PAN1_LODEL
ID PAN1_LODEL Reviewed; 1505 AA.
AC A5DVD6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; ORFNames=LELG_01322;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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; CH981524; EDK43144.1; -; Genomic_DNA.
DR RefSeq; XP_001528802.1; XM_001528752.1.
DR AlphaFoldDB; A5DVD6; -.
DR SMR; A5DVD6; -.
DR STRING; 379508.A5DVD6; -.
DR PRIDE; A5DVD6; -.
DR EnsemblFungi; EDK43144; EDK43144; LELG_01322.
DR GeneID; 5235850; -.
DR KEGG; lel:LELG_01322; -.
DR VEuPathDB; FungiDB:LELG_01322; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001619_0_0_1; -.
DR InParanoid; A5DVD6; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000001996; 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:0016043; P:cellular component organization; IEA:UniProt.
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..1505
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349478"
FT DOMAIN 85..174
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 118..153
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 492..581
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 525..560
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1474..1491
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 677..752
FT /evidence="ECO:0000255"
FT COMPBIAS 588..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1505 AA; 160431 MW; 23B501FA9DAC80B0 CRC64;
MFNSYQATGM GYNPNQQQQQ PPPPQQQQQL YSQPTAFGQP NLYGSNMQQG YIQTQPTGFA
GAPTVIENNE LKIPSIRLSF ITAEDQKKFE HLFRSAVPRG EQSMSGDTAS NILLRSGLTP
VVLAEIWTLS DIDKTGALLF PEFALSLHLC NMAKRGEPLP GVLPQKWHNE VQSFIDAINF
SIPDDPNKIL ANTPFAKKDD WLSNVGQPQS NWMAPQGTGY PQTSFLQNQA TGFAQQPTGF
GQQATGFGQQ ATGFGQQSSW LAPQATGFNN SAPPPSTSFG GTGTGIVAGA GAGASAAPTG
GFVPLQPQQT AGLIQKPAGL QPQSTGFMAP QRTGGLAPQA TGLAPQATGL QAQRTGGFGV
PQQATGYQQS FNTGGLQANK TGPLQPNHTG YNFQQQQQQQ QQATGLQRQP TGVLQQQPTG
YLQQQPTGYL QSQPTGRPGE WGFVSMPTGG MPGLNSMQQV FQPNNTQTYQ DLHKVMNDNS
ASNVTWAISK QEKQIYDRLF QAWDTGRNGY VDSNVALNVF TKSGLGRQDL EAIWTLADTD
DVGKLNKNQF AVAMHLIYRR LNGLEIPLRL PPELIPPADK TLKDTMDSLK NSLKNGGAKQ
TRSKPMTKPD GSRFKNDDSD FGYVSSSRYK KKSEEEKQAN ARTSKDFGLS IDDMKKLIRE
KKILIDAMDV EDEDRQRTSD REVDALKSKI YELQKKLSGS SNNGGNSKEA LLAKLERTGK
RIPSLLQQLN QVNQEISEKS VELVKLQLKR EDPSWDEAKV DVSGAGGKFD LKQKMAMLTG
KGGSAMADSK YRDAVEKSKS DLKNQSDMVK DIESGIRSLE DDCSAKLRTT AKNAVGYEKW
ENGFGVSKAV ADFVKELNKL KADAQPEFAR SADNTTTARS SSAYAQQVPP AASRTFSAQE
TNASPGAVTS TGTGGSGSGS GSATYSTPEE RAAYIKAEAA KRMASRLEKL GISRTKRAPK
AAEKHDEIVS KPSPSREEPP RLSGEAAIAN PVERAPSADK TPVNTAHAES HAQTTSSNRA
PEAKPEQVSV PVESQRENFR ENKWDEEKQY RPSQTNNNDN NNISSTHQSQ EHIVKENAKN
VESAPQAPTS NYSQQPPAFG GAFQSESSRA TETEQAESKK ESETTPVVPP APAAASTEPA
QPAQPAQASQ ASKPAQPAQP ANSTEPASAS ASEQPAVRRH ENNPFFKNKF QPVDTQKISM
QRNFQRGTSN DNSWSDSEEE DSEDEAPNRA GAAQLANLLF GSMSSQPTGN AAFAKSAAQE
PSKDEKSIGA ENASGHESKM NAELSSSENT AAGVSQVNET PAQSSYEEPS LQEQSSYESN
AVPAAPSLPE SVPPPAPAPE APSLPQSVPP PPPIPSEYSA PPAPSLPRDV PPAPEAPSLP
QSIPPPPPVP SEYSAPPAPP APPAPSLPQS IPPPPPVPSE YSAPPAPPAP PAPPAPPAPS
LPSSIPPPPP APPLSSNDSS LASAAAPPAG GAPNIGALLG QITGGKSLKK VETKVSSGAT
VGRVL
