PAN1_AJECN
ID PAN1_AJECN Reviewed; 1481 AA.
AC A6R7X5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; ORFNames=HCAG_06416;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476660; EDN09249.1; -; Genomic_DNA.
DR RefSeq; XP_001538811.1; XM_001538761.1.
DR AlphaFoldDB; A6R7X5; -.
DR SMR; A6R7X5; -.
DR STRING; 339724.A6R7X5; -.
DR PRIDE; A6R7X5; -.
DR EnsemblFungi; EDN09249; EDN09249; HCAG_06416.
DR GeneID; 5445123; -.
DR KEGG; aje:HCAG_06416; -.
DR VEuPathDB; FungiDB:HCAG_06416; -.
DR HOGENOM; CLU_001963_1_0_1; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000009297; 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 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 Pfam; PF08226; DUF1720; 2.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 2.
DR PROSITE; PS51082; WH2; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endocytosis; Endosome; Membrane; Reference proteome; Repeat.
FT CHAIN 1..1481
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349462"
FT DOMAIN 173..261
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 205..240
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 453..542
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 486..521
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1449..1466
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 601..784
FT /evidence="ECO:0000255"
FT COILED 900..1097
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1346
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1370
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 160222 MW; D4D5E4354EF5D897 CRC64;
MYSNTFYGGS SSRPGPTGFG QQQPPPPPPP PPPQQQQQQQ QPQQQPFPGF SQPQQQNLQP
GAFMPQATGF AGSNPMQQMQ MPMQQPQPTG FPPSHQFTGF PLQNQQPPSA VTAVTQQQLS
APLPNPPHET GMTSTQIAHS FAQPATPAVP AQQHASSGSK IPNMRLSFIT AQDQAKFEQL
FKSAVGNNQA LDGETAKDLL MRSKLPGSDL SNIWVLSDTT KSGRLLFPEF ALAMYLCNLK
LTGKELPSVL PERIANEVSS MVDIISFAVP DARPAPPQTN VPKFDAPLMQ NASAPPAPQQ
PQPQQPSNTQ LLSQLTSQPT GFYNQATGLQ PPSIVQPQQT GFPAQNAGLR PQQTGFLSNT
QPTGYNGPRP PMPPMPTGYG SGLSPSQTGL APLNAQPTGV PGQWGFVNAP ATGLPNIEAL
QQRLMPQPGR EGGFTTQGLS GNATIPWAVT KDEKKIYDQL FRAWDGFNKG FIGGDVAIEI
MGQSGLERQD LERIWTLSDP NNRGRLNMDE FAVAMHLIYR KLNGYPVPNR LPPELIPPST
RNFNDSIGTV KSLLSQDAES RKSSGAFLQP QQTGVSYLKN HSFRSGSSTP GAGRKDATVF
KNNDDAIGDR REAESLMERI RRVQDDIDTD PKAAFRITDS GAERRSLRRQ LQSYQDQLPE
LASNVRKVER SIADARLELF RLKDAKAHPS AAAAIVGTGP GGTVTESDRI KARARARMQA
RAAELAGRPP PSTDDDGAAA RRLEEETASV KAERERNDAM TRDVEESVKE FTRSLEDSLK
DVDENSTREH ERRRWEEALG VEDTIRDFIY DLQRASRTAR VRKDERTASS QRSVSNNRYD
NVSSNGDTLP VRPSQPQSTG SPSLAGLTHQ ERVTSAKERA QKRIAERMAA AGLKPNSDGS
GETLLERQER EKREREERRK RAEEEDAKRE QERQRRIAEE QNGPPVKAAT TGKKPPPPPS
RKGKADGVSP AETRKLGDLK NAAREKAEHE GKERALREEQ LAQEAESRRL EAEARQQEEE
LAREREAAQA RLRALEEQVR QGKIKKQEEK RRKQLAEKEA KEKEARLAIQ RAELEAAQAR
ERELQRQLEG LDEEESSDDE GPVEVTPQNS TPTQSAVLPS ATTTMASPPS VPRPATPPAA
PFEPELAFEV ASATSTSIPS PESVKQRVAA DTESRNPYFR KMGQSVDTQP PSFHTPPEQI
PDPLSTTEVA PPPASAPAPP KTEIQSTNPF HRLAQQQESQ KSAFAAAPLP GPLTRKSRAR
PEDDEWSIAE SENSSDDDDD RPAGGSAKHL ASILFGTMGP PRPLSAMDEK PESKSATPVQ
ESPTVAASPP PPPPPPPPPS EPAPVTTLPP AVAAQDVEED DDDDDENDFQ DAPSMPPPPP
PPPVPAPFAD APPTAPPPPP PPAFSAAAPP PPPPPPPVGG APGGPPPPPP PAGDAPAIPK
AAVPDAGAGR GALLASIQAG KGLRKVETKD RSAASVSGRV L
