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PAN1_MAGO7
ID   PAN1_MAGO7              Reviewed;        1462 AA.
AC   A4R8N4; G4N7H0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN   Name=PAN1; ORFNames=MGG_12839;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(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; CM001234; EHA50827.1; -; Genomic_DNA.
DR   RefSeq; XP_003717146.1; XM_003717098.1.
DR   AlphaFoldDB; A4R8N4; -.
DR   SMR; A4R8N4; -.
DR   STRING; 318829.MGG_12839T0; -.
DR   GeneID; 5050207; -.
DR   KEGG; mgr:MGG_12839; -.
DR   VEuPathDB; FungiDB:MGG_12839; -.
DR   eggNOG; KOG0998; Eukaryota.
DR   HOGENOM; CLU_001963_1_0_1; -.
DR   InParanoid; A4R8N4; -.
DR   OMA; PQRTGMQ; -.
DR   OrthoDB; 597979at2759; -.
DR   Proteomes; UP000009058; Chromosome 4.
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   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; Reference proteome; Repeat.
FT   CHAIN           1..1462
FT                   /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT                   /id="PRO_0000349479"
FT   DOMAIN          197..286
FT                   /note="EH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          230..265
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          463..552
FT                   /note="EH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          496..531
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          1429..1446
FT                   /note="WH2"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          884..1462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          643..745
FT                   /evidence="ECO:0000255"
FT   COILED          815..847
FT                   /evidence="ECO:0000255"
FT   COILED          986..1023
FT                   /evidence="ECO:0000255"
FT   COILED          1050..1165
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        102..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..908
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..947
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        985..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1047
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1168..1186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1207..1232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1234..1248
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1333..1418
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1462 AA;  157423 MW;  17D9AC8249D7EAF3 CRC64;
     MYSNSNSFLG GGNSMRPGPQ QYGSSFNAGS GQQQQQQQQQ QQPPQQSPFA AQQTGFAQVP
     LQHQYTGYPA MQQPMQTGQI QPQYTGFPGH QQGFQGSAPP MPAIPQQFQH QFQHQQQQQQ
     PPPQPQQSAS FLSSQPTTSS SLQTPSAPAA AMKPQPTGFS QMAASFQTGG QSAPKPAQAS
     KGTKIPNIRL SFITAQDQAK FETLFKSAVG DGQTTMSGEK ARDILMRSRL DGEYLSQIWT
     LADTTRSGQL HFPEFALAMY LCNLKMNGKS LPSSLPENIK NEVSSMVDII NFSIAEDSAN
     ASSATNAPDF TVRQNTATPP TIQHPQPQPS NSQLLQAQMT GFPGAQQGFM AQANGGGLQP
     QQTGYPGMQN PQPTGYTGPR PPMPPMPTGL GAGGMGAMAA PLNAQPTGRP GQWGLVNTPS
     TGLPNIDALH ARMMPQQGRE QGSFTTAGLQ GNAVIPWAIT KDEKTRYDAL FKAWDGMNKG
     YIAGSQAIEI FGQSGLEKPD LERVWTLADH GNKGRLNLDE FAVAMHLIYR KLNGYPLPNS
     LPPELVPPST RNFNEAIGTM KNMLNQESDF RKNSGAALLP QKTGVSYLKT HSFRGQGGVP
     TGSRKDATVF KNDDDAVGYK SSARRRIGNG SPRPDSPSSV ASNEDLSIEQ LRKKIKEKQV
     LLDAMDFKDE KSFEEDDVLD RRDRKEAEDL YRRIRRIQED IDSHPDAPLP SGDSDAERRA
     LKRQLQNLKD SIPDLASQVR KTEKAIFEAR LELFRLKDAK AHPSSAPAIV GTGPGGAVTE
     SDRLKARAKA MMQQRTAALT GKKIDISSED TDAPKRLEEE SIQARTEKEN NERMVRDVEE
     SVQEFARSIE DSLQAGGQTA DNEHERRRWE DALGVEDEIR DFIFDLQRSS RSKRVRAQDR
     RADRSGPTSD PPRSEPASAP RHESPSAPAA RTGTPTSASS AGGSYSSYKT PEERAAFIKQ
     QAEQRMAERL AALGIKAPVK GGETPAQRME RERSERAAKL RQAEEEDARR EAERQARLAE
     EQGPPQPAAS APKTEAKPPP PPPSRKAAPD RETAAKKAEE ERLAQEQEEQ QRQMREMEAK
     AKAEEDALAR ENSAAEARLK ALEEQVRQGK LKKEEEKRRK KAALAEAKEK EAKLAARRQE
     IEAAKRREEE LQRQLEAMNE EGSSSDDDEP AQITPQASTP TVGSQELERK PSPPPQVAEP
     KTESRNPYFR MLSQSSEGPT SVSPQASVSP VPQQEAPAPA PPPAAPEAST NPFHRMTAPQ
     TAAPAPISRK RADTDDGWGS DKDDDEDDSD DDRPGGTSAA QLASILFGTM GPPRPLSAAD
     NKSVSSPTAV ASPPTVASPP PAPPGPPPVP AAAAPTVPST PSPAPEITSA PPAPPPPPPP
     MPSMGAPGAP PPPPPMPPTG APSAPPPPPP PPPAASSSSA PAATPAGGRP AGFLGEIQAG
     RALRKTTTKD KSAAAVAGRV LD
 
 
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