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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
 
 
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