ID A0A397T863_9GLOM Unreviewed; 2160 AA.
AC A0A397T863;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=C1645_873702 {ECO:0000313|EMBL:RIA94062.1};
OS Glomus cerebriforme.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA94062.1, ECO:0000313|Proteomes:UP000265703};
RN [1] {ECO:0000313|EMBL:RIA94062.1, ECO:0000313|Proteomes:UP000265703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA94062.1,
RC ECO:0000313|Proteomes:UP000265703};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RIA94062.1}.
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DR EMBL; QKYT01000091; RIA94062.1; -; Genomic_DNA.
DR STRING; 658196.A0A397T863; -.
DR Proteomes; UP000265703; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
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; cd00030; C2; 1.
DR CDD; cd00052; EH; 2.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
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; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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:SF5; DH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46006; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR AT 64C, ISOFORM A; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF06346; Drf_FH1; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF16652; PH_13; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF02205; WH2; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00246; WH2; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS51082; WH2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Reference proteome {ECO:0000313|Proteomes:UP000265703};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 46..127
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 242..331
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 275..310
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1214..1231
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT DOMAIN 1373..1438
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1440..1499
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1698..1880
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1919..2014
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2019..2134
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1647..1681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 472..518
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 638..672
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2160 AA; 241934 MW; DDD8DACE901A3F6A CRC64;
MYQNLQITYG QSPSSQPQVV AGATSGGEGG GPNIPNVRLS FITASDQTTF EKLYIQGCAG
GKYLTGEGAK EILVKSKLNG DTLAQIWKLS NLSKNNYLTF PEFALAMYLT NLKLKKQDLP
TTLSDNISNE VMGVIEQIKA IEQEHQKQQQ KQQLQTSQIQ RTISPSHPQM MSHPQQQYTG
MPMSHNMGQY SLNQSGIQGS PIMPNMMPFT QRMLPQQNPP EQYSTTGIVG NAKIPWAVTP
EEKIQYREIF KQWDSQGFGY LTGDKAREIL SQSGLPQSDL MQIWNLSDPN NNGKLNQDEF
AVAMHLIYRK LNGYDIPTTL PPELVPPSSR ELSESVNMIK NLLKSEAHNH SIGLGTHTSG
ANYAKSRSFT ATPTIKRNDA TVYKHKDDDN VYVSSSRHRV PTVSRSQNTS SYSSLSRSSS
VSENIGEDRS SKISELKKQI HEKQIMLEAL SYTAETAPTS YGSSYSSDYS DVNEWKNKIK
DIQGDINEKE RSNPEWLNRE FTRNLEELNS LLEQHKDLDY ELNNMLVMIV PDLISRVREM
DSKIPDAKLE LFKLKEGSGG GSDLNIIGTG PGGTITESDR IRAKAQAMIQ ARMAEITGKP
VSLGGGGSNS RLLEEETDRI NSEKAEREYK VVEIERSISK LQDSMIRISR EREEIENKYS
KVERNKRDRE SENQKWEDGI GVGDEVRRFI QDLKRDSSTS SRYDYNDSYS SSRSVPYNRS
PSTSSTSSSV YTSVSNTTAS SLSNSKSPEE RDAFIKAEAQ RRIQERFNAL GVKKTSYSKS
TPSSAPDSPT LSDRLAREKT ELAEKKARAE REAEERERIR SEKLLAEKQR KAELDAEKLR
KMEEFERREE ERRNQWLAEA KELEKAKDRK AREKEEAARE RELELERKRV EAAEREKKLE
EERLARIKRE AEERAAEEER RRIEQEALIE NSKAAREKAK KMEEEAKQRE EAAKREAERI
KTKREDSTFS VKSSDSGPQT PSSIDSSRNN PFLNLSSQEK KQIDSNEDDS IKSTNPFFKF
TSGSTVQSNA PSSPNDKHDD DDWNVVNNEE SSDDDFPPGN TRQLASKLFG SSSFEPPNFE
SLKTSPPQSS SVFTFSSPIS KVPTSNVTTT SDSIPPPPPL PNNSNDVPPP PPLPNSNDVP
PSPPLPNSND VPPPPPLPNS NDVPPPPPLP SFNDVPPPPP LPSFNDVPPP PPQPQQPLSS
GNQSKSSLPP PSNSRNALLS QIQQGAKLKP TKTNDRSSPS VGGKAHDSNS SAQSSSGGVP
QPATGMGGLS GLGALFAGGV PKLKSRGGIE TGSSATENST SKSSPPTRQK TMGRRVSADW
FGNLSSDQLA GEETPKPQST TKTETPVNEG NPILEQEVTS PTSISADNDI DYSQEFRVKS
LYNYPGSGGA DELTFDAGIV FVAHPSKNPK NVEWWHGLIE ETGSKGWFPK NFVEIYKEEK
EICKAKALYD YKPQNSTELE IKAGNIVSIL DKSLNDWWKA EFEGSKGFVP ANYVEEITSS
SDLNKTSTDE SNESDEENSS GDETNEDISS QDESSKDESF SKNHYVNSKT KIINSSMQED
LDSSSKKTNT KILPIDIPKL NIQSVNSPTK NTFKKEPLRV DVNGLFPAKL TRKSSLEVAR
SPSPTRLFGG SPIMSIPWMQ LGDHTHKNHN NSLLGVSPPN HPSRPESPVS PGYGPSSITW
TSIMDPETIK DLSKEERKRQ EAIYELITTE QSYLRDLQMI VEVFYGPLQN ILSTADLNII
FSNVEDILLC NTAILSDLEQ RQKDDKLFVN NIGDLLLNHS DDLKCYEIYC GGQLNSSKFL
QKKRNEDKLF AEFLKKAQQD PKCGSLDLSS FLLKPMQRIT RYPLLIRQIL HYTGKDHSDQ
EDLMRALHKA EAILESTNEA AREQENKLKL ADISTLVDLE DLEEKLDLTS TTRSVGKRQF
ILEGSLKKSK SGRNLYGYLF NDLLLLAQHN KKSVAKGYKY ALYKPPILLN EIVVKDTGQD
ETFQIVHIED VINLKASNIS VKQQWVNQLE TANGYCLEVE RQKQKKENLT PTNSIGTLKV
TVYEAVIPME AHEKIPVNTY CQVQLNRQVF KTKVVKDDIF PRWNQYLMFS VTTLEDTLKL
SVYQYDKYTQ DEYLGKAEIK LHFLEHYGGN ETDKIPLELK DVAPGRPFGS ISVYLNYKPF
//
