ID F0UQK6_AJEC8 Unreviewed; 1279 AA.
AC F0UQK6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
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};
GN ORFNames=HCEG_07398 {ECO:0000313|EMBL:EGC48183.1}, I7I53_10814
GN {ECO:0000313|EMBL:QSS50207.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|EMBL:EGC48183.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|EMBL:EGC48183.1};
RG The Broad Institute Genome Sequencing Platform;
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QSS50207.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H88 {ECO:0000313|EMBL:QSS50207.1};
RA Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT "Chromosome-level genome assembly of a human fungal pathogen reveals
RT clustering of transcriptionally co-regulated genes.";
RL Submitted (JAN-2021) 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; DS990641; EGC48183.1; -; Genomic_DNA.
DR EMBL; CP069102; QSS50207.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UQK6; -.
DR STRING; 544711.F0UQK6; -.
DR VEuPathDB; FungiDB:I7I53_10814; -.
DR HOGENOM; CLU_002006_0_0_1; -.
DR OMA; AMYLVRQ; -.
DR Proteomes; UP000008142; Unassembled WGS sequence.
DR Proteomes; UP000663419; Chromosome 1.
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; 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; 3.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00027; EH; 3.
DR SMART; SM00165; UBA; 1.
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; 1.
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};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT DOMAIN 15..101
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 140..230
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 292..382
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 325..360
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1238..1278
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 92..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1095
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 136515 MW; E02059F85FB34A92 CRC64;
MADGGHPNLN LTPEEKRVFY KLFQAADKTN LGVVTGEVAV SFFEKTSLPP ETLGLIWQIA
DTQNRGLLTP SGFGVVMRLI GHAQAGRAPT EELALQPGPL PKFSGLSKDI TEPTPQAPPV
ASSPPPGNGP VRVPPLVPDD IAKFTSLFER SEVQNGLLSG ENAKQIFERA RLPNEILGRI
WNLADTKQRG ALDTTEFIIA MHLLSAYRNG TMRVLPQTLP PGLYEAAARR GGVRTSTGSR
SSSDIPPVPA IPKQFSGSGP QRAQSPLNRP PQFQSTIPSQ PTGGDWTITP QEKAHFDTVF
ATVDKANVGY ITGDQAVEFF SNAQLPEETL ASIWDLADID SDGQLNKDEF AVAMYLVRQQ
RTTREALPQA LPPVLIPPSM RRQLQQPAPA AQIVPQNTAQ RSAAEDLFGL DVFGPPVQVA
QTTGGSNPSI QPPSSPTRAP LSASATSTFK PFVPSSSFGQ SLTPHSTGLS NAPAQQRSPP
PPSADDLLAD VDAEASKKVS QESVDLANLS NQIGSLSREM QNVQGKRAAA EHDLTQNSHQ
KKDFETRLAQ ARTMYEQEAK DFKALEERLA ALRAETRKLQ QDFALVEASR QDLQNQYNQV
NAALDADQRE NANLKEQIRQ ANAQVSQLKP LLDKARSAAR QQKGLVAINK KQLATVEGER
DRIQGEIDTT TKEVDDLRRQ ASEESSPASQ YPSVTSPAPS TASQTNPFFR RTASVSDNTR
SPPPPSSSQE PAKDAQSVFD NVFGTSFTVP SASAPPPPTT FRTESPAQQA SPAIANPPKT
SDTSGTMTPS ASPISTEHPP PPQSRQLSSS QLPIEGHQAS EASSVRPSPP ASRFGTSVTS
EPGTSPSAKS PFENEEPKPD TKLETSPNDS EKSTSQTGQE PGVSNTPGFF PADSAEAEST
KKDISFDELF GGITHARSPS QKANDFEEAF AAMKLKNGNG DSGFPEVADE KSKAVPSEFP
PIRELDDDED STDSEAAKGF DDDFSPVSPP RKNEQTSPDV VSPQTFAPPS TQGTSMPGMN
GQEPPMETSQ VTATTSNGLA HVDKNGTGAS QPALPGKKPT TPDFEAAFAG LELAPAKEAD
DDDDDDDDDD DDFESPFNKD SSNFDMTFDS PGAQSKSSTI ARANTGTSSG NNTTNADVFT
FGNNQQQHQP QSTSPFAQQT PGSTGPSAIS PGTVSQDWDA LFSVLDTSKA SQSANETNKP
ASSSEDQPPS DSAALSSFPQ PPGKKANPPG WALNSPTGED DMMLQRLTGM GYPRDESLAA
LEKFNYSLDK AADFLASKS
//
