PAN1_EMENI
ID PAN1_EMENI Reviewed; 1484 AA.
AC Q5B5B0; C8V406;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=AN4270;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000069; EAA58938.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF74351.1; -; Genomic_DNA.
DR RefSeq; XP_661874.1; XM_656782.1.
DR AlphaFoldDB; Q5B5B0; -.
DR SMR; Q5B5B0; -.
DR STRING; 162425.CADANIAP00004384; -.
DR PRIDE; Q5B5B0; -.
DR EnsemblFungi; CBF74351; CBF74351; ANIA_04270.
DR EnsemblFungi; EAA58938; EAA58938; AN4270.2.
DR GeneID; 2873692; -.
DR KEGG; ani:AN4270.2; -.
DR VEuPathDB; FungiDB:AN4270; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001963_1_0_1; -.
DR InParanoid; Q5B5B0; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00027; EH; 2.
DR SMART; SM00246; WH2; 1.
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..1484
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000349476"
FT DOMAIN 173..261
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 205..240
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 460..549
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 493..528
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1452..1469
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 635..760
FT /evidence="ECO:0000255"
FT COILED 807..843
FT /evidence="ECO:0000255"
FT COILED 965..1011
FT /evidence="ECO:0000255"
FT COILED 1052..1165
FT /evidence="ECO:0000255"
FT COMPBIAS 305..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1484 AA; 160720 MW; F24863BD6C48E1F0 CRC64;
MYSSSNSFLG GANSTRPGQQ PYMQQQPPFS QFGQQQPQNQ QTGLAPQPTG YNPQFSALGA
SQLQPQATGF PPGQIQPQYT GFPGVSPQPQ QTQPTGFPAS PQQTQYGGFP SLGQAPQIQV
TSNTNIPLRT GQQTSSEIAN SFQNASVATP TPPPKASGGK IPNIRLSFIT AQDQAKFEQL
FKSAVGDSQA MTGDKAKELL LRSKLPGSDL SRIWVLSDTT KSGQLLFPEF ALAMYLCNLR
ITGRDIPSVL PETIKNEVSS MVDIISFQVP DTQPEPVAKT NVPSFDAPLL ENKLAPPAPQ
QPRPQQPSNS QLLSQLTAQP TGFPPSSGYQ ANVAVQGQNQ GLVPQATVFP GQASSQNLQP
PQMGILNNPQ PTGYTGPRPP MPPMPTGFGS NLSPSQTGGL VAQPTGIPGQ WGFVNAPASG
LPNIEALKQQ LMPQPGREGG FSAAGLSGNA SIPWAITKEE KKIYDDLFRA WDGLHKGFIG
GDTAIEIMGQ SGLARNDLEA IWTLADPHNR GRLNMDEFAV AMHLIYRKLN GYPVPNRLPP
ELIPPSTRNL NDSIGTIKSM LSQDAEHRKA TGAFLQPQKT GVSYLKEHSF RGGAVSPGAG
RKDATLFKNN DEAAAGYRSS ARRRVGNSGR TPSPAASQAS EEELSVEQLK KKIRETQIML
DAVDFEDENR AEEEDALDRR DRREAESLMD RIRRVQDDID THPHAALRSL DTGAERRTLR
RQLQAYEDQV PQIASEVRRV EREIAEAKLE LFRLKDAKAH PNSALNIVGT GPGGAVTEAD
RIKARARARM QARAAELAGR PAPASQDDEE AATRRLEGEN ARVKAEREKN DSMTRDVEES
VKEFARSLED SLKEGEESST REHERRRWED ALGVEDVIRD FIYDLNRGSR TAHIRKEEDS
RGSSLEPRSR ESSAHTSTAA RPSPPASVGL TGASPVTHED RVAAARERAQ RRIAERMAAA
GLKPQTDAIE TLAQRQERER REREERVKRA EEEDAKREQE RQRRIAEEQR TPSTQAAKPA
GKKPPPAPPR GSRKGRTDST GQADAKKAAE GSAKTEQLAL EQALKEEQQA QEEETKRLET
EAKQREDEFA REQQEQEARL RALEEQVRQG KIKKQEEKRR REEAKKAAQE QEARLARQRA
ELEAAKERER QLQLELEGLD ESSSDEEGPV DIATPQDSTP TQSQVLPATS DPEPPAPPTP
VAEPPTVPEP EQTTASSSPE SSRAVSLRLS PETESKNPYF RRNVSQPTDY PPPTPPEVPQ
VSSTQMPDTQ STNPFHRLAQ QQQPPPPPPT QPAFTGSAPL ARKTRARPEA DDDWSAAESD
FESSDDEDDR AGGGSAKQLA SILFGTMAPP RPLSAMDTQS PSSKSATPVQ GSSIPPVPPI
PAEIEPSSVA DGASPPPPPP PPPPPPPAAA PPPLPSAESP AGIPPPPPPP MAPPAPPPPP
GPPAAAPAGA PDRSALLASI QAGKGLRKVQ TNDRSTSTSA GRVL
