PAN1_ASPNC
ID PAN1_ASPNC Reviewed; 1434 AA.
AC A2R180;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=An13g00290;
OS Aspergillus niger (strain 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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.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 -!- 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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}. Note=Cytoplasmic and cortical actin patches.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAN1 family. {ECO:0000305}.
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DR EMBL; AM270295; CAK46430.1; -; Genomic_DNA.
DR AlphaFoldDB; A2R180; -.
DR SMR; A2R180; -.
DR PaxDb; A2R180; -.
DR PRIDE; A2R180; -.
DR EnsemblFungi; CAK46430; CAK46430; An13g00290.
DR VEuPathDB; FungiDB:An13g00290; -.
DR HOGENOM; CLU_001963_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 2L.
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; 2.
DR InterPro; IPR013182; DUF1720.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF08226; DUF1720; 2.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 2.
DR PROSITE; PS51082; WH2; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endocytosis; Endosome; Membrane; Reference proteome; Repeat.
FT CHAIN 1..1434
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000349467"
FT DOMAIN 171..259
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 203..238
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 460..549
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 493..528
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1401..1418
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 607..815
FT /evidence="ECO:0000255"
FT COILED 941..1137
FT /evidence="ECO:0000255"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1286
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 154851 MW; 4E3563D676080D18 CRC64;
MYSSSNTFLG GANSARPGQP LMQQSPYSQQ FASGQQQQPP QQGGFAPQPT GYGPQMSSFG
ASQLQPQATG FPAGQLQPQF TGFPGAVPQS QQTGFQPPVQ QAQITGYPAQ SQPPQFQVPA
STGLPVRQAP RTSSEIADSF QDVAGMAPPP PPKASASKIP NIRLSFITAQ DQAKFEQLFK
SAVGDNQTMS GDKAKELLLR SKLPGNDLSK IWVLSDSTKS GQLFFPEFAL AMYLCNLRIT
GRELPSALPE KIRNEVSSMV DIISFQVPDT QPEPAVRTNV PNFDAPLLEN KSAPPAPQQP
QPQQPSNAQL LTQLTAQPTG FPQPTGFQQS QSPFPGQNSA LAPQATGFPG QPQQLQPQPT
GFMTNPQPTG YNGPRPPMPP MPTGFGSNLS PAQTGGVSAL AAQPTGIPGQ WGFVNAPATG
LPNIEALKQQ LMPQPGREGG FSAVGLSGNA HIPWAITKEE KKIYDDLFRA WDGFRKGFIG
GDTAIEIMGQ SGLDRSDLER IWTLADPNNR GRLNMDEFAV AMHLIYRKLN GYPVPNRLPP
ELVPPSTRNL NDSIGTIKSM LSQDAEMSPG GGRKDATLFK NNDEAAAGYR SSARRRVGNN
GRTPSPAASQ ASEEELSVDQ LKKKIREAQI MLDAVDFQDE NQAEEDDALD RRDRREAESL
MDRIRRVQDD IDTHPDASFR NLDTGAERRS LRRQLQAYED QVPQVASEVR RVEREIAEVR
LELFRLKDAK EHPNSASSIV GTGPGGTVTE ADRIKARARA RMQARAAELA GRPVPASQDD
DGAATRRLEA ENATVKAERE RNETMTRDVE ESVREFARSL EDSLKDGGES STREHERRRW
EDALGVEDVV RDFIYDLKRS SRTAHVRKEE QQRAADTQSQ RSRYNESPLG GAAGSQHSPT
PTGSVVSAGS THEDRVAAAR ERAQKRIAER MAAAGLKPHS DAGETLLQRQ EREKKEREER
LRRAEEEDAK REQERQRRLA EEQGGPTAQS AKPASKKPPP APPSRKGRTD SAGQAEAKKA
REEAAKVEQS TREQAIREEQ QAQEEETARL EAAAREREAE FLKEKEAQEA RLAALQEQVR
QGKIKKQEEK RRKEEAARAA KEQEARLATQ RAELEMAKER ERQLQLELEG LDESSSDEEG
PINITPQDST PTQSQVLPAV DTAVPPPAPA PAPELDVVTS PAESASSHAA PTSISPEAES
KNPYFKRISQ SDSQVPPPPP APQPAAPKAE SQSTNPFHRL AQQQESSKPA FTAPGPLERK
SRVRPEVDDD WSAAGSDFDD SSDDDDERPG GGSAKQLASI LFGTMAPPRP LSAMDDKTPS
KSSTPVQDSP ATPTPPTEAA ESPAAVPPPP PPPPAPAPAV PSPSAAAPPP PPPAPSMAPP
VPPPGVPPPP APPAAPTGGA GRGALLASIQ AGTGLRKVQT NDRSTSSSAG RVLD
