ID A0A1S3F8Z2_DIPOR Unreviewed; 765 AA.
AC A0A1S3F8Z2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Polycystic kidney disease 2-like 1 protein {ECO:0000313|RefSeq:XP_012873128.1};
GN Name=Pkd2l1 {ECO:0000313|RefSeq:XP_012873128.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012873128.1};
RN [1] {ECO:0000313|RefSeq:XP_012873128.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012873128.1};
RG RefSeq;
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}. 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 RefSeq; XP_012873128.1; XM_013017674.1.
DR AlphaFoldDB; A0A1S3F8Z2; -.
DR STRING; 10020.ENSDORP00000005825; -.
DR GeneID; 105986653; -.
DR KEGG; dord:105986653; -.
DR CTD; 9033; -.
DR InParanoid; A0A1S3F8Z2; -.
DR OrthoDB; 56358at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR InterPro; IPR046791; Polycystin_dom.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10877:SF194; POLYCYSTIC KIDNEY DISEASE 2-LIKE 1 PROTEIN; 1.
DR PANTHER; PTHR10877; POLYCYSTIN FAMILY MEMBER; 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.
PE 3: Inferred from homology;
KW Calcium {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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|PIRSR:PIRSR603915-1};
KW Ion transport {ECO:0000256|PIRSR:PIRSR603915-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603915-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
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|PIRSR:PIRSR603915-1}.
FT TRANSMEM 106..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 150..344
FT /note="Polycystin"
FT /evidence="ECO:0000259|Pfam:PF20519"
FT DOMAIN 345..569
FT /note="Polycystin cation channel PKD1/PKD2"
FT /evidence="ECO:0000259|Pfam:PF08016"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 657..684
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 659
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT DISULFID 212..225
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ SEQUENCE 765 AA; 87604 MW; 63B6811E3155177A CRC64;
MKSMGGPEGQ ELHKLDKGAW DNPAYSSSPS PHGTPRIYTV SSVASPSNEP LPKKPEDGVQ
EKTHSTLGSS CCLHICHCIR GLWGTTLTEN TAENRELYVK TTLRELLVYI VFLVDICLLT
YGMTSSSAYY YTKVMSELFL HTPSETGVSF QTISSMADFW DFAQGPLLDS LYWTKWYNNQ
SLGHGSHSFI YYENLLLGAP RLRQLRVRND SCVVHEDFRE DIFSCYDVYS PDKEEQLPFG
SVNGTAWTYH SQDELEGSSH WGRLTSYSGG GYYLDLPGSR QASAEALRDL QEGLWLDRGT
RVVFIDFSVY NANINLFCVL RLVVEFPATG GAIPSWQIRT VKLIRYVSNW DFFIIGCEII
FCIFIFYYVV EEVLEIHMHR LGYLSSIWNI LDLVVILLSM LAVGFHIFRT LEVNRLMGKL
LEQPNTYADF EFLAFWQTQY NNMNAVNLFF AWIKIFKYIS FNKTMTQLSS TLARCAKDIL
GFAIMFFIVF FAYAQLGYLL FGTQVENFST FTKCIFTQFR IILGDFDYNA INNANRILGP
VYFVTYVFFV FFVLLNMFLA IINDTYSEVK EELAGQKDEL QLYDLLKQGY KKTLLRLRLK
KEQVSDVQKV LQGGKQEIQF EDFTNTLREL GHEEHEITEL TAAFTRFDQD GNHILDEKEQ
EQMRQDLEEE RVALNAEIEN LGRSIVHSPA GELGTEAATS EGWVSGEEFY TLTRRVLQLE
TALEGVISQI DAVDSKLKML ERKGQPASSP GEQEEQRFGN TCIQL
//
