ID A0A317WKI1_9EURO Unreviewed; 1262 AA.
AC A0A317WKI1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein END3 {ECO:0000256|ARBA:ARBA00017312};
DE AltName: Full=Actin cytoskeleton-regulatory complex protein end3 {ECO:0000256|ARBA:ARBA00013889};
DE AltName: Full=Cytoskeletal adapter protein sagA {ECO:0000256|ARBA:ARBA00032224};
GN ORFNames=BO70DRAFT_369917 {ECO:0000313|EMBL:PWY86873.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY86873.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY86873.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY86873.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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}.
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:PWY86873.1}.
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DR EMBL; MSFL01000007; PWY86873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317WKI1; -.
DR STRING; 1448321.A0A317WKI1; -.
DR VEuPathDB; FungiDB:BO70DRAFT_369917; -.
DR OrthoDB; 12127at2759; -.
DR Proteomes; UP000247233; Unassembled WGS sequence.
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; 1.10.8.10; 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; IPR018247; EF_Hand_1_Ca_BS.
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; 3.
DR SMART; SM00027; EH; 3.
DR SUPFAM; SSF47473; EF-hand; 3.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT DOMAIN 16..102
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 140..231
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 173..208
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 290..380
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 323..358
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1229..1262
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 238..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 519..637
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 392..406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..972
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1262 AA; 133371 MW; 5D90CBE862C47D15 CRC64;
MADNARNPNL NLTPEEKRAF YQLFQAADTT NLGVITGEVA VPFFEKTHLA PETLGLIWQI
ADRENRGLLT PSGFGVVLRL IGHAQAGRAP TEELAYQAGP LPRFDGIVID ASPAPREAGT
TSPTPAAGAP IRVPPLNPED VNKFVSLFEK SDVSKSGVLS GETSKQIFER ARLPNEVLGR
IWNLADTRQQ GALDATEFVI AMHLLTSYKS GVMRGIPQTL PPGLYDAAAR RGPIRASVGS
RQGLDVPPVP AIPKQFTGPQ RTQSPISRQA FGSPLSAQST GSDWLVTPQE KAMFDNIFAT
VDTAKAGSIS GDQAVSFFMG AQLPEETLAQ IWDLADIDAD GQLTKDEFAV AMYLVRLTRS
GKEAMPQTLP PALIPPSMRR PGSAHFGPAA PAPAQVAPPA PIPAPPSAAD DLFGLDALSA
PVSGVPAAPS QFPQSTGGSN AAFQMPSSPG SRASPQTAST TFKPFVPTSS FGQSLHPQVT
GASAGVPPAV RSPPPPADDL LGDNDPEESK KLTQETTELA NLSNQIGSLA TEMQNVQTKR
TSAEHDLSQT SQQKRDFETR LAQARAMYEQ EVKNFKALEE RRNASRAETN RLQQEFALLD
GSRQDLQNQY NQVSAALSAD QQENLSLKEK IRQANAAVAQ LKPALEKARS DARQQKGMVA
INKKQLATVE GEHEKIQEEI KALSEEHPRE LEESVPVPGD FAAVTSPAES TTSQNTNPFF
KRTATGSSDN NALSPQISND QQRAFDSLFG PSFASPVAAT PPPAVSFRAE SLPTSGVPTP
SVSPPPASGF ALEPPAPAQS RQLTPSVLPL GESHSATSST MVSPPGSRFG GQDTASLGTT
SQTAGSEWVD PSSGELAQPA TSPFDEIEES NQRFPEVPVI AGQATGDAAS PSGDDKLAES
KDLSFDELFG GPAHKRSQSQ KENDFEEAFA AMKNGPGATK SNGPSPPAES EFPPIRELDD
DDDDDDSTDN EATMGFDDNF TPAFPPQSQV AAAPKPDSLE PSQLAAFPTP TSSEPPAAES
QLSPPNYEET VGKQEPGSMP PEFNGLLPSR EDPTAAPDAP HSVDSSTGEP IVGGEVQHND
STTPSGGKTS GPDFEAAFAG LNLAPANEAD DDEEEEDDFE TAVNSKNNVD FDFSFDNPSA
QKISNNADGN AASEFFNFDK NVSSSPPGSA TLPSDSNAKS QTHDWEALFA PLDNAGAAAS
GTNGVSNPAE LAPSAGNSKA PGWALQTGTE DDQILQRLTG MGFPRDESLD ALEKFDYNLD
KV
//
