ID A0A2H3IPJ6_9EURO Unreviewed; 557 AA.
AC A0A2H3IPJ6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ENTH/VHS {ECO:0000313|EMBL:PCH02814.1};
GN ORFNames=PENO1_035650 {ECO:0000313|EMBL:PCH02814.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH02814.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH02814.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH02814.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the epsin family.
CC {ECO:0000256|ARBA:ARBA00010130}.
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:PCH02814.1}.
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DR EMBL; NPFK01000077; PCH02814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IPJ6; -.
DR STRING; 290292.A0A2H3IPJ6; -.
DR OrthoDB; 1532at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR CDD; cd16991; ENTH_Ent1_Ent2; 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; EPSIN/ENT-RELATED; 1.
DR PANTHER; PTHR12276:SF110; FI19443P1; 1.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00726; UIM; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 10..143
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT REGION 160..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 61865 MW; F3F1EE7772D6A359 CRC64;
MSRALRSVKN VTKGYSSVQV KVRNATSNDP WGPTGTEMGE IAALTFNNPS DFYEIVDMLD
KRLNDKGKNW RHVLKSLKVL DYCLHEGSEL VVTWARKNVY IIKTLREFQY IDDEGRDVGQ
NVRVSAKELT ALILDEDRLR SERSDRKLWK SRVSGIDEGI QGYGGSSAAG GHRPNRDRRE
RRGREEDDTE YQLAIEASKV EAEEERKRRE RAARDDDDDD LARAIKLSKE EEELRRRELE
ESNAKSLFDD TPVAAAQPTG YNQGYQQQPA VDWFGNPLDT QQPLTTGYLN NQYAQPNGYQ
PTGQINAYGN GFQMQPTGYD PNQQFGQPQN NFYQNQSLQP QQTAFNNNNP YGTNPMYGQV
QQPQQDNYLQ PGSHNPWATD KQQGLDALRP MPTGSNNPFA SAINRPVSQP SRPGPPTLNT
LAEERATTAF NTMPSGPNPI ANYKAPSPLQ ASATSTKPLA TRDDGQYSRL NALLASGEGQ
DTFGNTGDLR IPAHHTAPGQ FINSAGQGFG PQPTGSNPFF HQQFTGVPQQ TGFGQSNNPF
GAPGHQQQQQ GGSLIDL
//
