PAN1_ASPCL
ID PAN1_ASPCL Reviewed; 1485 AA.
AC A1CD74;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=ACLA_005570;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027051; EAW11801.1; -; Genomic_DNA.
DR RefSeq; XP_001273227.1; XM_001273226.1.
DR AlphaFoldDB; A1CD74; -.
DR SMR; A1CD74; -.
DR STRING; 5057.CADACLAP00000422; -.
DR PRIDE; A1CD74; -.
DR EnsemblFungi; EAW11801; EAW11801; ACLA_005570.
DR GeneID; 4705390; -.
DR KEGG; act:ACLA_005570; -.
DR VEuPathDB; FungiDB:ACLA_005570; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001963_1_0_1; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000006701; 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; 2.
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; PF12763; EF-hand_4; 2.
DR Pfam; PF02205; WH2; 1.
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..1485
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000349464"
FT DOMAIN 174..262
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 206..241
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 465..554
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 498..533
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1452..1469
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 645..765
FT /evidence="ECO:0000255"
FT COILED 1054..1172
FT /evidence="ECO:0000255"
FT COMPBIAS 1..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 160694 MW; 1AFE35EC82F9A88B CRC64;
MYSSSNSFMG GANSARPGQP PFMQQPSYSQ YPPGQPQSQQ QTGFPSQPTG YGLQPPQLVG
SQLQPQQTGF PGQLQPQFTG FPGAAPQQQQ QQQQLGGFQQ SVQQPQFTGY PPQNQLLSLQ
APSTTGLPTR PAPRTSSEVA SSFNDGAGVA PPPPPKSAGS KIPSIRLSFI TAQDQAKFEQ
LFKSAVGDSQ TIDGGKAKEL LLRSRLPGSE LSKIWILSDT TKSGQLFFPE FALAMYLCNL
RITGRELPPS LPEKIKNEVS SMVDIISFGV PDTQPEPSRS NVPSFDAPLL ENKSAPPAPQ
QPQPQQPTNA HLLSQLAAQP TGFLPQQTGF QPNQSSFLGP SAGLAPQATG FPGQSQQQYL
QTQPTGLMTN PQATGYSGPR PPLPPMPTGF GSNLSPAQTG GASALVAQPT GIPGQWGFVN
APSSGLPNIE ALKQQLMPQP GREGGFTTAG LSGNASIPWA ITKEEKKIYD DLFRAWDGFH
KGFIGGDTAI EIMGQSGLNR QDLERIWTLA DPHNRGRLNM DEFAVAMHLI YRKLNGYPVP
SRLPPELIPP STRNLNDSIG TVKSLLSQDA ESRKASGAFL QPQKTGVSYL KEHSFRGGAR
SPGVGRKDAT LFKNNDEAAA GYRSSARRRV GNNARAASPA TSHTSEEELS VEQLKKKIRE
TQIMLDAVDF QDENRAEEDE ALDRRDRREA ESLMDRVRRI QDDIDTHPNA TFRNLDNGAE
KRSLRRQLQA YEDQVPQVAS EVRRIERELA EAKLELFRLK DAKAHPNSAS NIVGTGPGGA
VTEADRIKAR ARARMQARAA ELAGRPVPAS ADDDGAAARR LESESTVIRA DRERNEAMTR
DVEESVREFT RSLEDSFKEG GETSTREHER RRWEDALGVE DVIRDFIYDL KRGSRTAHVR
KEEETRTLPT HDHRVRHEDP SIASRPSPAP SAGSVGSAPG ATHEDRVAAA RERAQRRIAE
RMAAAGLKPH TDSTETLVQR QEREKREREE RLRRAEEEDA KREQERQRRL AEEQRGPAKP
AATKPVGKKP PPAPPSRRGR TDSAGQADAR PAVEETAATE QAAREQAIRE EQQAQEEETK
RLEMEAQQRE QELLKEKEAQ EARLRALEEQ VRQGKVRKQE EKRRKEEAER SAKEQEAKLA
AQRAELEMAR ERERQLQLEL EGLEDESSSD EEGPVNITPQ DSTPTQSQVL PAPSPAAAAP
EPELEPPVSP EITSSASSHA APSSFSPETE SKNPYFRITS QAAENQVSSP PPVPQTTITS
PKTDVQSTNP FHRLAQQEAA KPAFTAPGPL ERKSRVRPEA DDDWSAAGSD FDSSDDEDDE
RPGGGSAKQL ASILFGTMAP PRPLSAMDDK SPSKSSTPVQ DNTVASPVVP EASASLSAPA
APPPPPPPPP PPASAPMVVP SYDPSTAPPP PPPAPPIAPP APPPGPPPPP GPPPPPAPPG
AAAPAAPAGA ADRSALLASI QMGKGLRKVQ TNDRSSSSSA GRVLG
