PAN1_NEOFI
ID PAN1_NEOFI Reviewed; 1470 AA.
AC A1DC51;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=NFIA_024830;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027695; EAW19411.1; -; Genomic_DNA.
DR RefSeq; XP_001261308.1; XM_001261307.1.
DR AlphaFoldDB; A1DC51; -.
DR SMR; A1DC51; -.
DR STRING; 36630.CADNFIAP00002483; -.
DR EnsemblFungi; EAW19411; EAW19411; NFIA_024830.
DR GeneID; 4588024; -.
DR KEGG; nfi:NFIA_024830; -.
DR VEuPathDB; FungiDB:NFIA_024830; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001963_1_0_1; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000006702; 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; 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; 1.
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..1470
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000349480"
FT DOMAIN 169..257
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 201..236
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 458..547
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 491..526
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1437..1454
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 633..758
FT /evidence="ECO:0000255"
FT COILED 963..1159
FT /evidence="ECO:0000255"
FT COMPBIAS 28..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1470 AA; 159284 MW; 7E21E2116D9F690A CRC64;
MYSSSNSFLG GVNNARPGQP PFMQQPPYSQ FPQGQQQIPQ QTGFQPQPAG YGPQSASHLQ
PQPTGFPTGQ LQPQFTGFPG AAPQQQQQQL GGYQAPAQQP QFTGYPPQSQ PPSLQVPSTT
GLPTRLAPRT SSEIANSFSD GAGVAPPPPP KSSGSKIPNI RLSFITAQDQ AKFEQLFKSA
VGDSQTMDGE KAKELLLRSR LPGSELSKIW VLSDTTKSGQ LFFPEFALAM YLCNLRITGR
ELPATLPDKI KNEVSSMVDI ISFGVPDTEP QASARTNVPS FDAPLLENKS APPAPQHPKP
QQPSNAQFLS QLAAQPTGFG PQATGLQPNQ PSLLGANAAL APQATGFPGQ SQQQYLQPQP
TGLMTNPQAT GYNGPRPPLP PMPTGFGSNL SSMQTGGLVA QPTGIPGQWG FVNAPSSGLP
NIEALKQQLM PQPGREGGFT TAGLSGNASI PWAITKEEKK IYDDLFRAWD GFHKGFIGGD
TAIEIMGQSG LDRKDLERIW TLADPNNRGR LNMDEFAVAM HLIYRKLNGY PVPNRLPPEL
IPPSTRNLND SIGAVKSLLS QDAENRKASG AFLQPQKTGV SYLKEHSFRG GARSPGFGRK
DATLFKNNDE AAAGYRSSAR RRMGNDARPS SPAASQASEE ELSVEQLKKK IRETQIMLDA
VDFNDENRAE EDEVLDRRDR LEAESLMDRT RRVQDDIDTH PNAAFRNLDN GAERRALRRQ
LQAFEDQVPQ VASEVRRIER EIADAKLELF RLKDAKAHPN SAANIVGTGP GGTVTEADRI
KARARARMQA RAAELAGRPV PASVDDDGAA ARRLEAESTS IRADREKNEA MTRDVEESVR
EFTRSLEDSL KEEGETSTRE HERRRWEDAL GVEDVIRDFI YDLQRGSRTA HVRKEEESRA
SEQRLRHEEP SAGVSRLSPA PSAGSAGSLP GSTHEDRVAA ARERAQRRIA ERMAAAGLKP
HTDTSETLLQ RQEREKRERE ERLRQAEEED AKREQERQRR LAEEQRSTSN APAKPVGKKP
PPAPPSRRGR TDSAGQAEVK KAAEETVTAE QAAREQAIRE EQQAQEEETN RLEMEAQQRE
EELLKEKEAQ EARLRALEEQ VRQGKIRKQE EKRRKEEAER LAKEKEAALA AQRAEIERAK
ERERQLQLEL EGLDEESSSD DEGPANITPE DSTPTQSQLL PTVTPAAPVS APESEQAGSP
EDTSSQAPPV GFSSETESKN PYFKITHQAA DTQVVSPPPA PQPNVTSPRA DVHSTNPFHR
LAQQESSKPV FTGSAPLERK SRARPEADDD WSAAGSEFDS SDDDDDERPG GGSAKQLASI
LFGTMAPPRP LSAMDDKSPS KSSTPVQDSP VTSLPVPEPN GSLSAPAAPP PPPPPPPPAA
VPSYDSSVAP PPPPAPPMAP PMAPPAPPPG PPPPPGPPPP PAPPAAGGPP TPAGAPDRSA
LLASIQMGKG LRKVQTNDRS TSSSAGRVLD
