ID   PAN1_PODAN              Reviewed;        1441 AA.
AC   B2AWS3; A0A090CTR5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 2.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN   Name=PAN1; OrderedLocusNames=Pa_7_8140; ORFNames=PODANS_7_8140;
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
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; CU633900; CAP68847.1; -; Genomic_DNA.
DR   EMBL; FO904942; CDP32330.1; -; Genomic_DNA.
DR   RefSeq; XP_001908174.1; XM_001908139.1.
DR   AlphaFoldDB; B2AWS3; -.
DR   SMR; B2AWS3; -.
DR   STRING; 5145.XP_001908174.1; -.
DR   PRIDE; B2AWS3; -.
DR   EnsemblFungi; CAP68847; CAP68847; PODANS_7_8140.
DR   GeneID; 6192616; -.
DR   KEGG; pan:PODANSg5209; -.
DR   eggNOG; KOG0998; Eukaryota.
DR   HOGENOM; CLU_001963_1_0_1; -.
DR   OrthoDB; 597979at2759; -.
DR   Proteomes; UP000001197; Chromosome 7.
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..1441
FT                   /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT                   /id="PRO_0000349484"
FT   DOMAIN          188..277
FT                   /note="EH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          221..256
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          440..529
FT                   /note="EH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          473..508
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..1441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          618..735
FT                   /evidence="ECO:0000255"
FT   COILED          791..820
FT                   /evidence="ECO:0000255"
FT   COILED          956..997
FT                   /evidence="ECO:0000255"
FT   COILED          1028..1143
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..146
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..890
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..916
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1151..1170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1177..1191
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1239
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1321..1402
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        507
FT                   /note="R -> C (in Ref. 1; CAP68847)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1441 AA;  155180 MW;  063A65619B863C1B CRC64;
     MYSNPNSFLG GNSQRPGQPQ YGNQFGAGAG QPQLQQPGPF APQPTGFGQQ PALQQQYTGY
     PGLQAPQPTG QLQPQFTGFG QAPQQNVGAA APPMPAMPQQ FQQQFQQQQQ QFQQQPQQTS
     SPFGAAPSQQ PPASALAPPA PPMKPQPTGF HEMAASFQTA GGSKSTASAP RKTNKIPNIR
     LSFITAQDQA KFETLFKSAV GDGQTTMTGE KARDLLLRSR LDGDSLSHIW TLADTTRSGQ
     LHFPEFALAM YLCNLKLTGK TLPEHLPENI KNEVSSMVDI INFSVAEEAA NASDSGIRQN
     TATPPVIQHP QPQPSNSQLL QAQMTGFPSQ QTGFLGAQPT GMPQATGYTG PRPPMPPMPT
     GFGSSLTPNA GPGGMVAPLN AQPTGIPGQW GLVNTPATGL PLIDALQARM MPQQGREQQT
     YTTAGLQGNA VIPWAITKDE KTRYDSLFRA WDGLHKGYIS GDQAIEILGQ SGLEKPDLER
     VWTLADNGNK GRLDMDEFAV AMHLIYRKLN GYPVPNQLPP ELVPPSTRNF NQSIGMVKNM
     LHQESEYRKN SGAALLPQKT GVSYLKGHSF KGAGAGFGNR KDATVFKNND EEVGYRSSAR
     RRVGNNSPRP ESPASVNSSE ELSIEQLRKK IKEKQVLLDA MDFADEKHAE EDDILDRRDR
     READELYRRI RRIQEDIDNH PDASLISADS DAERRALKRQ LQNLTDKIPD LASQVRKTEK
     AIADARLELF RLRDAKAHPS SAAAIIGTGP GGTVTESDRL KARAKAMMQQ RTAALTGKKI
     EVSNDDLDAP KRLEEESIKI RTEKENNERM VRDVEDSVRE FAKGIEDNMK EGAQDSTTEH
     EKRRWEDGLG VEDEVRDFIY DLQRSSRAAR IRSQDRQGGR QPTQEPTRAE APPSARSVSP
     AVSRTSTPSA PVAGGGSYSS YKTPEERAAF IKQQAEQRMA ERLAALGIKA PTKPGETAAQ
     RMERERAERA AKLRQAEEED ARREAERQAR IAEETGAPAP AAQAAVPKPE GKKPPPPPSR
     KTPKVDDRRA EEEAAARKAE EGRLERERGE QERQTRELEE RAKDQEDELA KERAEADARL
     KALEEQVRQG KLKKEEEKRK KKAAMAEAKE QEAKLAQRRA EIEAARKREE ELRKQLEALD
     VEDSSSDDDE GPEQITPQAS TPTLGGSQVG GSQELEPAPP TPVPAPVQSP PQIVTSSPAE
     TESRNPYFRM RAQAAETTPA PPAPPAPVAP PPPPQPDVST NPFHRMTQAA AAPAPSGPVS
     RKRPEDDGWG SDKEDDDEDS DDDRPGQGAA HLASILFGTM APPRPLSATG DKSAAASPPV
     TSPVASPPPA IPSPTAAGAP PAPPPPPPMP GMGAPPPPPP PPPMPGSGAP AAPPPPPPPA
     PGGAPPPPPP PPPPPGGAPA PAAPAGGRPA AFLGEIQAGR ALRKTQTKDK SGAAVAGRVL
     D