PAN1_DEBHA
ID PAN1_DEBHA Reviewed; 1449 AA.
AC Q6BNL1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; OrderedLocusNames=DEHA2E20856g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG88482.2; -; Genomic_DNA.
DR RefSeq; XP_460209.2; XM_460209.1.
DR AlphaFoldDB; Q6BNL1; -.
DR SMR; Q6BNL1; -.
DR STRING; 4959.XP_460209.2; -.
DR EnsemblFungi; CAG88482; CAG88482; DEHA2E20856g.
DR GeneID; 2902075; -.
DR KEGG; dha:DEHA2E20856g; -.
DR VEuPathDB; FungiDB:DEHA2E20856g; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001619_0_0_1; -.
DR InParanoid; Q6BNL1; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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:0016043; P:cellular component organization; IEA:UniProt.
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; 3.
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..1449
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349475"
FT DOMAIN 128..217
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 161..196
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 480..569
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 513..548
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1415..1432
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1050..1108
FT /evidence="ECO:0000255"
FT COMPBIAS 239..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1449 AA; 157583 MW; 8974B4FA9C619D51 CRC64;
MYNPYQQQQA AYNPQQQQTG FAGGFNQQQQ YVQPQQTGYY NPNQPPSLPN QATGFYQPQQ
QGMFNASSFQ NQPTGFAQQP SIQPQQTGYV QTQPTGFQQP GTNSAPTVTE NSELKIPSMR
LSFITAADQS KFEHLFRTAV PKGEQAISGD SARDILLRSG LQPITLAEIW SLADTNKSGS
LLFPEFALAL HLCNLSLKGD PLPTMLPEKW SNEVKSFVDA ISFSVPENPA NILSNTPFAS
SGASSNPINN DWMAPQATGF NNSGAVPSTS FQAQPTGFGA SQEMMAQRTG NPPLPQQATG
FGSNNVAPLL PQRTGGGTLI PLQPQQTSNL IPAQKTGPLQ PQTTGFQTQN PHQTGPGALQ
PQSTGFAQRM NNGPLQAQTT GFQQQTTGFQ PQSTGFQPQS TGFQPQSTGF QPQQTGPLQA
QPTGKPGQWG FVSTPTGGIP GMNAMEQHFL PSSQLPTNNL QNAMGGSLKT NVTWSITKQE
KQIYDGVFSA WDSRNKGFID GEVAINIFGK SGLARPDLES IWNLADTNNR GKLNKDEFAV
AMHLVYRRLN GFDLPLRLPP ELVPPSTKHI QDSMDTLKNS LKSGSAKSSP PVKPGKTDGK
RYKNDDSNFG YVSNVRHRKK NVSNNDSSNG DEKPSHNSDL TIADLKKLVR EKKILLDAVD
AEDQDAAISN RQMESRNYQE IDSLKQQIRK IQSQLNDNVS SSGSIGERKQ LMDKLNYLTR
DKVPGLISKI HQVNKDIATS KVELFKLKLS KENPDWQPED AEAGIVGTGV NGEVTDADRQ
KFKSKQLLKQ RMAALTGKSH GSGNELDVKL HQEIKNTRSE GEIQSGMIND IEASIKDLED
GCAANLQVTN KEEVGTDKWE NGNNLNEEVA KFVRELNSSK PKQQSSSQVN STLSQGQPQT
QPQSNNVEAG IVSPQVTGAS DSSTASHEYR TPEERSAYIK AQAEKRMNER LAKLGLTRHM
TSGSSSTIEQ QTQNKTTSLY ANSETSKNAE RKLESQPEYQ QQQQQQQQQQ PPPPQRQQSQ
QEAQLQDKGT NGQPDSPRQV GQKPTEIMDN ESDDDNEEYV ALMKKKEEME ARERKRKLKK
KQDKEARLEK LKREMEELKK KEEAGDSSDD EEPITEVASY GPSGSASKSS TTKSIEQPIV
EEKTNEEQIA APVVEADTFV PKTHDNNPFA RIQNNSSTPG SNNGSKDNLF FKPEKEVKLD
PKKAAAQRAS QRGLGDFNDW SDEEENSSED EGPNRAGAAQ LASLLFGGMS QPVPKSSTVT
PNQEFHDAED IPHFDSQESK ENNNGEYTSQ PTSVIQEKPD AIDSTSEAQV KSIPVEVEAP
SPDNFTPPPP PPPSNIPPLP NTSAPPPPPP PPPPMDTPPI PSSSAPPPPP PPPGAAPPLP
NASVPPPPRG APPLPGDSSL SSGTKQAPPS GGNVDIGALL GQIKTGSSLK KVDENEKRIA
DGAVVGRVL
