-3 {ECO:0000313|Ensembl:ENSKMAP00000016886.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000016886.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000016886.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the epsin family.
CC {ECO:0000256|ARBA:ARBA00010130}.
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DR RefSeq; XP_017280935.1; XM_017425446.1.
DR AlphaFoldDB; A0A3Q3AKP4; -.
DR Ensembl; ENSKMAT00000017120.1; ENSKMAP00000016886.1; ENSKMAG00000012591.1.
DR GeneID; 108241361; -.
DR CTD; 794862; -.
DR GeneTree; ENSGT00940000158217; -.
DR OMA; GHDQGIH; -.
DR OrthoDB; 1532at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR CDD; cd16990; ENTH_Epsin; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12276:SF16; EPSIN-3; 1.
DR PANTHER; PTHR12276; EPSIN/ENT-RELATED; 1.
DR Pfam; PF01417; ENTH; 1.
DR Pfam; PF02809; UIM; 3.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00726; UIM; 3.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 2.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT DOMAIN 12..144
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT REGION 142..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 63844 MW; A329B3EBC3D3F300 CRC64;
MQSSSIRRQV KNMVNNFTEA EIKVREATSN DHWGPPSTLM AEIADLTYNV VTFAEVMGII
WKRLNDHGKN WRHVYKALTL LDYLVKSGSE RVAKASRDNI FAIQTLKDFQ YLDRDGRDQG
INVREKAKQL VALLKDEEKL KRERSRALKT KSRLGGGSSG GSSSSSGYVS SSYTSHHSVE
DFSSSRCRSS SSANTTSSSR YAPDLEQAIP STTGEEELQL QLALAMSREE SEKPVKRAPA
APLDMDEDAQ LQLALSLSKE EHKQEQLSRR GNESDLQKAL EESKREMEGK GGTAFMDLVD
IFAVPADAPP IDNRWNNTSS RAAAGAGGTD PWDSLDNIPR ADSPWMVPPP SHSPPPPWEP
PSNSWAAAQN NVSNRKASGQ DLAFSGVSAP LVADPFLAPS ERTAVRGAAS NFPPRSPSDG
DFFDAAMDGD DMGINGQRTD SPDHFELSSL RESLVNPNPR TCPTPEAFLG PSAASLVNLE
ALIPTNPAAK TTNPFLSGMS APSAANPFQS EQPKLSLNQI GSAPAAPHAT SLPYSASLPL
PTSHQGATIP SSLTHPTQPG LDLPGKLPEP LLPFSSAINQ ELQESNQNPF L
//
