ID A0A0D0C9M0_9AGAM Unreviewed; 1083 AA.
AC A0A0D0C9M0;
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};
DE Flags: Fragment;
GN ORFNames=PAXRUDRAFT_834026 {ECO:0000313|EMBL:KIK79582.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK79582.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIK79582.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK79582.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
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}.
CC -!- SIMILARITY: Belongs to the PAN1 family.
CC {ECO:0000256|ARBA:ARBA00009351}.
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DR EMBL; KN826240; KIK79582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0C9M0; -.
DR STRING; 930991.A0A0D0C9M0; -.
DR HOGENOM; CLU_007200_0_0_1; -.
DR InParanoid; A0A0D0C9M0; -.
DR OrthoDB; 1518208at2759; -.
DR Proteomes; UP000054538; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00052; EH; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
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; 1.
DR Pfam; PF02205; WH2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00027; EH; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 1.
DR PROSITE; PS51082; WH2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000054538}.
FT DOMAIN 224..313
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 257..292
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1059..1076
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..601
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..730
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..785
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..905
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1083
FT /evidence="ECO:0000313|EMBL:KIK79582.1"
SQ SEQUENCE 1083 AA; 117290 MW; AD5331C50A7F340C CRC64;
MSQWGPPGFQ YPMPQTGIPS VQPHQQQFQP GHWQPMNPSA QFQQPQGGFA AQPGVPAMGV
GFGGLAPQPT GFTGARPPPP PPPVPPLPSQ FQQGAPPPPP LPQQPSLLNK FGGSSPSSFT
SPSLAVQPTG VGFVSQYTGF PGRIPTSLSP QVTGFVDPRL QLIASSFMPA NVTSPYSSGG
APQLAPPLQQ EPGGLSFQQS FQQHNQSHGR GTTPKIPWVL SKGEKKQYDQ IFRAWDAQGT
GFLNGDTALE VLGQSGLDRN DLAKIWMLAD ADSRGKLNLA EFHVAMGLIH RRLNGSDIPD
ELPHELVPPS TRDLDTSVDF LKDILKNDTR ARAHSPSAFD TPISRLKERS FTSSSSSFTQ
QGGRQDATVY KHQETEPPGG FYQPRNRHVD RSAVRSRADD ASPAVSDLSS IKRQLLNTQK
MLDDTLATER SADALDRDLE DLRYRIRRLQ EDLEYVSKGP KTATKDEEKR RLERDLVRLM
HEEIPELERK LEEREAKRER EQRQWARDRD RRNQRSGRFG DDDGGSHSPA SRYRQEEDSR
GASRYDHDDR DYDRDRSYRD RDVDRDRELS PATRTPPPPP APPANNTSQP PPAPPARSPV
PAIKNMTPAE RQAFLRAEAQ RRLDARKQAL GIVTPSSTSV ASPTLDTTIE NRLAQEKKEA
EERVREAEKQ ADEREKQRKE KLEAEKALKE GKFLSPTPTT RAPAPAPGPV PTPTAPTSKV
APPPPKPRAR PLPPPRKESA TRAVAPLAQE PAPPAPPAPP APPVPIPTIR SILSPAVPPA
PVEPVEDPED VALRQRTEAL NRRREERAAM LRKLEEEEEE ARKAEEAYRA RRDQFLATKA
ASPTVSPTPS AVNSPSPPPP PAPPVPVPVP FPAALTAAEE PEFEEVAPPP PPPPPPAPPA
SAPPGDKSST NPFSRLMKEG AGSTPPAPQA ATANSNPFFR AQAASPAVPA PPKSPGIPPP
VKTTYHTAPK DSDDEWDDVM EKEDDDSSDG ELGTRDTRMG LAQQLFGTLL PSRPQSAGPP
PQSTGSPASP PPPPPPVPLA PAALPTASAP IAAPPPTGNR SALLSAITGG ARLRKAVTND
RSA
//
