PAN1_BOTFB
ID PAN1_BOTFB Reviewed; 1444 AA.
AC A6S9N4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=BC1G_09414;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476901; EDN30169.1; -; Genomic_DNA.
DR RefSeq; XP_001552073.1; XM_001552023.1.
DR AlphaFoldDB; A6S9N4; -.
DR SMR; A6S9N4; -.
DR GeneID; 5432593; -.
DR KEGG; bfu:BCIN_05g00930; -.
DR VEuPathDB; FungiDB:Bcin05g00930; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
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 Pfam; PF08226; DUF1720; 2.
DR Pfam; PF12763; EF-hand_4; 2.
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.
PE 3: Inferred from homology;
KW Actin-binding; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endocytosis; Endosome; Membrane; Repeat.
FT CHAIN 1..1444
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000349470"
FT DOMAIN 184..272
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 216..251
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 467..556
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 500..535
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1411..1428
FT /note="WH2"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 685..763
FT /evidence="ECO:0000255"
FT COILED 980..1157
FT /evidence="ECO:0000255"
FT COMPBIAS 1..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1444 AA; 155899 MW; DD35B4B4A6B6FE0F CRC64;
MFSGSNSYLG GNTGRQPPQQ PQQQYGGFQP NQGFQPQQTG FQPQQTGFQP QPTGYGNAAP
LQPNFTGYPL QPQPTGYSQP SQAGFPGGQQ QQQQFNNAPQ QQNFQTGAPP IPQIPQQFQQ
PQQTQQAQPP PAPPVQQPQA TGFAAMADSF KPAAAEPSKP RGRRASKGGA KIPSIRLSFI
TAQDQAKFET LFKSAVGDGQ TLSGEKSRDL LLRSKLDGNS LSQIWTLADT TRSGQLHFPE
FALAMYLCNL KLVGKQLPSV LPDVIKNEVS SMVDIINFAI DDDAPAATNA PSFDGRQNTA
TPPTIQQPQP MASNSALLTA QMTGYPGQQN NFSGGFQPQQ TGFQGQMQTG FSGQQGGLQP
QPTGYNQMSN PQATGYNGPR PPMPPMPSNF SSHLSPAQTG MQGGMIAPLN SQPTGVDGQW
GLVNAPAPNI DLLHSRMMPQ QGREQGNFTT AGITGNAEIP WGITKDEKTR YDSVFKAWDG
FGKGYISGDV AIEVFGQSGL PKPDLERVWT LADHGNKGKL NMDEFAVAMH LIYRKLNGYP
LPAQLPPALI PPSTRNFNDS IGAVKSLLHQ ESNFRKNSGA TLLPQKTGVS YLKNHSFRGD
ATPGRTGRKD ATVYKNNDDD VGYKSSARRR LGASSPRPSS PGSTTSNDDL SLDQLRKKIA
ERQVILDAID FKAENAADED DALDRKDRRE AEDLYHRIRR IQEDIDAHPD ASLRNVDSGA
ERRALKRQLQ TLTDKLPDIA SRVRRTERSI ADAKLELFRL KDAKAHPGSA SSIVGTGPGG
AITESDRLKA RAKAMMQQRS AALTGKKIEA SNDDLDAPKR LEEENLKIRT EKENNERMVQ
DVEESVRDFS RGLEDSLKDG GESSSSEHEK RRWEDGLGVE DEVKDFIFDL QRSSRSARVR
TDDRSRETPR TEASHASPAP AARSETPSSQ PSSTPTPAGG SYSQYKTPED RAAYIKQQAE
KRMAERLAAL GIKAPSKSGE TTQQRLEREK NERAAKLRQA EEEDAKREAE RQARIAEEQG
APPPAPEQPK ETAKKPPPPP SRKAARSDAS ERKAEEERII NEQKAQIIAT NELEDDAQRQ
EAELAKEREA AQARVKALED QMKAGKLKKE EEKKKRKALQ AETKQQEARL AAQRAEIEAA
QARERELQRQ LEAIDDSDSS DDDEGPEQVT PQASTPTQGS QELERKEPSP PPPPPSIPVV
VSPVPAIATT TSLPSPTPQV TSPVVSPPVD TETRNPFLKK MAQSGDASTA STASNNPFHR
LPAQELSTPA PIQVQPTGNR PSRVRPEEDD WDVVGSDKED DSSDDEGPGA GGARHLASIL
FGTMAPPRPL SSMGNEATSA PESPAVASPP AATPPPPPVP NFNAPPPPPM PSAGAPGGPP
PPPPPPPGMG APPPPPMPPM GGAPAPPAGV RPAGLLGEIQ MGRSLKKTQT KDKSSAAVAG
RVLD
