ID   PAN1_COCIM              Reviewed;        1485 AA.
AC   Q1DQC1; A0A0D8JVG9; I9XL05;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN   Name=PAN1; ORFNames=CIMG_07492;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
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).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704913; KJF60936.1; -; Genomic_DNA.
DR   RefSeq; XP_004445197.1; XM_004445140.1.
DR   AlphaFoldDB; Q1DQC1; -.
DR   SMR; Q1DQC1; -.
DR   STRING; 246410.Q1DQC1; -.
DR   EnsemblFungi; KJF60936; KJF60936; CIMG_07492.
DR   GeneID; 4559664; -.
DR   KEGG; cim:CIMG_07492; -.
DR   VEuPathDB; FungiDB:CIMG_07492; -.
DR   InParanoid; Q1DQC1; -.
DR   OMA; PQRTGMQ; -.
DR   OrthoDB; 597979at2759; -.
DR   Proteomes; UP000001261; 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; 1.
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..1485
FT                   /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT                   /id="PRO_0000349474"
FT   DOMAIN          157..245
FT                   /note="EH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          189..224
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          438..527
FT                   /note="EH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          471..506
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          1453..1470
FT                   /note="WH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..1485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          647..737
FT                   /evidence="ECO:0000255"
FT   COILED          1024..1150
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..363
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..843
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..938
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1015
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1172..1188
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1219..1272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1348..1362
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1387..1448
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1485 AA;  162595 MW;  FD077CFC2EC10589 CRC64;
     MYSSSNSFLN PNAARPGQQQ YGQPQQQYTG FQQQQQPTGF MPQPTGFAGG QMQPMQPQPT
     GNFSRGPFQQ SSFQAQPPQM TGYPPQNQPF QPQQQQSQTM QQQSTPAPSL PARLPGQTSS
     QIANSFQTIS SPTTGVNPHH APSKIPTQRL SFITAQDQAK FEQLFKSAVG DSQSMDGETA
     RDLLLRSKLP GSELSKIWVL SDTTKSGHLL FPEFALAMYL CNLRLTGREL PPSLPDRVKN
     EVSSMVDIIS FAVPDDNPPV APKTNVPNFD QPLMQNTSAP PAPQQPQPQQ PSNSQLLSQL
     TAQPTGFYNQ ATGFQPPSIV APQPTGFPGQ NASLRPQATG LQPNPQATGY TGPRPPMPPM
     PAGFGSSLSP SQTGAPPLAA QPTGIPGQWG FVNAPATGLP NIEALKQRLM PQPSREGGYT
     TAGLAGNATI PWAVTKDEKK IYDQLFRAWD GLNKGFIGGD VAIEIMGQSG LDRQDLERIW
     TLSDPHNRGR LNMDEFAVAM HLIYRKLNGY PIPNRLPPEL IPPSTRNLDD SIGAVKSMLS
     QDAEQRKVSG AFFQPQKTGV SYLKTHSFRT GSASPGLGRK DATVFKNNDD DVVAYKSSAR
     RRAGGTPSPS PSSTPAEKVD NDLSVEQLKK KIRETQIMLD ATDFRDENRA EEDEVLNRRD
     RKEAESLMER IRRVQDDIDT DLKAAFRNAD SGAERRALRR QLQAFQDQLP ELASNVRKLE
     RSIADSKLEL FRLKDAKLHP GAAMEIIGTG PGGAVTEADR IKARARARMQ ARAAELAGRP
     APQADDGSAA RRLEEEKATV AAERERHDAM TRDVEESVKE FSQSLEDSLR DQDENSTRDH
     ERRRWEEALG VEDQIRDLIF DLQRNRRTAK VRKEEERAMR ADNSSYLQPQ ARNRSPVNDD
     GRRRTSPLRS ASASPSFAGL SHEERVASAR ERAQKRIAER MAAAGLRPSS DASESFPERQ
     EREKREKEER RRRAEEEDAK REAERQKRLA QEKSPVTSPP PKPSSKKPPP PPSRKVRTDV
     TESVEAKKAE DSVVASKARA EQEEKERALK QEQEAQEAER KQLEDEAKRQ EEELAREKEA
     AQARLRALEE QVRQGKIKKQ EEKRRKQQAE KEAKEKEARL AAQRAELEAA QARERELQRQ
     LENMGEEESS SDDEGPIEIT PQTSTPTQSQ VLPAPFPQPS PPTAALPVPA IQEPDQDVAR
     EPSPTLPSPV ETPEPVKQTL PPETESRNPY FRQLSQQSAP SAAQPTHEMQ STNPFHRLAQ
     QESTSKSAFT TDATVPGPLE RKSRVRPEED DWSAAESENE SDEDDDRVAG GSAKQLASIL
     FGTMAPPRPL SAMDEKTESK AQSPVQNAVV TPPPPPPAPE ADDSPEIEAE REIADMSPAA
     PDDAGFYTPP SIPPPPPPPM PGMEASAGAP PPPPPPPPGD APPPPGGAPP PPPGPPPPAP
     PGPAPGPPGR EAGRGALLAD IKAGKGLRKV VTKDRSGVAT AGRVL