PAN1_PICGU
ID PAN1_PICGU Reviewed; 1440 AA.
AC A5DP36;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; ORFNames=PGUG_05037;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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; CH408160; EDK40939.2; -; Genomic_DNA.
DR RefSeq; XP_001483082.1; XM_001483032.1.
DR AlphaFoldDB; A5DP36; -.
DR SMR; A5DP36; -.
DR STRING; 4929.XP_001483082.1; -.
DR EnsemblFungi; EDK40939; EDK40939; PGUG_05037.
DR GeneID; 5124796; -.
DR KEGG; pgu:PGUG_05037; -.
DR VEuPathDB; FungiDB:PGUG_05037; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001619_0_0_1; -.
DR InParanoid; A5DP36; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000001997; 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 SMART; SM00054; EFh; 3.
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..1440
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349482"
FT DOMAIN 117..206
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 150..185
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 480..569
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 513..548
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1405..1422
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 627..686
FT /evidence="ECO:0000255"
FT COILED 1024..1076
FT /evidence="ECO:0000255"
FT COMPBIAS 241..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1022
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1254
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 155758 MW; EF87BC9978DEE42D CRC64;
MYNPYQQPSY GAPQQPQQTG YGFNATGGNA MPQSQFQSTG YYQQQPTYQQ PGFQPQQTGF
QPQATGYSVP QTSYQTGFQV QQTGFQPQQT GFQQQSAETN TELKIPNIRL SFITASDQSK
FEHLFRTAVR KGETAISGDA ARDILLRSGL PPVTLAEIWS LSDTNKSGSL LFPEFALSLH
LCNLALKSEP LPSVLPEKWS NEVQSFVDAI SFSVPEDPSK ILANTPFASL GTEEKTSWMD
APAAPSTSFQ PQLTGFQPPQ MPAQRTGGQI TAQRTGGGSL IPLQPQQTAG LVPAGLQRQN
TGYQPPQPLQ SQNTGFQSSV GRQNTGYQPP LQQQGTGYQP LKQQNTGYQP PLQQQGTGYQ
PPLQQQGTGY QPPLQQQGTG YQPLQSQGTG FQSQGTIQPQ GTGFQPQSTG FQPQPTGLSS
QPTGKPGQWG FVSTPTGGIP GLSAMEQHFL PNTQLSSNNL QNAMGGSLKT NVTWAITKQE
KSIYDGIFQA WDKSRQGFID GETAIGIFGK SGLARPDLET IWNLADGDNK GKLNKDEFSV
AMHLVYRRLN GFDLPLRLPP ELIPPSKKHI QESMDSLKNS LRGGNNKPKR TQTSSSLYKH
DDDDVGYVST ARHRKKSDSS SGSGSGTMSI EQLKKEIREK KILLDAMDSE DRDSSVLSQR
DREWNEREIE SLKFRILQAH NKLESSGISG SHEEKVQLLD RLRHLTQDKM PKLISNIHVV
NNEICSRQMK VAKLRLQKEH PDWAPEASDA DIVGTGPNGE VTDYDRKKFK SKQLLKRRMA
ALSGAKTGST DTAVDDQLAK ATEDAKNLGD QQRKMIEEIS GSIKDLEDGC ISALQSTTRE
DSYEKWEKGQ GVSSDVAAFI RSLPKSEGSK NGRNEKTQSP YTQPTKSQSQ SAQSTQSQSQ
STQSVQTQPA QPATYSSYSS PEDRAAYIKA QAEKRMNERL AKLGITRRKE TGSKAPEVPK
EPVEAPKPQE IETPKETETQ RETNTKSTSQ TSKAEPQKVS VPPAIPSSSQ APAIPSPAIP
PAPEDDSEDE EYAALMKQKQ EMEERRLRKK KEKEERLARL KREMEEMNKE EDSDEEPVTS
VPTYTNGSVK SSTQPISQSE EVPKTEEEKS GESEQTASKP EATPTEQAPK PDLVSTSAQS
KANPFSKNNN PFFKPTQTPT IDPKKAAAQR DSQRGLGSDD WSDSDDNSSD DDGPNRAGAA
RLASMLFGGM APPPRAPTIE KEETGSKETA EVPPPTEVAP PPVPAAPPAS VPPPISAASS
KETDSDDEWG TPSAEAANDH DDFDFGNNFE PSMAPSPPPV PTQHIPEPVT DVPPIPQSIP
PPPQSFAATV EDAPPPPPIP SQVPPPPPPP PSLFPTESSN APPAPPPPPP PSAPSAVPPP
PPMAPAAPPS APAPSPGGPP GGAPNIGALL GQITGGKSLK KVDDSQKRIA DGATVGRVVD
