ID A0A2L2TS67_9HYPO Unreviewed; 1247 AA.
AC A0A2L2TS67;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEI69021.1};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI69021.1, ECO:0000313|Proteomes:UP000245910};
RN [1] {ECO:0000313|Proteomes:UP000245910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA King R.;
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC required for the internalization of endosomes during actin-coupled
CC endocytosis. The complex links the site of endocytosis to the cell
CC membrane-associated actin cytoskeleton. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization.
CC {ECO:0000256|ARBA:ARBA00025194}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000256|ARBA:ARBA00011159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; LN649231; CEI69021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2TS67; -.
DR STRING; 56646.A0A2L2TS67; -.
DR OrthoDB; 12127at2759; -.
DR Proteomes; UP000245910; Chromosome iii.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00052; EH; 3.
DR CDD; cd14270; UBA; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
DR PANTHER; PTHR11216:SF161; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE CLONE 15, ISOFORM A; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00027; EH; 3.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF47473; EF-hand; 3.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 3.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Reference proteome {ECO:0000313|Proteomes:UP000245910}.
FT DOMAIN 15..91
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 149..239
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 291..326
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 292..383
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 327..360
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1206..1246
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 107..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 672..699
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 110..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..975
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1247 AA; 131684 MW; 67A8F4B61CB5C6EC CRC64;
MAADEAPNLN LSPDEKRTYG QLFRQADSES VGVVVGEIAV RFFHKTGLDS RILGEIWQIA
DKENRGFLTP AGFGIALRLI GHAQAGREPT PEIALQQAPL PRFDGIAPQP TGGIPPPPPV
PVSSPPPPAA LQAQSTGGPI RIPPLTPEKV TQYTGLFERQ PLQNGQLPGD QARGIFEKSG
LPNEALGRIW QLADTEQRGA LILTEFIIAM HLLTSMKTGA LRSLPNVLPP GLYEAASRRG
PVPRQSSTGP GISAIPRQLS GTAQVRTNSP LGRPPMSPQQ SGASDWAVTP ADKARFDQIY
ADLDKGNKGY ITGEEAVSFF SQSNLPEDSL AQIWDLADTN SQGQLSREQF AVAMYLIRQQ
RTGRSVPLPT TLPANLIPPS LRSQVRPHTA TSAFDPPPAP VIQAPPQPKS ALDDLFGLDS
GSSTPAPPPP AQAPMSTGGS NANDPFAGGS SFTPTSPVKP ALTGTSGSNF KPFVPSSSFG
RGLTQHPTGG STGSGQKLST PSASEDLLSD NDEASKNISE ETTELANLSN QISSLSKQTQ
DVQAKRTTTQ NELNQATSQK QNFEQRLAQL RSLYEKEAQD TRALEEQLSN ARKETSKLQA
ECMTLEGTYR DTQAQHQQTL QALQADKQEN TNLRERIRVV NGEIAQLKPQ IEKLKSEARQ
QKGLVAINKK QLSTTEGERD KLKTEAEDLT KSIDDLRQAN TGSPASVSAQ IASPAASVSS
ANNPFFRRTA STDIMGAFAS PPPTKNASDK SFDDLFGPAF PPSSSATPPP AAQSGFFKPQ
HTGASNASAG SYNTPPVQGS PVMSRQATLA ADPPAPPESR QISSSFLPFP DHTESLSSSR
QVSPPASRLD DPLHGSITPV PGDFKSSDSV GSVPGAFPGE DLAESKDTLS TPNDAPREAA
KDDESKPADS ADPFGGNDEA KAKADFENAF AAFTTAKTQS KPSPEANKSS AFDSEFPPIS
ELERDEEEDS DSSSDNGGFD DNFTPASPPA KPATEGSPEL THAAPASTSP QPAQEANSPE
EPKAASAEQP SSPATITETN AQKSSVDDIF GAAATGTAPA SQQAAPSNPP QAKGGFEDLD
SDFEGLEDAK EGSADEDFAN ISRSGLDDFN PVFDSSPPGS QAKTESTAFG NESFDFVSAS
STGPTQPAAG AQQQKAPEAH DWDAIFSGMD SPSAAAAQPA PAEKPEGAEP HPGQQALNRT
FSTESEHDDP ILKSLTGMGY KRSEALEALE KYDYDLDKAA NYLASRS
//
