PAN1_KLULA
ID PAN1_KLULA Reviewed; 1324 AA.
AC Q6CQX9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; OrderedLocusNames=KLLA0D13398g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382124; CAH00756.1; -; Genomic_DNA.
DR RefSeq; XP_453660.1; XM_453660.1.
DR AlphaFoldDB; Q6CQX9; -.
DR SMR; Q6CQX9; -.
DR STRING; 28985.XP_453660.1; -.
DR PRIDE; Q6CQX9; -.
DR EnsemblFungi; CAH00756; CAH00756; KLLA0_D13398g.
DR GeneID; 2893445; -.
DR KEGG; kla:KLLA0_D13398g; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_006042_0_0_1; -.
DR InParanoid; Q6CQX9; -.
DR OMA; PQRTGMQ; -.
DR Proteomes; UP000000598; Chromosome D.
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; 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; PF12763; EF-hand_4; 2.
DR SMART; SM00054; EFh; 3.
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..1324
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349477"
FT DOMAIN 199..288
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 232..267
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 494..583
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 527..562
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 622..690
FT /evidence="ECO:0000255"
FT COILED 999..1036
FT /evidence="ECO:0000255"
FT COMPBIAS 318..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 540
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 544
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 551
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 1324 AA; 145295 MW; B74937625748836D CRC64;
MYNQYQQQPQ QPQQFGGQQQ FNAQPQSTGY GNFYQQQVPT QGQQQQFSGF QTFSNAGALN
QQPTGFSQQT QAQPQQPQQQ QPQSQPQQGM QQPFGNQQQQ MPLTQQLTGF NSMMPQTSFG
QPQQQMPMNT SFNQGMSTTA VNAPTGPLQP QQTGFYSQQQ PLEPLKPTAT GFINSFANTG
VDNTLKIPAI RLSFITTQDQ AKFEKLFRSV VTPGSNTITG DQCRNILVKS GLQPHQLAKI
WTLSDTNKAG VLLFPEFALA MYLVNSVLQG DSIPYELDSR TKAEVSSFVD AINFSVSNDS
EVEQKPKTPF DDLTAGISMM QPQPTGYMPQ LSFGSQPQQM QQQQQQQQQQ PQQQSFQGLT
QQPTGGYGAA PQTSFGNTSQ ALQPQSTGFM PQNSFNQPLN AQTTGGFSSV LNIPPPGSMP
QTSFTQQAPM QTSLATGGGF LQPQATGYLP PSNFQATAPL QAQKTGFGNN DLYTSANLAS
KFIARKEEAI TPEEKSLFYK IFETYDVEKT GNLDSATAVE IFRKSGLNRS DLEHIWNLCD
TNNSGNLNKQ EFALGMHLVY RRLNGEVLPN TLPPSLIPSS TKILNTVKDQ LKQGVDKNNR
QPTKEDGLRF RNNDDELLPS SRNRRKTIDQ SKKVNENKEK IENLKNLIRE KKELLASEKL
RLENDSQRKQ SENADLLRSI ENLKSQIQAL PSTSKKSPSA NNAVPHDLQS RFDTLTARIP
NLFKEISDVS KELVSSQLAL HHLKVDHPIR GSGPNCKITE LDCKNARQRL TLTAGMCTLV
GRPEPNYDNL EAQAQHFNEG IETIEKDDQK NQSAINNIST WIQEISSSVQ AIIHGRTPSM
GLEMDKWESG IGLEPEVRDF IISWKNRRNF DNSSYNTAGY SNGIQISSSA TYRNNARAPE
EKDSYSSFQT PEERSAYVKE QAKKKMEEKL AALGIKKKSG SSQSSPNPPQ LTQQQQPQQQ
QQQQQQQQQQ QQQQPNYYQQ PSQPAAAVNN SNLPKANDDD DEDEEDEEER RLLEQLEKLK
LKKKQEKEAR LAAKRQTSSS PAETKNDNGH DSWDDEPTPT NPTGNQSQAG SHHQYNPFGK
SEATQQKPAS GAGTPQLNNT PTGGRNPFFK QAPSQSSSFD LKAAEQQRRV QRGLDDSDGW
SDDDETEKVN TTANKAVDVS STAVPATSTA SVPVAPSLPQ ISATTQEQSS VAVPIAPPLP
LVKSESSLIP PPPPLPTSIT EGSGAPPVPI APPLPQINSD VAPAVPVAAP LLKVGGTATL
AENEEPKPDD ASDVLSIPES VASDEEDKFH TPGAEDVSVA PTGAIPPAPP APPVPVIPPP
PPMP
