PAN1_PICST
ID PAN1_PICST Reviewed; 1373 AA.
AC A3LN86;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; ORFNames=PICST_55255;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000496; ABN64814.2; -; Genomic_DNA.
DR RefSeq; XP_001382843.2; XM_001382806.1.
DR AlphaFoldDB; A3LN86; -.
DR SMR; A3LN86; -.
DR STRING; 4924.XP_001382843.2; -.
DR PRIDE; A3LN86; -.
DR EnsemblFungi; ABN64814; ABN64814; PICST_55255.
DR GeneID; 4837591; -.
DR KEGG; pic:PICST_55255; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001619_0_0_1; -.
DR InParanoid; A3LN86; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
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:0016043; P:cellular component organization; IEA:UniProt.
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 InterPro; IPR003124; WH2_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.
DR PROSITE; PS51082; WH2; 1.
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_0000349483"
FT DOMAIN 116..205
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 149..184
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 465..554
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 498..533
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1338..1355
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 271..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1007..1066
FT /evidence="ECO:0000255"
FT COMPBIAS 283..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1330
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 147329 MW; FD269C5E0EC76A84 CRC64;
MYNPYQQQQA GFAPQQTGFA YANQPSQQPQ QSQSQLANQA TGFYQPQLQQ QTLFASSQFQ
PQTSFGTVAS IQPQQTGYIQ TQPTGFASQG IAAPTVVENS SLKIPSIRLS FITAEDQKKF
EHLFRTAVPK GEQAINGDSA STILLRSGLT PVTLAEIWSL SDTNKSGSLL FPEFALSLHL
CSMAKRGEPL PGYLPEKWAN EVKSFVDAIS FSVPEDPDKI LANTPFASFS GTNTQDDWLS
NLNNQTNSAA ATSNFGAPGF TSFQPQATGY GGGLPLASQR TGPGLASIGT TSFSAPTAPT
APTAAPLASQ RTGGGTLIPL QPQQTAGLIP AQKTGPLNGF PQQLQQQSTG YQPQLQQLQQ
QSTGYQPQLQ QLQQQSTGYQ SQLLAQRTGP LQSQSTGFQP APLQSQPTGR PGEWGFVHTP
TGGIPGLNAM QQHFLPNADL PTNNLQNQMG GDLKSNVTWA ITKQEKSIYD GIFQAWDTTR
RGYIDGDVAL NVFSKSGLSR PDLESIWTLA DTSDRGKLNK DEFSVAMHLV YRRLNGLDIP
LRLPPELIPP SNKYLQDSMD TMKNSLRGGV NNKSYSGGKQ TKSDGTRFKN DDDDFGYVSN
ARHRRRSTAT DNGPKSIKSS SDSDLSVEDL KKLIREKRIL IDALDAEDQD AVLNKKKESQ
HNIDIIEKLK SQIKDVQASL NSKGLDAPIE EKKQLLGVLN SLTRDKVPNL ISNIYKVHND
IAKAKVELLK AKLLKQNPSW NPDSNESEIQ GTGPNGEVTE LDRRKFQSKQ LLKQRMAALT
GRTSNSGSNA DLDLQLKQES EKAKSESINQ SNIVKDIESS IKELEDGCAT HLQTSATEES
GSEKWERGQG ISAEVAAFVR ELNSFAESQR RNIAAQNSSS LESSTVSSTA EVSQPASSVS
SQPVSASSSY RTPEERAAYI KAQAEKKMNE RLAKLGISRS RNATIAEPNP PTKVDAQPAT
PPVAPAVVES AAVSPPVKKQ PPPVSPRSVR VEQQKPAPPV DSSSDDDDEE YAAILKQKQQ
LEAKEKERKL AKQKQKQARL DKIKKEMEEI KRRQAEAEAE EDSDEEPSSV PTYTVSNSAP
KAVAKTAEDP VVEPVIAKSV EQEAVPDQVA APKAHESNPF SKVQATPTGN STNPFFKPTT
KESTIDPKKA AAQRASQRGL SKNDGWSDSD DNESEDDQPN RAGAAQLASL LFGGMAPKSK
ESTPQQTPQQ EKTESEALSK SVSTLKDPSG SDDEFSTPPP DAPSQQTVAP PIPTEVPPIP
TGAPPIPTGA PPIPTEAPPI PVGGPSSFAP PPPPPPPPPP GPPPIPNAPF GAPPPPPPPP
GPPPPVSNGV TAPPVTADIG ALLGQIQGGK SLKKVDASQQ KISSNDLAGT VLS
