ID A0A139HF35_9PEZI Unreviewed; 1431 AA.
AC A0A139HF35;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AC578_8190 {ECO:0000313|EMBL:KXT00979.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT00979.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT00979.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT00979.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXT00979.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFZN01000064; KXT00979.1; -; Genomic_DNA.
DR STRING; 321146.A0A139HF35; -.
DR OrthoDB; 2734911at2759; -.
DR Proteomes; UP000070133; 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; 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; PF12763; EF-hand_4; 2.
DR Pfam; PF02205; WH2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
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:UP000070133}.
FT DOMAIN 159..247
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 434..523
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 467..502
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1399..1416
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 691..732
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1393
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1431 AA; 155106 MW; E75DA1202D4CBFE0 CRC64;
MFSSSSSYLG GANSARQQPQ YGQQQGFQQQ PQYGAQQPGF GQAPLQQQYT GYPAGALQPQ
ATGFPGQQQP QQQYGQQQQQ YPGFQPPQPT GFQQPPQQQQ PPQQTGFQQP VQPQPTGMTS
NDMANSFRSS ATQPAPSTPA KSGGSKIPNI RLSFITAADQ AKFEQLFKSA TSGEQALSGE
KAKDLLLRSK LDGNSLAQIW TLSDTTKSGQ LLFPEFALAM YLCNLKLTGK TLPSSLPEKV
RNEVSSMVDI ISFAVEDSSS GSAPSSNAPN FNEPPKIQQP QAQNPSNTQL LSTLTAQPTG
AFQGLVPQPT GFQQPQQAGF QQPMQTGLQP QATGFPQGQG YTGPRPPMPP MPTGFGPSSG
LSPQQTGYPM AAPLNAQPTG RPGQWGLVNA PASGLPNLQA MQQQMMPQPG RESGFTTQGL
RGNATVPWAV TKDEKKIYDD MFKAWDGFGK GYITGNQALE IFGQSGLEKP DLERIWTLSD
PHNKGRLNLD EFAVAMHLIY RKLNGYPIPN QLPPELIPPS TRNINNSIDA MKGLLRGEAD
ERKSSGAFLQ PQRTGVSYLK GHSFKANGTR GSRKDATVFK NNDDDVGYRS SARRRVGDHA
RSGSPALSDT SSVNTADDMS IDQLKKTIRE KQVLLDAMDF EDEGKADEED ALDRKDRKEA
EELFRRIRRI QEDIDGHPNS AFKTGDSDAE RRSLQRQLRN MQDRLPELAS HVRRCERAIA
DAQLELFRLK DAKANPSSAQ AIVGTGPGGA VTESDRLKAR AKAMMQQRSA ALTGKKIDIG
DDGTAAAQRL EEESKRVTRE REDNEKMVRD VEESVTEYSK GLESSLKEGA ESASDEHERR
RWEDGLGVED EVKDFIFDLQ RSSRAARVRN EERSQPRAKP PVEDDSSRTS TPVTGTGSPA
SNRAPAASSP ATTGSSYSSY RTAEERAAFI KQQAEQRMAE RLAALGIKAP SKSGGETAAQ
RAERERQERE NKLRQAEEED ARREQERRAR IDGESIVPPS PAATAGKPKP PPPAPRKNRS
ESLQSDTQHK AEVKVAETQI KEQALREQEA ALAKETEQME DEEARQEREL RQQRQEAEAS
LRALEEQVKA GKAKKAEEKK AREAAKRENA EKEARLAAQR AEIEAAKERE RQLRLQLESM
DDDDSSDDEV ERNTPVESTP TQNVEPPKIN EPPPPAPPLP ETSAPPPPPP PPMPETVTSP
PAVSSPPSES KNPFFKSMNQ PAAPTSNGTS PEASEKKDTN PFHRLTQQDL AKQQALPEPT
AAPSRTRSKP ADEDDWSVLE SSDDESDDDD KPQGGSAKQL ASILFGTMAP PRPLSAMDSP
VSGPGSPANA GRIASPPPTS STPSAAPPPP PMPGAFDAPL GAPPPPPPPM PDSGAPPPPP
GPPPAPMPAS SGPPAGLPDR SGLLEQIQLG KGLKKVQTKD RSQAATAGRV L
//
