ID A5ABT0_ASPNC Unreviewed; 1015 AA.
AC A5ABT0;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Contig An11c0340, genomic contig {ECO:0000313|EMBL:CAK97115.1};
GN ORFNames=An11g10320 {ECO:0000313|EMBL:CAK97115.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK97115.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK97115.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 SLA2 family.
CC {ECO:0000256|ARBA:ARBA00010135}.
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DR EMBL; AM270251; CAK97115.1; -; Genomic_DNA.
DR AlphaFoldDB; A5ABT0; -.
DR EnsemblFungi; CAK97115; CAK97115; An11g10320.
DR HOGENOM; CLU_004601_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
DR GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
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:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
DR GO; GO:0007015; P:actin filament organization; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
DR CDD; cd17007; ANTH_N_Sla2p; 1.
DR Gene3D; 1.25.40.90; -; 1.
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; 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:SF15; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR Pfam; PF07651; ANTH; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 1..129
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 782..1015
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 255..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..565
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 974..1010
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 260..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 115205 MW; 246F74F4EC409041 CRC64;
MSRTETDLAI NIRKATSIEE TAPKRKHVRS CIVYTWDHKS SSAFWAGMKV QPVLADEVQT
FKALITIHKV LQEGHPIVVR EAQQHVNWVD SLMRGVGGDG IRGYGPLIRE YVFYLESKLA
FHRNHPEFNG LFEYEEYISL KTTNDPNEGY EAITDLMTLQ DQIDAFQKLI FSHFQSGTNN
ECRISALVPL VQESYGIYKF ITSMLRAMHT TTGDTEALEP LRGRYDAQHY RLVRFYYECS
NLRYLTSLIT VPKLPQDPPN LLSEDDERPA LPKRPVKEPE PQPSPPPKMT AAEPEPISDF
WTTEAKRQQE EYEAEQRRLQ QQWEDQQRQQ LLAQQQAQRD FEEQQRLQAE QQRLAQEQLL
RDQYQTQTQG RLAELEQENL NARAQYERDQ LMLQQYDRRV KDLEEQMNHL NSNLNLQNAS
KDEQIRALQE QVNTWRSKYE ALAKLYSQLR QEHLDLLQTT KSLKLKAASA QEAIERREKL
ERELKTKNLE LADMIRERDR ALHDRDRLTG NNKEELEKVK RELRFALERA ENAERSKGTE
ISTLLSKYNR EMADLEEALR VISNKTSERA GDHDLALREK DEEIEVYKWR KQSQGDVDNA
LDSQIDTVLH GTVSKINDII DSVLQTGVQR VDDALYELDS SMQAGNQNAS PPYVLSQIEK
ASASATEFST AFNNFIADGP NSTHAEIIRT VSIFSGSVAD VLSNTKGLTR FANDDKSADQ
LVNAARKSAQ ATVRFFRGLQ SFRLEGLEAL QKTDVVINNN LEVQRDLQTL SKLVDAFAPK
SAKIATNGDL GDLVDQELTR AADAIDAAAQ RLAKLKNKPR DGFSTYELRI NDVILAAAIA
VTNAIAELIK AATASQQEIV REGREQPLGL RGLISAAKAV ASSTNTLIET ADGVISGRNS
PEQLIVASND VAASTAQLVA ASRVKATFMS KSQDRLETAS KAVGAACRAL VRQVQDIIKE
KNHDDSEAVD YTKLSSHEFK VREMEQQVEI LQLENSLSRA RQRLGEMRKI SYQED
//
