ID PAN1_PYRO7 Reviewed; 1462 AA.
AC A4R8N4; G4N7H0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; ORFNames=MGG_12839;
OS Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Magnaporthe 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; 242507.A4R8N4; -.
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; 2734911at2759; -.
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 Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR PANTHER; PTHR11216:SF177; ACTIN CYTOSKELETON-REGULATORY COMPLEX PROTEIN PAN1; 1.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; EF-hand; 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
//
