PAN1_SCLS1
ID PAN1_SCLS1 Reviewed; 1373 AA.
AC A7EKZ0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=SS1G_05987;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
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; CH476627; EDO03506.1; -; Genomic_DNA.
DR RefSeq; XP_001593065.1; XM_001593015.1.
DR AlphaFoldDB; A7EKZ0; -.
DR SMR; A7EKZ0; -.
DR STRING; 665079.A7EKZ0; -.
DR EnsemblFungi; EDO03506; EDO03506; SS1G_05987.
DR GeneID; 5489540; -.
DR KEGG; ssl:SS1G_05987; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001963_1_0_1; -.
DR InParanoid; A7EKZ0; -.
DR OMA; PQRTGMQ; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
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 Pfam; PF08226; DUF1720; 2.
DR Pfam; PF12763; EF-hand_4; 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..1373
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000349485"
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 471..560
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 504..539
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1340..1357
FT /note="WH2"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 757..789
FT /evidence="ECO:0000255"
FT COILED 917..959
FT /evidence="ECO:0000255"
FT COILED 1001..1094
FT /evidence="ECO:0000255"
FT COMPBIAS 1..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 148344 MW; 9E90BCD5A8A75327 CRC64;
MFSGSNSYLG GNSGRQPPQQ QPQQQQQYGG FQPNQGFQPQ QTGFQPQQTG FQPQPTGYGN
VAPLQPNFTG YPLQAQPTGY SQPPQSGFPG GQQQFNNAPQ QQSFQTGAPP MPQIPQQFQQ
QPQQIQQAQP SPAAPVQQPQ ATGFAAMADS FKSASEPSKP RGRRASKGGA KIPSIRLSFI
TAQDQAKFET LFKSAVGDGQ TLSGEKSRDL LLRSKLDGNS LSQIWTLADT TRSGQLHFPE
FALAMYLCNL KLVGKSLPSV LPDQIKNEVS SMVDIINFAI EDDGPAGTNA PSFDSRQSTA
TPPTIQQPQP MPSNSALLTA QMTGFPGQQN NFSGGFQSQP TGFQSSMQTG FPGQQGGLQP
QPTGFSQNMS NPQATGYTGP RPPMPPMPSN FSSNLSPAQT GMQGGMIAPL NSQPTGVPGQ
WGLVNAPATG LPNIDLLQSR MMPQQGREQG NFTTAGITGN AVIPWAVTKE EKTRYDSVFK
AWDGFGKGFI GGDVAIEVFG QSGLEKPDLE RIWTLSDHGN KGKLNMDEFA VAMHLIYRKL
NGYPLPAQLP PELVPPSTRN FNDSIGAVKS LLHQESDFRK NSGATLLPQK TGLKKKVREK
QVLLDAIDFK DENAADEDDA LDRKDRREAE DLYRRIRRIQ EDIDAHPDAS LRNVDSGAER
RAMKRQLQTL TDKLPDIASR VRRTERSIAD AKLELFRLKD AKAHPGSASS IVGTGPGGAV
TESDRLKARA KAMMQQRSAA LTGKKIEISN DDLDAPKRLE EENLKIRTEK ENNERMVQDV
EESVRDFSRG LEDSLKDGGE SSSSEHEKRR WEDGLGVEDE VKDFIFDLQR SSRSAKVRTD
DRSREAPTET SRVSSAPAAR SETPSSQPSS TPTPSAGTYS QYKTAEDRAA YIKQQAEQRM
AERLAALGIR APSKPGETTQ QRLEREKNER AAKLKQAEEE DARREAERQA RIAEEQGVAP
HTPDQPKEIT KKPPPPPSRK AARSDASERK FEEDRILKEQ KSQIIATNEL EDDAQRQENE
LAKEREAAQA RVKALEEQMK AGKLKKEEEK KKRKALQAET KQQEARLAAQ RAEIEAAQAR
ERELQRQLEA IDDSDSSDDD EGPEQVTPQA STPTQGSQEF ERKEASPPPP PPSVPVIVSP
VPAAATTTSL PPPTPQVTSP VVSPPAETET RNPFLKKMAQ SGDASAASTA SNNPFHRLPS
QELPAPAPIQ VQPTGNRPSR VRPEEDDWDV VGSDKEDDSS DDEGPGAGGA RHLASILFGT
MGPPRPLSAM GNEATSAPHS PAAASPPVAS PPPPPPMPSA GAPGGPPPPP PPPPPGMGAP
PPPPMPPMGG APAAPPAGGR PAGFLGEIQM GKALKKTQTK DKSAAATAGR VLD
