ID PAN1_ASPFC Reviewed; 1467 AA.
AC B0YC95;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=AFUB_089400;
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
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; DS499601; EDP48226.1; -; Genomic_DNA.
DR AlphaFoldDB; B0YC95; -.
DR SMR; B0YC95; -.
DR EnsemblFungi; EDP48226; EDP48226; AFUB_089400.
DR VEuPathDB; FungiDB:AFUB_089400; -.
DR HOGENOM; CLU_001963_1_0_1; -.
DR PhylomeDB; B0YC95; -.
DR Proteomes; UP000001699; 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 CDD; cd22070; WH2_Pan1-like; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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 PANTHER; PTHR11216:SF177; ACTIN CYTOSKELETON-REGULATORY COMPLEX PROTEIN PAN1; 1.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
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 SMART; SM00246; WH2; 1.
DR SUPFAM; SSF47473; EF-hand; 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; Repeat.
FT CHAIN 1..1467
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000349465"
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 1434..1451
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 266..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 634..758
FT /evidence="ECO:0000255"
FT COILED 965..1162
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 301..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1467 AA; 159394 MW; D043F610D5A01869 CRC64;
MYSSSNSFLG GVNNARPGQP PFMQQPPYSQ LPQGQQQIPQ QTGFQPQPTG YGSQSASHLQ
PQPTGFPTGQ LQPQFTGFPG AAPPQQQQQF GGYQAPAQQP QLTGYPPQSQ PPSLQVPSTT
GLPTRLAPRT SSEIANSFSD GAGVAPPPPP KSSGSKIPNI RLSFITAQDQ AKFEQLFKSA
VGDSQTMDGE KAKELLLRSR LPGSELSKIW VLSDTTKSGQ LFFPEFALAM YLCNLRITGR
ELPSTLPDKI KNEVSGMVDI ISFGVPDTEP QGAARTNVPS FDAPLLENKS APPAPQHPKP
QQPSNAQFLS QLAAQPTGFG PQATGLQPNQ PSLLGANATL APQTTGFPGQ SQQQYLHSQP
TGLMTNPQAT GYNGPRPPLP PMPTGFGSNL SSMQTGGLAA QPTGIPGQWG FVNAPSSGLP
NIEALKQQLM PQPGREGGFT TAGLSGNASI PWAITKEEKK IYDDLFRAWD GLHKGFIGGD
TAIEIMGQSG LDRKDLERIW TLADPNNRGR LNMDEFAVAM HLIYRKLNGY PVPNRLPPEL
IPPSTRNLND SIGAVKSLLS QDAESRKASG AFLQPQKTGV SYLKEHSFRG GARSPGFGRK
DATLFKNNDE AAAGYRSSAR RRVGNDARPS SPPTSQASEE ELSVEQLKKK IRETQIMLDA
VDFKDENRAE EDEVLDRRDR LEAESLMDRT RRVQDDIDTH PNAVFRKLDN GAERRSLRRQ
LQAFEDQVPQ IASEVRRIER EIADAKLELF RLKDAKAHPN SAANIVGTGP GGTVTEADRI
KARARARMQA RAAELAGRPV PASVDDDGAA VRRLEAESAS IRADREKNEA MTRDVEESVR
EFTRSLEDSL KEEGETSTRE HERRRWEDAL GVEDVIRDFI YDLQRGSRTA HIRKEEESRA
SAQEQRLRHE EPSPGVSRLS PAPSAGSAGS LPGSTHEDRV AAARERAQRR IAERMAAAGL
KPHTDTSETL LQRQEREKRE REERLRRAEE EDAKREQERQ RRLAEEQRST SDTPAKPVGK
KPPPAPPSRR GRTDSAGQAE VKKAAEETIT AEQAAREQAI REEQQAQEEE TNRLEMEAQK
REEELLKEKE AQEARLRALE EQVRQGKIRK QEEKRRKEEA ERLAKEKEAA LAAQRAEIER
AKERERQLQL ELERLDEESS SDDEGPVNIT PEDSTPTQSQ LLPTVTPAAP VSAPESEQAG
SPEDTSSQAP PVDFKLETES KNPYFKITHQ ATDTQVVSSP PVPQPSFTSP KADVHSTNPF
HRLAKQETSK PAFTGSAPLE RKSRARPEAD DDWSAAGSEF DSSDDDDDER PGGGSAKQLA
SILFGTMAPP RPLSAMDDKS PSKSSTPVQD SPVASLPVPE SNGSLSAPAA PPPPPPPPPA
AVPSYDPSVA PPPPPAPPMA PPAPPPGPPP PPGPPPPPAP PAASGPPTPA GAPDRSALLA
SIQKGKGLRK VQTNDRSTSS IAGRVLD
//
