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
//