PAN1_YARLI
ID PAN1_YARLI Reviewed; 1634 AA.
AC Q6C908;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; OrderedLocusNames=YALI0D15304g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382130; CAG81042.1; -; Genomic_DNA.
DR RefSeq; XP_502854.1; XM_502854.1.
DR AlphaFoldDB; Q6C908; -.
DR SMR; Q6C908; -.
DR STRING; 4952.CAG81042; -.
DR PRIDE; Q6C908; -.
DR EnsemblFungi; CAG81042; CAG81042; YALI0_D15304g.
DR GeneID; 2910754; -.
DR KEGG; yli:YALI0D15304g; -.
DR VEuPathDB; FungiDB:YALI0_D15304g; -.
DR HOGENOM; CLU_001963_1_0_1; -.
DR InParanoid; Q6C908; -.
DR OMA; PQRTGMQ; -.
DR Proteomes; UP000001300; Chromosome D.
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; 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..1634
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349487"
FT DOMAIN 233..322
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 266..301
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 576..665
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 609..644
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1599..1616
FT /note="WH2"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 748..803
FT /evidence="ECO:0000255"
FT COILED 831..859
FT /evidence="ECO:0000255"
FT COILED 1131..1198
FT /evidence="ECO:0000255"
FT COMPBIAS 9..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1634 AA; 171976 MW; F29C5DC8538EA5F3 CRC64;
MYGYQGTGGQ QPLGAQPTGF GFGNTPVQQQ QQPMQPMQQS QPTGYQAPGG FQNYQPTGFA
QQQQQQQPQQ TGFQSMQPPM QQTGFQSQPN VSMYQGGGGQ GYQSAPMLHQ QTMQTGYQPQ
QQQPGFTGFQ PQQQQQQQQT GFTGFQQQPQ QQQPGFTGFQ SQPTGYNANA SAPAATPAAP
LQQQKTGNAR DPFAPTLPAR PPLTSQPTGG GNKSVVDGVY IPNVRLSFLT ADDQRNFENL
FRQALPKGEQ ALSGDKARDI LFRSGLPPIT LSAIWNLADT TRSGALLFPE FAVAMYLCGQ
AVKGQTVPNN LSENIKNEVS SMVDIISFNI PDAGSRPSSS GQSVPQSQPQ QQQQQSSASM
LAGLNLGQPT GYQQQQATGY QPMQQQSTGY PMQAMQPQIT GGMPLQQQRT GPMQPLQQQS
TGYAPLQSQL TGGAPLQSQL TGGAPLQSQL TGGAPLQSQL TGGAPLQQQS TGYAPLQQQS
TGYAPLQQQS TGYMPQQQTG MQPQSTGYGS MQPLTAMPTG KPGQWGFINT PSQGLPGIET
MQQRLMPQAT GAPVQQLPPM QLQQSATVNW AIAKEEKQIY DGIFMAWDKK RAGAIDGDTA
IKIFTQSGLN RADLEAIWTL SDPSNKGRLD RDEFAVAMHL IYRHLNGYPI PSRLPPELVP
PSSKNFSDSV NQVKSYLKAG GGRTGGSKLK SRSFTGDSTI KKDATVFKND DSDFGYTSRN
RRGGSSSTAS SNGSSGNDIS LSGKGSSISE LKKLIREKQI LLDAIDAEDS DMSRDSNLER
RDQEAVADLK RRIQNVQRDI DVAPHSAIST DVGASADAKR NLMRKLDHLG DRLPQLASNV
RRIEDKIANA KMELFRLKNP TSLVGTGPGG AITEADRIKA RSKAKLQARM AALTGKGTTT
GADASEEEDY EHRLLTHTSE VERSKAQNYE MIHDIEDSVK SLQRDLSSKL RETQEEVSED
RQRRRWEEAV GVEDDVRQFI YSLRSTRSSR PAPATASSSA PATGSPATAA PISATSTGAS
TPSAPAAGVD RKAQLKAEAE RKMNERLAAL GIKRKEKAQA HGFAPPDAKP AEASPAASPA
VASPAVASPA ATPAVSSPAP VSRGVPAPAA ATPATDPATT PAVPVSAPAD DSDSDDEEYE
KLMAQKREQE ERFKKQQEAD KKKEEEKKQK KAAKEERMRK LREEMEANEA REKAWKESQS
KEAEADEAEG DVGAAALAAF SNKATAPSTT PTAVAATPPV ATSTPSPAAP TVPAADDNNP
FHRLNNGGDA AAAAPAAGGE DNNPFLRPGT NQPIAAPSPA SFSEAPKEAP KPVDPVKISN
QRANQRAAKN DDDDWGMSSD EDDDQDYHRG NAAELASQLF RTMAPPIQRQ PTGGAPITAT
PTGSAPAAPP AAPPVAPAAV EVAVAASEAT PGPESAPPAP PMPEINIPPA TEAPSAPAAT
EAPPAPPSAP TTIETTHLPP PVDTHNDMSS SEFDFETPEG SPTQQTFAEA APPVAAPPPP
PPTAAAAAPT GIPPPPPSAP GFGAPEAPSG IPPPPPPAPG FGAPPPPPGP APSFDAPGGA
PPPPPPGPPP PMFGAPAPPS MTGPSAGDLP ERPPAATGGI TALLGEITGG KTLRRVDDKD
KKISSNPSAG AVLN
