PAN1_ASPTN
ID PAN1_ASPTN Reviewed; 1469 AA.
AC Q0CPW4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=ATEG_04270;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476599; EAU34717.1; -; Genomic_DNA.
DR RefSeq; XP_001213448.1; XM_001213448.1.
DR AlphaFoldDB; Q0CPW4; -.
DR SMR; Q0CPW4; -.
DR STRING; 341663.Q0CPW4; -.
DR EnsemblFungi; EAU34717; EAU34717; ATEG_04270.
DR GeneID; 4320329; -.
DR eggNOG; KOG0998; Eukaryota.
DR eggNOG; KOG4392; Eukaryota.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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:0006897; P:endocytosis; IEA:UniProtKB-KW.
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; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF02205; WH2; 1.
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..1469
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000349469"
FT DOMAIN 175..263
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 207..242
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 466..555
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 499..534
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1436..1453
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 641..767
FT /evidence="ECO:0000255"
FT COILED 973..1172
FT /evidence="ECO:0000255"
FT COMPBIAS 1..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 159065 MW; A6FE360360AF9FA5 CRC64;
MYSSSNSFLG GANSARPGQQ PPFMQQQQQP SYSQFPPGQQ QQPQPTGFAP QPTGYAQPQL
SSFGSQLQPQ PTGFPSGQLQ PQFTGFPGAA PQQSQQPQPT GFQPQQPQFT GYPPQSQPPQ
LQVPAATGLP LRPAQTSSEI ANSFRDASGA APPPPPKSSG SKIPNIRLSF ITAQDQAKFE
QLFKSAVGDS QTMSGDKARE LLLRSRLSGS DLSKIWVLSD STKSGQLFFP EFALAMYLCN
LRLTGRDLPD ALPETIKNEV SSMVDIISFQ VPDTQPEPVV RTNVPNFDAP LMENKLAPPA
PQQPQPQQPT NSQLLNQLTA QPTGFLSQPT GLSPNQAPFG QQSNLAPQPT GLPGQPQQQS
LQPQPTGFMS NPQPTGYSGP RPPVPPIPTG YASNLSPSQT GGMSGLVAQP TGIPGQWGFV
NAPSSGLPNI EALKQQLMPQ PGREGGFSTA GLAGNASIPW AITKEEKKIY DDLFRAWDGF
RKGFIGGDTA IEIMGQSGLN RQDLERIWTL ADPNNRGRLN MDEFAVAMHL IYRKLNGYPV
PNRLPPELIP PSTRNLNDSI GTIKSLLSQD AESRKATGAF LQPQKTGVSY LKEHSFRGGA
VSPGVGRKDA TLFKNDDQAA AGYRSSARRR VGNNGRTPSP AASSQASEDE LSVEQLKKKI
RETQIMLDAV DFQDETRAEE DDALDRRDRR EAESLMDRIR RVQDEIDTHP NAAFRNLDNG
AERRSLRRQL QAYEDQVPQV ASEVRRVERE IAEARLELFR LKDAKAHPNS ALNIVGTGPG
GTVTEADRIK ARARARMQAR AAELAGRPAP ATQDDEGAAA RRLESESANV KADREKNDAM
TRDVEDSVKD FARSLEDSLK DVSENSTREH EKRRWEDALG VEDVIRDFIY DLKRNSRTAH
IRKEEASRAS PSQSQQSRYD EPPAVRPSPP PSTGSTGSLP GTTHEDRVAA AKERAQKRIA
ERLAAAGLKP HSEASETLVQ RQEREKRERE ERLKRAEEED ALREQERQRR LAEERGTPAQ
PSTKPIGKKP PPAPPSRRAR TDSADQSEAK KAADEAAKVE QTAREQAIRE EQQVQEEETK
RLEDEARQRE EEFMKEKEAQ EARLRALQEQ VQQGKIKKQE EKRRKEEAER RAKEQEAKLA
AQRAELEAAK ERERQLQREL EAMEEESSSD DEGPEFATPR NGSPAQTEAP TAEAPPPPPP
APATAPPVPA IAEPEAPTSP ATSPASSRAN LSPEAESKNP WFKKIGQPAD SQPAPVPQAA
TTPSDTHSTN PFHRLAQQQE STAPAFTGSA PLERKTRARP EDDDDWSAAG SEFDSSDDED
DRAGGGSAKQ LASILFGTMA PPRPLSAMDD KSPSKTPTPV QETPAPAPEA DAAPSAPVAA
PPPPPPPPVP AAAPNGSAGA PPPPPPPPAP PMAPPPPPAG VPPPPAPPAA PAGAADRGAL
LASIQAGKGL RKVQTNDRST SSTAGRVLD
