ID A0A0D2CJV2_9EURO Unreviewed; 1463 AA.
AC A0A0D2CJV2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1 {ECO:0000256|ARBA:ARBA00015110};
DE AltName: Full=Actin cytoskeleton-regulatory complex protein pan1 {ECO:0000256|ARBA:ARBA00020728};
GN ORFNames=PV07_06135 {ECO:0000313|EMBL:KIW30390.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW30390.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW30390.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW30390.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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.
CC {ECO:0000256|ARBA:ARBA00025194}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000256|ARBA:ARBA00011159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the PAN1 family.
CC {ECO:0000256|ARBA:ARBA00009351}.
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DR EMBL; KN847042; KIW30390.1; -; Genomic_DNA.
DR RefSeq; XP_016250606.1; XM_016393087.1.
DR STRING; 569365.A0A0D2CJV2; -.
DR GeneID; 27345329; -.
DR VEuPathDB; FungiDB:PV07_06135; -.
DR HOGENOM; CLU_001963_1_0_1; -.
DR OrthoDB; 2734911at2759; -.
DR Proteomes; UP000054466; 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 Gene3D; 1.10.238.10; EF-hand; 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 PANTHER; PTHR11216:SF177; ACTIN CYTOSKELETON-REGULATORY COMPLEX PROTEIN PAN1; 1.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
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; EF-hand; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 2.
DR PROSITE; PS51082; WH2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT DOMAIN 174..262
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 453..542
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 486..521
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1430..1447
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 712..753
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 27..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1266
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1463 AA; 158167 MW; 188192ECAE730FA8 CRC64;
MYSSSNSFLG GTNSARPGPA PGGFGPQQSF GSFNQAPPQQ QSPFAPQPTG FPGQLQAQQT
GFPGYQQPQQ GFQAPAQQPQ FTGYPPQNQP QQPQFQQPPP QAPAFQQQPS FQAAPPAPPQ
QPPAAAPLRP QQTSAQIAAS FTQGSTSAPA AKRRQSKSSS RIPNIRLSFI TATDQAKFEQ
LFKSAAGEGQ ALSGEKAKDL LLRSKLPGSA LSQIWVLSDT TKSGQLLFPE FALAMYLCNL
RLTGKELPGV LPEKIKNEVS SMVDIISFGV PDEKPLPPTR SNVPDFDAPL RQNAVSPPAP
QQPTPQQPSN QQLLTQLTSQ PTGFYNQATG FQPGLQSQPT GFPGLSQGLQ AQATGFVNPA
QPAGFGGARP SMPLMPTGGF GSNVSPQQTG PLQAQPTGLP GQWGFVNTPA GGLPNIEALQ
QRLMPQSGRE AGGYTTQGLS GTAKIPWAVT KDEKRIYDQL FRAWDGLGRG FIAGETAIEI
MGQSGLERSD LESIWTLSDP NNKGRLNMDE FAVAMHLIYR KLNGYPIPAR LPPELIPPST
KNFNSSIDTV KSLLSQDAEA RKSSGAFLQP QKTGISYLKD HSFRSSSASP NFGRKDATVF
RNNDDDVGYR SSARRRLGHG GRTPSPAPSS DMGDSVYDEL TPDQIRKKIR EKKILLDATD
FQDERQADDD DVLDRRDRRE AEDLFRQIRR IQDDIDTHPN AGFAGGDTGA ERRAMRRELQ
RYQDRLPALA SDVRKVEKNI AEAKLQLFRL KDAKAHPNSA SNIVGTGPKG TVTEADRIKA
RARARMQARA AELAGRPAPA ADDEAGAQRR LEQESSKVKS EQERHEAMTR DVEESVKDFV
SSLEDGLRDQ GENATQEHER RRWEEALGVE DEIKELIYDL QRSSRTAKIR KEEQSRPARK
ASRDYSHDEA TSTNGNLPSR PAPSSAPSAS PVTTGHSQQD RIATAKEKAL KRIQERMAAA
GIKPAGESSE TPQQRQEREK QERAERLRKA EAEDARREQE RQQRLANEGV TPPSPKAEKK
PPPPPTRKQR QDSTDFSAKK AAEAAARAKA EEEAAAQIRA EQEAEARERE RLEAQAKTQE
DELEKEREAA QARLRALEEQ VKAGKVKKQE EKARKKAAER EAKEKEAKLA AQRAELEAAR
ERERQLQLQL EHLGDESSSD EDDEGPQQIT PQESTPATSQ LLTGSIASPP PSTTAPEPSA
SSGHEPTPVS SPPAAEESRN PYFRKLSQTQ PSENGRPVFS PPPIPQAQTF SPPPAAPQPP
APAVESLPST NPFHRIAQQE AAKPLTPSFT GAQSRRRPEE DEWSAAGSEK DEDSDDEADH
PGGGSAKHLA SILFGTMAPP RPLSAMDSKP QTPVQEPPPI PGAFDSGSAP PPPPIPGAGA
PTAPPPPPPM PDSGAFNAPP PPPPFPTSGA PGGPPPPPPM PAPARAGTGD IGALLGEIQK
GKGLRKTETK DRSASSVAGR VLD
//
