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Database: UniProt
Entry: A0A6A5DU92_PERFL
LinkDB: A0A6A5DU92_PERFL
Original site: A0A6A5DU92_PERFL 
ID   A0A6A5DU92_PERFL        Unreviewed;      1379 AA.
AC   A0A6A5DU92;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   13-SEP-2023, entry version 10.
DE   RecName: Full=I/LWEQ domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PFLUV_G00205100 {ECO:0000313|EMBL:KAF1377857.1};
OS   Perca fluviatilis (European perch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX   NCBI_TaxID=8168 {ECO:0000313|EMBL:KAF1377857.1, ECO:0000313|Proteomes:UP000465112};
RN   [1] {ECO:0000313|EMBL:KAF1377857.1, ECO:0000313|Proteomes:UP000465112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:KAF1377857.1};
RA   Roques C., Zahm M., Cabau C., Klopp C., Bouchez O., Donnadieu C., Kuhl H.,
RA   Gislard M., Guendouz S., Journot L., Haffray P., Bestin A., Morvezen R.,
RA   Feron R., Wen M., Jouanno E., Herpin A., Schartl M., Postlethwait J.,
RA   Schaerlinger B., Chardard D., Lecocq T., Poncet C., Jaffrelo L.,
RA   Lampietro C., Guiguen Y.;
RT   "A chromosome-scale genome assembly of the European perch, Perca
RT   fluviatilis.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SLA2 family.
CC       {ECO:0000256|ARBA:ARBA00010135}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAF1377857.1}.
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DR   EMBL; VHII01000017; KAF1377857.1; -; Genomic_DNA.
DR   OrthoDB; 7775at2759; -.
DR   Proteomes; UP000465112; Chromosome 17.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR   Gene3D; 1.20.5.1700; -; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 6.10.250.920; -; 2.
DR   Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR   InterPro; IPR011417; ANTH_dom.
DR   InterPro; IPR013809; ENTH.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR032422; HIP1_clath-bd.
DR   InterPro; IPR035964; I/LWEQ_dom_sf.
DR   InterPro; IPR002558; ILWEQ_dom.
DR   InterPro; IPR030224; Sla2_fam.
DR   PANTHER; PTHR10407; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR10407:SF10; HUNTINGTIN-INTERACTING PROTEIN 1-RELATED PROTEIN; 1.
DR   Pfam; PF07651; ANTH; 1.
DR   Pfam; PF16515; HIP1_clath_bdg; 2.
DR   Pfam; PF01608; I_LWEQ; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SMART; SM00307; ILWEQ; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF109885; I/LWEQ domain; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50945; I_LWEQ; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000465112}.
FT   DOMAIN          19..147
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   DOMAIN          861..1102
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000259|PROSITE:PS50945"
FT   REGION          1102..1379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          362..396
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          470..666
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1116..1130
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1132..1291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1292..1306
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1307..1363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1379 AA;  154012 MW;  B5D404D716F5A656 CRC64;
     MSKTKTKSDN KTEKALAAEK EQFNKQQLHN ISKTLISGET PLKEKYVRNI IMGTHKEGGA
     STFWSYTLNL PLSSNSMISW KFCYLLHKVL RDGHRNAVRD SHRYCRNVKD MGILWGNLHD
     RYGHIVALSA KFLCLKMEFH AKHKVIPANL EASDETFDRE TGSDVTKVLD ITQELMDYWD
     AGLKMEETVL RQLDANGAKS TTPAGQCRLT PLIPLILDCS LLYHFSVLSM FKLHSRIAPD
     VLLGHRERFR DLFNSLTQFF DRARETEFFK TIIQIPDLPD EPPNFLRASA LAEYKKPVVV
     MPNEERHNEE EVEMQPELRE APQYYMLSQM GGPDASAEQR ETENESLKRE LQVLKPELQL
     IKTEAQRCLT ELKAQVNRLE AEVDEQRTQK QMAMMEKEHL RMEVEALRCT NVANVGAQIG
     FKEADHRAQA AELRFAQLKE RHAELITSHA DLMKKNAETV KLLSGTQHGQ DDLLKYKQQL
     ENELENLRQE KRNTTSQQQQ EVQRLNTELL EQRAELALLR STLDNKDKEG SQVSSSLAAL
     QAERDVLLRS AREKDAELSS LRQQAQQQQG SLDLERERLQ RELEALRAQL QQQLAINAEQ
     KLEIDRLRRE LDSTRAELNR ANSALQSKEM SGTQLSSSVA GLQAEREALL RSMRDQEGEL
     NSLRQQAQLH HSSLEQERQR SSVELGNLHA QLQQQACREA ELSKKLQDEQ FCLLQCAVVE
     AEGIILDAVA KLDDPIHVSC ICSPDYLVNR ADITLRSIDK IQQSHVVYLG NRNDASGLLR
     SVTQFSHLAA DTIVNGSATS HSAPTDQADR LTDSCRDCAN HCLQFLKDLK LQASLQRADP
     SAVRYTVQRI LALGQDLRPK GQDVMKGELA YMVDKEMSAT STAIEEAVLR MDEILNQAKR
     ETSGIKLEVN QSILGSCSDL MKAVHMLVTA STDLQKDIVE GGRGAASVTE FYAKNSRWTE
     GLISASKAVG WGATQLLDSA DRVVGEKGTY EELIACSHEI AASTAQLVAA SKVKADRNNK
     KLNTLKQASR HVNDMAAVVV TSTKHGQQQI SDQGVMDFSG MSLIKLKTEE MEVQVKVLQL
     ESQLEQERVR LGELRKRHYK LDASGDDGAD AEDGADSFPP PPPPTLLECA PVPPSFSQTQ
     PYLNTQSYAA SNPFAPAQTP TQSFSVPQSY TQTNTYTPSQ TSIPSQTYTP SQTSIPSQTY
     TPSQTSIPSQ TYTPSQTSIP SQTYTPSQTS IPSQTYTPSQ TSIPSQTYTP SQTSIPSQTY
     TPSQTSIPSQ TYTPSQTSIP SQTYTPSQSF IPTQPYTPPQ PFTPNPTQTY LKPQSYSLSA
     PSTNPSSLSR PQSPSLPRAS PQNNTESTKP ASRKPSIFTK SGNLLKNAFK RGETGTGES
//
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