ID K7F2Y5_PELSI Unreviewed; 770 AA.
AC K7F2Y5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Polycystin-2 {ECO:0000256|ARBA:ARBA00040113};
GN Name=PKD2 {ECO:0000313|Ensembl:ENSPSIP00000002395.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000002395.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000002395.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC projection, cilium membrane {ECO:0000256|ARBA:ARBA00004272}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004272}. Cytoplasmic vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004156}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the polycystin family.
CC {ECO:0000256|ARBA:ARBA00007200}.
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DR EMBL; AGCU01138485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01138486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01138487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01138488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01138489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01138490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7F2Y5; -.
DR Ensembl; ENSPSIT00000002403.1; ENSPSIP00000002395.1; ENSPSIG00000002360.1.
DR GeneTree; ENSGT00940000159025; -.
DR HOGENOM; CLU_012097_0_0_1; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR InterPro; IPR046791; Polycystin_dom.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10877; POLYCYSTIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10877:SF114; POLYCYSTIN-2; 1.
DR Pfam; PF18109; Fer4_24; 1.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF20519; Polycystin_dom; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR603915-1};
KW Calcium channel {ECO:0000256|PIRSR:PIRSR603915-1};
KW Calcium transport {ECO:0000256|PIRSR:PIRSR603915-1};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|PIRSR:PIRSR603915-
KW 1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRSR:PIRSR603915-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603915-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT TRANSMEM 24..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 551..586
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 565..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 564
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 566
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 568
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 570
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 575
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT DISULFID 131..144
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ SEQUENCE 770 AA; 89084 MW; 5C832354BEEC945F CRC64;
LWGTRLMEEN TSRERYLKSV LRELITYVIF VVVLCVLTYG MVSSSMYYYT RVMSQLFLET
PLSKMEKTNF KTLSTMEDFW KFTEGPLLDG LYWEMWYNNK TTTENRSFIY YENLLLGVPR
IRQLKVKNGS CSIPEDLKDE IKECYDVYSV ANEDTDPFGL QNGTAWIYTS EQDLNGSSHW
GLIASYSGAG YYQDLSRSRE ATAAQIANLK KHLWLDRGTR ATFIDFSVYN ANINLFCIVR
LLVEFPATGG LISSWQFQPV KLTHYISTFD FFLAACEMAF CLFMLYYIVE EILEIHIHKL
HYFRSLWNCL DILIIMLSVA AIGINIYRRS TVDRLLKKQL EDQNTFPNFE PLAYWQIQFN
NISAVTVFFV WIKLFKFVSF NRTMSQLSTT MSRCAKDVIG FAIMFFIIFL AYAQLAYLVF
GTQIDNFSTF QDCVFTQFRI ILGDFNFTEV EEANRVFGPI YFTTFVFFMF FILLNMFLAI
INDTYSEVKS DMAQQKAEME LSDLIKKGYS KAMIKLKLKK ATVDDISENL RQGGGKLNFD
ELRQDLKGKG HTDAEIEAIF TKYDQDGDQE LTEHEHQQMR DDLEKEREDL DLDRSVLPRP
MSGRSFPRSL DDSEEDDDED SGHSSRRRGS SSSGVSYEEF QVLVRRVDRM EHSIGSIVSK
IDAVIVKLEA MERAKLKRRD VLGRLLDGVT EDERLGRDNE IHREQMEQLV REELERWESD
DTVSRMSHCL GTPVGLNSQP RSRNSRPSSS QSTEGIDRSG GGNGGSNIHV
//
