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PAN1_KLULA
ID   PAN1_KLULA              Reviewed;        1324 AA.
AC   Q6CQX9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN   Name=PAN1; OrderedLocusNames=KLLA0D13398g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382124; CAH00756.1; -; Genomic_DNA.
DR   RefSeq; XP_453660.1; XM_453660.1.
DR   AlphaFoldDB; Q6CQX9; -.
DR   SMR; Q6CQX9; -.
DR   STRING; 28985.XP_453660.1; -.
DR   PRIDE; Q6CQX9; -.
DR   EnsemblFungi; CAH00756; CAH00756; KLLA0_D13398g.
DR   GeneID; 2893445; -.
DR   KEGG; kla:KLLA0_D13398g; -.
DR   eggNOG; KOG0998; Eukaryota.
DR   HOGENOM; CLU_006042_0_0_1; -.
DR   InParanoid; Q6CQX9; -.
DR   OMA; PQRTGMQ; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR   GO; GO:1990964; C:actin cytoskeleton-regulatory complex; IEA:EnsemblFungi.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0071933; F:Arp2/3 complex binding; IEA:EnsemblFungi.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0000147; P:actin cortical patch assembly; IEA:EnsemblFungi.
DR   GO; GO:0007120; P:axial cellular bud site selection; IEA:EnsemblFungi.
DR   GO; GO:0007121; P:bipolar cellular bud site selection; IEA:EnsemblFungi.
DR   GO; GO:0071555; P:cell wall organization; IEA:EnsemblFungi.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
DR   CDD; cd00052; EH; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000261; EH_dom.
DR   Pfam; PF12763; EF-hand_4; 2.
DR   SMART; SM00054; EFh; 3.
DR   SMART; SM00027; EH; 2.
DR   SUPFAM; SSF47473; SSF47473; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50031; EH; 2.
PE   3: Inferred from homology;
KW   Actin-binding; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Endocytosis; Endosome; Membrane; Metal-binding;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1324
FT                   /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT                   /id="PRO_0000349477"
FT   DOMAIN          199..288
FT                   /note="EH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          232..267
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          494..583
FT                   /note="EH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          527..562
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1201..1240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1259..1324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          622..690
FT                   /evidence="ECO:0000255"
FT   COILED          999..1036
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        318..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..914
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..994
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1033
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1152..1175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1204..1236
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1303..1324
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         540
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         542
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         544
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         546
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         551
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   1324 AA;  145295 MW;  B74937625748836D CRC64;
     MYNQYQQQPQ QPQQFGGQQQ FNAQPQSTGY GNFYQQQVPT QGQQQQFSGF QTFSNAGALN
     QQPTGFSQQT QAQPQQPQQQ QPQSQPQQGM QQPFGNQQQQ MPLTQQLTGF NSMMPQTSFG
     QPQQQMPMNT SFNQGMSTTA VNAPTGPLQP QQTGFYSQQQ PLEPLKPTAT GFINSFANTG
     VDNTLKIPAI RLSFITTQDQ AKFEKLFRSV VTPGSNTITG DQCRNILVKS GLQPHQLAKI
     WTLSDTNKAG VLLFPEFALA MYLVNSVLQG DSIPYELDSR TKAEVSSFVD AINFSVSNDS
     EVEQKPKTPF DDLTAGISMM QPQPTGYMPQ LSFGSQPQQM QQQQQQQQQQ PQQQSFQGLT
     QQPTGGYGAA PQTSFGNTSQ ALQPQSTGFM PQNSFNQPLN AQTTGGFSSV LNIPPPGSMP
     QTSFTQQAPM QTSLATGGGF LQPQATGYLP PSNFQATAPL QAQKTGFGNN DLYTSANLAS
     KFIARKEEAI TPEEKSLFYK IFETYDVEKT GNLDSATAVE IFRKSGLNRS DLEHIWNLCD
     TNNSGNLNKQ EFALGMHLVY RRLNGEVLPN TLPPSLIPSS TKILNTVKDQ LKQGVDKNNR
     QPTKEDGLRF RNNDDELLPS SRNRRKTIDQ SKKVNENKEK IENLKNLIRE KKELLASEKL
     RLENDSQRKQ SENADLLRSI ENLKSQIQAL PSTSKKSPSA NNAVPHDLQS RFDTLTARIP
     NLFKEISDVS KELVSSQLAL HHLKVDHPIR GSGPNCKITE LDCKNARQRL TLTAGMCTLV
     GRPEPNYDNL EAQAQHFNEG IETIEKDDQK NQSAINNIST WIQEISSSVQ AIIHGRTPSM
     GLEMDKWESG IGLEPEVRDF IISWKNRRNF DNSSYNTAGY SNGIQISSSA TYRNNARAPE
     EKDSYSSFQT PEERSAYVKE QAKKKMEEKL AALGIKKKSG SSQSSPNPPQ LTQQQQPQQQ
     QQQQQQQQQQ QQQQPNYYQQ PSQPAAAVNN SNLPKANDDD DEDEEDEEER RLLEQLEKLK
     LKKKQEKEAR LAAKRQTSSS PAETKNDNGH DSWDDEPTPT NPTGNQSQAG SHHQYNPFGK
     SEATQQKPAS GAGTPQLNNT PTGGRNPFFK QAPSQSSSFD LKAAEQQRRV QRGLDDSDGW
     SDDDETEKVN TTANKAVDVS STAVPATSTA SVPVAPSLPQ ISATTQEQSS VAVPIAPPLP
     LVKSESSLIP PPPPLPTSIT EGSGAPPVPI APPLPQINSD VAPAVPVAAP LLKVGGTATL
     AENEEPKPDD ASDVLSIPES VASDEEDKFH TPGAEDVSVA PTGAIPPAPP APPVPVIPPP
     PPMP
 
 
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