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Database: UniProt/TrEMBL
Entry: A8PA90_COPC7
LinkDB: A8PA90_COPC7
Original site: A8PA90_COPC7 
ID   A8PA90_COPC7            Unreviewed;      2084 AA.
AC   A8PA90;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 2.
DT   24-JAN-2024, entry version 100.
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=CC1G_06124 {ECO:0000313|EMBL:EAU81913.2};
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU81913.2, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU81913.2, ECO:0000313|Proteomes:UP000001861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC   {ECO:0000313|Proteomes:UP000001861};
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAU81913.2}.
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DR   EMBL; AACS02000002; EAU81913.2; -; Genomic_DNA.
DR   RefSeq; XP_001839934.2; XM_001839882.2.
DR   STRING; 240176.A8PA90; -.
DR   GeneID; 6016557; -.
DR   KEGG; cci:CC1G_06124; -.
DR   VEuPathDB; FungiDB:CC1G_06124; -.
DR   eggNOG; KOG0998; Eukaryota.
DR   eggNOG; KOG1029; Eukaryota.
DR   eggNOG; KOG4305; Eukaryota.
DR   HOGENOM; CLU_235129_0_0_1; -.
DR   InParanoid; A8PA90; -.
DR   OMA; DWWKAEQ; -.
DR   OrthoDB; 2734911at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd00052; EH; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd00174; SH3; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000261; EH_dom.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003124; WH2_dom.
DR   PANTHER; PTHR46006:SF6; GUANINE NUCLEOTIDE EXCHANGE FACTOR, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR46006; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR AT 64C, ISOFORM A; 1.
DR   Pfam; PF12763; EF-hand_4; 1.
DR   Pfam; PF16652; PH_13; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00027; EH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 2.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 2.
DR   PROSITE; PS51082; WH2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          240..329
FT                   /note="EH"
FT                   /evidence="ECO:0000259|PROSITE:PS50031"
FT   DOMAIN          273..308
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          1065..1082
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   DOMAIN          1214..1273
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1274..1333
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1743..1931
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1969..2064
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..1184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1350..1527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1577..1672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..776
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..838
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..875
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..947
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..976
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1020
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1021..1058
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1108..1125
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1382..1409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1410..1426
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1427..1441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1488..1524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1577..1597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1598..1623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1624..1638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1646..1660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2084 AA;  229032 MW;  354B11A301016AFD CRC64;
     MSQWGQPQQG FQYPMQTGFQ PGNPQFQQNV QFQPQGPQMG QQQPQFQPTG QGFQQGGFGA
     PGGGLQPQPT GFPMQRPAGF QQPQQTGFPG GQQMPLQAQP TGFVGGNFGQ QQAAPPPVPP
     LPQQFQQQNQ GGPMQGLQQP QQPNRFLTTS PGLGAGLVPQ ATGFPVRTGP LVPQATGFVD
     PRLQMMSQTF MPMNTSAPFT PGGMPQLPPQ QNLQQSFQQY NQDQRGTATQ QMSWALSKAE
     KKNYDRIFRS WDTSNSGFIS GQNALEGFSQ CGLPQAELAK IWSLADIDDR GKLNIAEFHV
     AMGLIYRRLN GNPIPDVLPP ELVPPSARDL DSSVDFLKDV LKHESRSKSP SSIDSPVSRL
     KSRSFNSSGN SLEGRDATIY KHNDTEPPGG FYKPRSRHVD RDAIRRTDDD SPSSDLTDMK
     RQLANTAHML DRESEAHAAR TREDEELDQE MADLKYRVKR VQEDLDYNSR GPRTAAKEDE
     RRKLERELLS LMHERIPEVE RKLKAREERK ERERREWARN RDRANERFGR FDAKEDSYSR
     RYDDRDRDYD RPSSRNYDRD RERDRDWDRE RDRDRSYRRS RSRSRSRDRR DRSRDRDYDT
     RSPPPRSGAS PAPPSLRPDS AASRATPKPV RSPAPDLKNM TPEERRAHAQ RLIQERRIAL
     GLDVAPSPTP VDTSIEDRLQ QEKKEAEEKA KAAEKEREER ERARKERLER EKAAKEEATA
     PPTVAVTPPA PTTAPAPPAP TPKAAPPPPK ARGAPPPPPT RSRAPAPPPP TRAAAAPAPP
     AHKEPEVDPE EEFRAREAEL KRQREERFRQ RMKELEEEEE RLAKEEEERI KARIEALKQR
     QAAKPPSPPP APAAPEAPPA PPAPPAPPAP APPAAAAVSA PVSAVSPPVE KSTNPFSKFM
     KEQGGAAAAA TSSPPAPPAT TSTTNPWARP QTAPPPSRSP APPAPKGSYH IAPSSNTDDD
     WDDIKEKDDS DDSSDEDEID KSRAARANIA QQLFGSMLPR PQSAAPASTG GRSATASPAP
     LSAPPTAPPA PPAPAPPAPP APAAPAAPPP PAAPRAPAPA SGPGDVGALM ASIQGGLRLR
     PTKTVDKSRP AVTGKIIGDA APPEHINNAP RPASPPTPRQ EYTSPAPIPE APAVNDESSS
     SQPSHNRGQS VDWMSNRAAA DAGIAPVPQL PSMAEAEEDD YEHVEVPTEA PIPAIQVDEP
     ADPSSELMND IDKSIEHRVR SLYAYEGDGP EDLSFAENVI LTAHPSKTGG DWWYGKTVKD
     GKSGLFPKTY VEVVRPFKAK ALYDYAPENP DELPLSEGQL VSVVDNSEEE WWKAEKDGVV
     LVVPAAYLEL VEEPTELPPT TPSRMTLSIA TESQSSTSVD HSFSPRKGEE SLNAPENAAK
     QEAPDDSQTS SVGDSTDVDA ETGSSDSEYL SFEESDDDDN DAQLEDTEEE RMARERERQM
     VLEAAGLIVK TIDGVKPPPT KLTRTRSKAH RRPVSPSTTS SPPKRRAPPE APVRRKPRPK
     RLLSTDKELP PIPIEIEEEQ ESAKPMDPVV QLDDAYARYE SFKNQQMESL NINRLSVIST
     DSGSLRSLSP TVASFTLVQP PSPGATSSTF SLGSKENATP HKESEPQQDK YRSHFRHYFS
     RSRTPESTET TPSSIRKLQI SGPMPLGSVT PASKSAGASP RNSVHGGAAL PGSPKSLQFQ
     SISVVRPGTS GDHLTVGQPL SAASTVTPGV DSPSRAASPT FGTSWASLVD KTALEGIPSN
     ERKRQEAIFE LINTEVAYVR DLQLIVEASV FYSSMLDILS HKEITVVFAN VEDILLTNTA
     FLSSLEERQK ECRLYIDRIG DILVNHFPNM GVYLEYCVNQ QQANKVLQSL IQSKPALVEH
     LNKLKENPAT RNLDLSSYLL EPMQRITRYP LLIKQIAHYT SASESAEISE QKAIAEAKEL
     SEKLLDSINE TIRDQEGKET LKKLSEGGLW IGQGRLDLTA PTRYMGARKL LKQGVVAKAK
     SGRKLKAFLC SDILVLTDQS GRNLYRMPIP LAHAEVKEIT GTLRDDTGFQ ILQPYPRGGE
     SINLKAASPK ECKEWIKQIE LASRRCRHAE ERAIRKGYHS TPRR
//
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