ID F2ULH3_SALR5 Unreviewed; 1009 AA.
AC F2ULH3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=EF-hand domain-containing protein {ECO:0000259|PROSITE:PS50222};
GN ORFNames=PTSG_09605 {ECO:0000313|EMBL:EGD77972.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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; GL832980; EGD77972.1; -; Genomic_DNA.
DR RefSeq; XP_004990034.1; XM_004989977.1.
DR AlphaFoldDB; F2ULH3; -.
DR STRING; 946362.F2ULH3; -.
DR EnsemblProtists; EGD77972; EGD77972; PTSG_09605.
DR GeneID; 16070586; -.
DR KEGG; sre:PTSG_09605; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; F2ULH3; -.
DR OMA; LLICRIM; -.
DR OrthoDB; 5403296at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR Gene3D; 1.10.287.70; -; 2.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR46726; TWO PORE CHANNEL 3; 1.
DR PANTHER; PTHR46726:SF1; TWO PORE CHANNEL 3; 1.
DR Pfam; PF00520; Ion_trans; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 86..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 635..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 357..392
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..710
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 111532 MW; 49F79C0DBF212027 CRC64;
MPAHHDNGST ERAPLLGSDP QRHDEEHPTF AGRQHRHGRM LTSDTDDVHS FHLMLLRATV
FVEDACALRP MAHRQDTKAL NLRRWYFSRG VQAVLLLITL VNATLVFYEN PQAFFSPSTL
RRRDIVPTAI EVVSLLVLGV DAYLRYSMTG WMFYKMQPLE LVYAGATTAG LIGCVLNMAI
AAAPAWHRLL RPVYLSIRWP DMTLIATTLA WSLRDVVPHI VLLTILNAAA ALMAMIIFPS
DPNFSTFSDA LEALLVFTSG SNSPDVMLPS LNQTSLSVIF FFALSILSTV LILGIVLATI
YNRSVVYMNQ VSRHRFAQRR TAFRLAFLCL DRVSQNVASG LIDFATMRAL LKSVWHVDDR
LIGVLLSLLD KNNTGTINVH EFTYMFELML LKVERVRPTR TWVRTHLPWL YRMCDLGWLA
ATADAVLVVN LIVLAVDLTA SPPEKAVVCA PYCGVYLACA IVYLLELLIT TTALGWRRIL
RNPLALVDML LVVAIFIGQV DAFNGTSQLI PLAFARALLI CRIMRLGRML ARVALFRLMF
TSVARVLSQL PGLLGVLLAT YYIFALLGIA LFKDRLGFNP ALANSTYAEG GLQVFNFDTF
GQACISLWVV QLQLEIQDLI DACMQVTSPW SVLYFMAWLL VSYLLILNVF FAFLIDSVDV
LINRPKRKEY FRVTAAGVRK IQEDEASTHA AVRDDSDDDE DDDDDEEGDD GISSGGGRGG
RGGVDSRADG RGSSRGGGHS DVTTASPVAP WQRPQHVQAT TPERRAVLRG TAEGAEYRRS
TSQETVMATT TPIDNSDKHD AGPPWRPQIR SSAAVRQRRA ATRSEDSTDA DAPGAMHPQS
GLEEEVVEGD ALSEDEDALD VFEIEQEVDE PPPTTEPTPA AVVMMTNTGR VRTRRLARPE
RRTSTVVYGV EYRPGYDTII GADGDTSSQD NDDEQDLDLE AVARMFGWHL QDGSHHVDET
AATQGMRTTT THAPADDVDA AVAMEEAALD EHVVLLDASG TAERVLQAL
//
