PAN1_ASHGO
ID PAN1_ASHGO Reviewed; 1248 AA.
AC Q75AA0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; OrderedLocusNames=ADR018C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 300; 308; 318; 331-332; 875;
RP 942 AND C-TERMINUS.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51938.2; -; Genomic_DNA.
DR RefSeq; NP_984114.2; NM_209467.2.
DR AlphaFoldDB; Q75AA0; -.
DR SMR; Q75AA0; -.
DR STRING; 33169.AAS51938; -.
DR EnsemblFungi; AAS51938; AAS51938; AGOS_ADR018C.
DR GeneID; 4620263; -.
DR KEGG; ago:AGOS_ADR018C; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_006042_0_0_1; -.
DR InParanoid; Q75AA0; -.
DR OMA; PQRTGMQ; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
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; 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: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; IBA:GO_Central.
DR GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
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; 1.
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; 3.
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..1248
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349463"
FT DOMAIN 93..182
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 126..161
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 426..449
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 427..516
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 460..495
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 313..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 566..601
FT /evidence="ECO:0000255"
FT COILED 713..746
FT /evidence="ECO:0000255"
FT COILED 787..879
FT /evidence="ECO:0000255"
FT COILED 965..997
FT /evidence="ECO:0000255"
FT COMPBIAS 800..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 477
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 1248 AA; 134238 MW; 3FA541F82E30F5BC CRC64;
MYNPYQQSGG PAYGADGYGQ QGYGQAYGQQ GFGQAYGQQG GGYEAGPAAT YTAGAAQPLR
PTATGFVNAA ASRGLNTELK IPLFRLSFLT AADQAKFETL FRSAVRPGAT TITGEDCKHI
LLRSGLSPFQ LGLIWTLCDT NNAGELLFPE FALAMHLVNG VLQGERIPRA LDSKVKNEVS
SFVDLINFSV GSNSPPPEGQ KARTPFDALT QGAGTLQPQA TGFMPPTSFG VPQATGLGFG
QAPMQPQATG YMPPTSFGAG LGAHTTGGNA LASQMTGGLQ QYAGGAFQNY QATGGKGLGA
QVTGGFAQQP AGANPLLSQL TGGQGFQQQR QPTGANSLMP QVTGGFQQPS NAIGSQPPAM
GMPQGLSQGQ SVGLQAQATG FLPPSQFAPT APLAAQKTGF GNNEIYSHAA FASGFPAGED
DKLTPEEKSL FYNIFDTYDT DKTGQLHFKV AAEIFRKSGL NRSELERIWN LCDTNNSGQL
NRQEFAVGMH LIYRRINGHN LPHTLPPSLV PSSTRILNNV KNQLKVSSSS KKEPTRIDGL
AYKNNDDDIL PSFKNRRKTF TEPRQSKDNK TVDDLKKLVE EKRRKLESER SQLSLRQKDQ
QIKDEETMRH VDSLMHQIRS LPMKKHAAVP SDMKARFDSL TSSISTLFNN IAEIDDEITN
AKVHLYRLKN PSSIVGSGPN GEVTEYDQKK ARQKAVLAAR MAALTGTPIE TPSEADLRRE
EQGLNEEVAK IKEESRKNQE ILNDIKSSIT EISAPISTFI YGSGNADKDP AYERWELGIG
LEPEVCDFIR KLKETQTQAQ AQEQARAQEQ ARAQEQARAQ EKARAQEKAR AQEQARVQEQ
ARAQEQARAQ EQARAQEQAR AQEQARAQEQ AKADAASRES TRSPEEFARW PQDQSPSHPG
LTASVSPQSQ SVSVSNRGTP QLGQQQMGSG FYSDYQSADA RAAYVRQQSQ LKQPAPAPTS
TTDFNSEDEE DEEERSLREQ LAALKLKRKA EKEAKLAVGR NQTGASQDPA VRASPDEWDE
QPSRPSHTPV YSTSPAMASQ GELPKQGSSA PHLHPTTTGD RSPFFKQKQG STSTFDLKAA
EQQRRLQRGL DDGDGWSDDE DSSSKPTQPT ATTSATDIPS SGADSGARAP VSAAPASIVR
PDGSTATQPP VVPSPPVPQP GPSSGAPIPI APPLPTLNGQ QAGPAPSVAP TGHVERAASQ
PQINDGNEDD EDSDVLSIPE SVESEDGKDQ YTTAIPEIPY IPPPPPLP
