PAN1_CANAL
ID PAN1_CANAL Reviewed; 1396 AA.
AC Q5AHB1; A0A1D8PGW1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; OrderedLocusNames=CAALFM_C203380WA;
GN ORFNames=CaO19.8505, CaO19.886;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17431925; DOI=10.1002/yea.1489;
RA Martin R., Hellwig D., Schaub Y., Bauer J., Walther A., Wendland J.;
RT "Functional analysis of Candida albicans genes whose Saccharomyces
RT cerevisiae homologues are involved in endocytosis.";
RL Yeast 24:511-522(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, ECO:0000269|PubMed:17431925}.
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:0000269|PubMed:17431925}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17431925}; Cytoplasmic side
CC {ECO:0000269|PubMed:17431925}. Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:17431925}. Note=Localizes at sites of polarized
CC growth like the hyphal tip.
CC -!- SIMILARITY: Belongs to the PAN1 family. {ECO:0000305}.
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DR EMBL; CP017624; AOW27374.1; -; Genomic_DNA.
DR RefSeq; XP_721009.2; XM_715916.2.
DR AlphaFoldDB; Q5AHB1; -.
DR SMR; Q5AHB1; -.
DR BioGRID; 1220357; 1.
DR STRING; 237561.Q5AHB1; -.
DR PRIDE; Q5AHB1; -.
DR GeneID; 3637386; -.
DR KEGG; cal:CAALFM_C203380WA; -.
DR CGD; CAL0000184200; PAN1.
DR VEuPathDB; FungiDB:C2_03380W_A; -.
DR eggNOG; KOG0998; Eukaryota.
DR eggNOG; KOG1029; Eukaryota.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_001619_0_0_1; -.
DR InParanoid; Q5AHB1; -.
DR OrthoDB; 597979at2759; -.
DR PRO; PR:Q5AHB1; -.
DR Proteomes; UP000000559; Chromosome 2.
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 InterPro; IPR003124; WH2_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.
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..1396
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349471"
FT DOMAIN 122..211
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 155..190
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 472..561
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 505..540
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1365..1382
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1037..1093
FT /evidence="ECO:0000255"
FT COMPBIAS 611..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1396 AA; 152369 MW; E61D9B421CB1CA29 CRC64;
MYNPYQQQQQ GMGYNPQQQT GYGYNNYQMP QQPQFNQQPM YPQATGFVPQ QPNLYGSNFQ
TSGGSGMAPQ QTGFSQQQTM QPQQTGYIQT QPTGFGGTAP IVTENSELKI PSIRLSFISA
EDQKKFEHLF RTAVPKGEQS ISGDSASGIL LRSGLSAVTL AEIWNLSDID KTGSLLFPEF
ALSLHLCSMA KRGEPLPGIL PEKWLNEVRS FVDQINFTVP DDPSKILANT PFANFAPKKE
SDWLAPQSTG YLQNQSAPPM TSFQPQVTGF GGQGLVSQAT GGVPMPSTTF GNAAGLTAQR
TGGGTLIPLQ PQQTAGLIPA QKTGPLNPQT TGFNQQSLQQ QRTGGLPQQL TGYQGPPQGQ
GQQLQQQRTG GFPQVQSQPT GGFVPQTSFQ QPQLVSQRTG PMQAQPTGSL QAQPTGRPGE
WGFVSMPTGG IPGLNAMQQH FLPNNQLPTS NLHSAMDNKL KENVTWAITK QEKQIYDGLF
QAWDNQKKGY VDSNVALNVF TKSGLSRSDL ESIWTLVDTD DTGKLNKNQF AVAMHLIYRR
LNGYDIPLRL PPELIPPADR TLKDTMDSLK NSLKGGVNNK PTKPPKPQSK PDGTRFKNDD
NNFGYVSNVR HRRKSTSDES HKSSVKSSSD YDLSIEDMKK LIHEKRILLD ALDTEDQANN
YSRSSSSMHE KQIIENLKKE IMAVQTKLDE RGNDGPSSDE RNKLLATLDH LTRDVVPRLI
SDIHKVNQEI SRKKAEVFKL ELLKKNPSWN PEDDESQIQG TGPNGEVTDY DRIKYQSRQK
LKQRMAALTG KSTGGNSDLD LELKQATEKA QDEASRQSEM IQDIAAGIKT MEDECAAKLS
SSVTEDVGHE KWEQGKGISS EVAKFVKELE AFSKEQRRNI AKSQKQEQTR EPLAKQQTNA
SLVSDSGAAK SAYATPEERA AYIKQQAEKR MNERLAKLGI TRKSKSTEQK PPVESKSVSN
HSPVPDSEVK SVTRNANEVE VQKPKPDSQP VSKNREPAEQ PNSKADTNSV GSQNVVSNTN
DDTSGDDDDE EYKAILKQKQ EMEARERERK LRKQKAKEER LAKIKKEMEE MKKREMEESQ
DEEEEEAKQV TSVHVSRAQS SNANSNVIPQ QETATENVNT VSQPTSTDTA KQSYHPHESN
PFSKMNNNTS QNSTVTNTGT NPFFKSTSQE TKIDPHKAEA QRASQRGVAS SGGWSDSEEE
ESEEESPNRA GAAKLASLLF GGMPQPPTTS SSSLNNDAEK VSEQEHENAK QVASTPLSND
DNGKTDSGPS GFAGENESSF SQAPPIPVDA PPAPNSIPPP PPPPPQFSNE APPVPDSIPP
PPPPPSVPST VPALPDSMPP PPPPPPPPAA PNNTSSSQQA SGAPNIGALL GQITGGASLR
KVETKVSSGA TVGRVL
