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PAN1_ASPFU
ID   PAN1_ASPFU              Reviewed;        1467 AA.
AC   Q4WG58;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN   Name=pan1; ORFNames=AFUA_7G03870;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000009; EAL87083.1; -; Genomic_DNA.
DR   RefSeq; XP_749121.1; XM_744028.1.
DR   AlphaFoldDB; Q4WG58; -.
DR   SMR; Q4WG58; -.
DR   STRING; 746128.CADAFUBP00008690; -.
DR   EnsemblFungi; EAL87083; EAL87083; AFUA_7G03870.
DR   GeneID; 3506426; -.
DR   KEGG; afm:AFUA_7G03870; -.
DR   VEuPathDB; FungiDB:Afu7g03870; -.
DR   eggNOG; KOG0998; Eukaryota.
DR   HOGENOM; CLU_001963_1_0_1; -.
DR   InParanoid; Q4WG58; -.
DR   OMA; PQRTGMQ; -.
DR   OrthoDB; 597979at2759; -.
DR   Proteomes; UP000002530; Chromosome 7.
DR   GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000147; P:actin cortical patch assembly; IBA:GO_Central.
DR   GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
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; SM00027; EH; 2.
DR   SMART; SM00246; WH2; 1.
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..1467
FT                   /note="Actin cytoskeleton-regulatory complex protein pan1"
FT                   /id="PRO_0000349466"
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;  159383 MW;  9FB43C08C408D2AA 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 TLADPSNRGR 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 PPGPLPPPAP PAASGPPTPA GAPDRSALLA
     SIQKGKGLRK VQTNDRSTSS IAGRVLD
 
 
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