ID A0A2S4L4P1_9HYPO Unreviewed; 1232 AA.
AC A0A2S4L4P1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Calcium-binding protein {ECO:0000313|EMBL:POR37405.1};
GN ORFNames=TPAR_02407 {ECO:0000313|EMBL:POR37405.1};
OS Tolypocladium paradoxum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=94208 {ECO:0000313|EMBL:POR37405.1, ECO:0000313|Proteomes:UP000237481};
RN [1] {ECO:0000313|EMBL:POR37405.1, ECO:0000313|Proteomes:UP000237481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR37405.1,
RC ECO:0000313|Proteomes:UP000237481};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00025194}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000256|ARBA:ARBA00011159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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:POR37405.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PKSG01000252; POR37405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4L4P1; -.
DR STRING; 94208.A0A2S4L4P1; -.
DR OrthoDB; 12127at2759; -.
DR Proteomes; UP000237481; 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 Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
DR PANTHER; PTHR11216:SF161; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE CLONE 15, ISOFORM A; 1.
DR Pfam; PF12763; EF-hand_4; 3.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00027; EH; 3.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF47473; EF-hand; 3.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 3.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Reference proteome {ECO:0000313|Proteomes:UP000237481}.
FT DOMAIN 20..96
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 146..236
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 292..327
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 293..383
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 1191..1231
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 236..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 521..597
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 633..660
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 237..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1232 AA; 128904 MW; 8655BE26E0C793D2 CRC64;
MPADTGADSA APNLNLTPDE KRVYGDLFKQ ADPENLRVVT GDAALSFFDK TRLDSRVLGE
IWQIADKENR GFLTPAGFGI VLRLIGHAQA GREPRPELAF QPGPLPRFDG IQLATSTASP
VPPVPTAIQP QGTGGAIRIP PLAPDKVAQY TGLFERQPLQ GNMLAGEQAR QIFDKSGLPN
ETLGRIWALA DTEQRGALVL PEFVIAMHLL TSMKTGALRA LPTVLPAGLY EAVTQRGSIS
GPRQSPSNTG MSAIPRQMSG SAQPRTGSPL GRPLGPQTTG AAGAGDWAVT AADKERFDQI
YATLDKTKKG YITGDEAVPF FSQSNLSEDA LAQIWDLADF DSQGHLTPEG FAVAMFLIRQ
QRSRSTALPS TLPTNLIPPS MRNQVRPATS TSAFDPPPMT QPPPPQPKSA LEDLFGLDSS
TPSPALAAAP TQTTMSTGGS NANDPFSGGS YALSPSSPAQ ASAPGSTFKP FVPSSSFGRG
LNVQPSGDAA GTASMQPHSE DLLEDHDPEA SKNITGETTE LANLSNQIGS LSKQMQDVQN
KRTITQNELN QTNSQKQNFE QRLAQLRTLY EKEAENTRAL EEQLRKSRSE TQKLQSECMT
LDGTYRDVQT QHQQVLASLQ ADQQENGSLR ERIRVVNGEI AQLKTQIEKL KSEARQQKGL
VAINKKQLAT TEGDRDKLKT EAEGLARGGE DVSRQVDSSS PVSMSAQVAS PAQSTASGNN
PFFKRTASTD IMGAFASPPA RAVPDKSFDD VFGPSFPTGS TSTPPPPAAF KQQHTGNSAA
SAGSYNTASS TPNVSRQGTL SAEPPAPPES RQISSSFLPF PDQTESLSSS RQVSPPASRA
EGSITGSSNS FPGETASTGG SATGGPGAST SEDDEKSETP SATPVPGDAQ GANAGETASK
GPQAESGAAG GSAPFGSNDQ AKAKADFDNA FAAFTSNKSQ SPGAPEGVKS QSAFATEFPP
ISELERDDDS ESDSERGGFE DDFAPASPHS KAGVKQSSGP GATAESKNAE KPSSPATITN
SNSNLAAPKS STIADDIFGS AAPPAAASGP GQANLAAKGA FDDLDDDFEG LEDAKEGSAD
DDFANISRDD FNPVFDSSPP ASQTKSESTA FGNESSFDFV SSNSATGAPA AAGGSQQKAA
DSHDWDAIFA GLDSPSTVTP PGLNNLSTAN NHENKDSRPP PPGRALTEQG VHDDPILKNL
TGMGYSRSDA VAALEKYDYN LERAANYLAS QS
//
