ID F2PHG0_TRIEC Unreviewed; 1477 AA.
AC F2PHG0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=TEQG_00381 {ECO:0000313|EMBL:EGE01328.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995718; EGE01328.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:TEQG_00381; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001963_1_0_1; -.
DR Proteomes; UP000009169; 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 SMART; SM00246; WH2; 1.
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}.
FT DOMAIN 154..242
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 1445..1462
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 691..718
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1477 AA; 161045 MW; A8E0017B6FD3E3EF CRC64;
MYSFPTGQPG QQQQQYGGQQ QQQYPGFQQP PQQQQQQPGP FMPQPTGYGM PQLQPQATGF
PGAMQQPQPH QQQAPPFQSS LQPPQMTGYP TQQSSSLQVP QPTSQAPQPT GHTSSQMAQS
FQNIPGQAPA APARNAHAGS KIPPMRLSFI TVQDQAKFEQ LFKSAVGDSQ SLDGETARDL
LLRSKLPGSE LSKIWVLSDT TKSGRLMFPE FALAMYLCNL RITGRDLPAT LPDRIKNEVS
SMVDIISFAV PDDHPPQAPR SNAPNFDQPL MQNTSAPPAP QQPQPQQPSN SQLLSQLTAQ
PTGFYNQATG FQPPSAMQPQ PTGFPGGLRP QVTGMPQNPQ ATGYSGPRPP MPPMPASFTS
GLTPGQTGGA APLTAQPTGM PGQWGFVNAP ATGLPNIEAL QQRLMPQAGR ETGTFTTAGL
SGNATIPWAV TKDEKKIYDE LFRAWDGLGK GFIGGDVAIE IMGQSGLERQ HLEQIWTLSD
PNNRGRLNKD EFAVAMHLIY RKLNGYPIPN RLPPELVPPS TRNLNDSIGA VKSMLSQDAE
ARKSSGAFLQ PQKTGVSYLK THSFNSASGG AGYPRKDATV FKNNDDAVGY KSSARRRIGA
GRTPSPATSV RSEKSDDDLS VEQLKKKIRE TKIMLDATDF RDESHAEEEQ AMDRRDKREA
ESLMDRIRRV QDDIDTDPKA SLRNLDSSAE RRSMRRQLQA YQDQLPELAS NVRKTERAIA
DCRLELFRLK DAKENPGSAL EIIGTGPGGA ITESDRIKAR ARARMQARAA ELAGRPAPAA
ADEGAAARRL EEERSKINSE RERNDAMTRD VEESVKEFSA SLEDSLKGDN ENSTREHERR
RWEEALGVED QIRDLIYDLQ RIVDGEDQKE NIICRERDKA SREASNANQY GSQADIQSRP
SPEPRSSSQS PSLAGTTHEQ RVAAARERAQ RRIAERMAAA GLKPADAGES FMERQEREKR
EREERRLRAE EEDAKREQER QRRLESEQAP APPPAKAGPK KAPPPPPSRK ARSDSAEQNE
TKKAEEEALA IRAKEEQEAA LRQEQQAQEA ETEQLEDETR RQEEELAREK EAAQTRLKAL
EEQVRQGKIK KQEQKRRKQQ AEQEAREKEA KLAAQRAELE AAQERERELQ RQLESLGDEE
SSSDDEGPGF VTPEDTTPTQ SQVLEEPKAA IPSPAPPEPV QRPPPAPHIP EIITDDDGAQ
LFRPQSPEPF VHSVMSKPIV PETESRNPYF RQLSQSSSEP SAAETPAPAP APAPPAPETQ
STNPFHRLAQ DNAKSAFSVG TAALPGPLER KSRARPEEDD DWSVAESENS SDDDDRAAGG
GAKQLASILF GTMAPPRPLS AMDEPHDSKA ATPQPTHTPI PPPPAPPIPA SPSPAEQKDE
EPFQEAQEAP SMPPPAPPLP NMAAPSAPPP PPPPPPGGAP PPPPPPPPPL GPAPGGGAGG
PMGMGRGALL GDIQAGKTLK KVVTKDRSTA MSAGRVL
//
