PAN1_CANGA
ID PAN1_CANGA Reviewed; 1374 AA.
AC Q6FPQ7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; OrderedLocusNames=CAGL0J01892g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
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DR EMBL; CR380956; CAG60736.1; -; Genomic_DNA.
DR RefSeq; XP_447787.1; XM_447787.1.
DR AlphaFoldDB; Q6FPQ7; -.
DR SMR; Q6FPQ7; -.
DR STRING; 5478.XP_447787.1; -.
DR EnsemblFungi; CAG60736; CAG60736; CAGL0J01892g.
DR GeneID; 2889812; -.
DR KEGG; cgr:CAGL0J01892g; -.
DR CGD; CAL0133524; PAN1.
DR VEuPathDB; FungiDB:CAGL0J01892g; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_006042_0_0_1; -.
DR InParanoid; Q6FPQ7; -.
DR OMA; PQRTGMQ; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:1990964; C:actin cytoskeleton-regulatory complex; IEA:EnsemblFungi.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; IEA:EnsemblFungi.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
DR GO; GO:0007120; P:axial cellular bud site selection; IEA:EnsemblFungi.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IEA:EnsemblFungi.
DR GO; GO:0071555; P:cell wall organization; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
DR CDD; cd00052; EH; 2.
DR InterPro; IPR013182; DUF1720.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 2.
PE 3: Inferred from homology;
KW Actin-binding; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endocytosis; Endosome; Membrane; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..1374
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349472"
FT DOMAIN 206..295
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 239..274
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 569..657
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 601..636
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 706..783
FT /evidence="ECO:0000255"
FT COILED 1050..1103
FT /evidence="ECO:0000255"
FT COMPBIAS 681..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 614
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 616
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 618
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 620
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 625
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 1374 AA; 150836 MW; 659FE29FB5089AF6 CRC64;
MYQYSNQTGN GVYGNPPMQP LQNYGSSGYQ QTAPMQQPLQ TGYQQPMQQT MNQNQGMQLP
QQQYQQQQPL QQQPMQQQPM QQQSFQQPQL QQPLQQQPTQ TGMQQQPLQQ QLTQSGMLQQ
PLQPQMQQSS QTIQPNQLNV QNTVQSQQSV QPLLPQQTGF YRQGNQPVLE PLKPTATGFV
NSFANNGLDN NLKIPAIRLS FITAQDQAKF ETLFRSIVTK GSNTVSGENC RAILMKSGLQ
PSQLARIWQL SDTNRAGELL FPEFALAMHL INNVLQGDSI PYELDSKTKN EVSSFIDAIN
LSVVSTESDF KTPFDDLFKP QQSLQPQGTG FLPQTSFGLP AQPTGGFGQP QPTTFGQLQA
QVTGGFGQPQ PTTFGLQPQT TGGFVQAQQV TGGIAQQPSM NPLTQQGTGF AQNQQGTGGF
LQQQGTGSFN NAGFVQPQNT GSFVPQQQQQ PVVQSQPIAP QSTGGFGPPM PTTFGIQPQS
TGGFVQPQVT GGLQPALTGN IPQTSFGAQP FNQQLQPQAT GYLPPSQFSA TMPLTAQKTG
FGNNEIYAQS NFNGPSFSTQ ESDIITSEEK SLFYKIFETF SQNRGVLDSA TAVEIFRKSG
LNRSDLEKIW NLCDINNTGQ LNKQEFALGM HLVYGRLNGR SIPDRLPPSL IPSSTKILDN
VKNQLISSSS DGNRKSFTRM DALSYKNDDN DKLPNFRNRR KNYPTDNDAD KERQRRQERE
REEAAKKKEQ ERKTKMDIER ARKQGSFTNS EPEFTDVSVS EIEDIKRRIT EAQQKLAVRN
QSIPNDLKKR FNEVVARLPT LFVEIYKVDT EIMQARIELC KRRTPSSIIG TGPGGSITED
DRRKAKSKAL LRSRMNALTG KGDNSDEPDI ESESFTKEIE KIQSESAQNK KIIKDIRISI
SELSAPIRSI MTGSLPTCSS TDFEKWEIGV GLENDVREFV LTLKKGLLYV SEPSHMNSNQ
TLSHPPAAAL KKEATGEDRA AQLKEQAQKR MKERLAKFGI SRRETRDLES SKQQESGSTP
DAVPAAQTAN ASQTPFEEVI SSPQKMEVTS TAGEDNEEED EEERKLKEQL ELLKQKKNAE
KEKRLADLRR QIEEAEKEEE HPSVAQSNSG NVQSSSNQPA SVPVANSQPQ NLQNTHITTK
PLSLNQTGSS YDMASNTYFK PTQTSQSAFD REKAEQQRKI QRGLESDDDG WSDDDDDLYS
KPNTAPQTAP VLDSSNTPQP GMNASVPAPI APPIPTPQAS SPAVPVAPPI PAVTPSESSI
PMTSNADVAG ADHLDQDTDI SGAAASADKQ NTSHVSHIPP VPVAPPLPQV SSIAPPPPLP
NLSVPQPHET VDNDDGSDVL SIPDSVESDK EDLAPAGHTP AAMGIPPPPP LPNF
