ID A0A091LSU0_9GRUI Unreviewed; 771 AA.
AC A0A091LSU0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Polycystin-2 {ECO:0000256|ARBA:ARBA00040113};
DE Flags: Fragment;
GN ORFNames=N324_06787 {ECO:0000313|EMBL:KFP45851.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP45851.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP45851.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP45851.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK764157; KFP45851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LSU0; -.
DR Proteomes; UP000053330; 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:UP000053330};
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 27..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 554..589
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 568..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 567
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 569
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 571
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 573
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 578
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT DISULFID 134..147
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP45851.1"
FT NON_TER 771
FT /evidence="ECO:0000313|EMBL:KFP45851.1"
SQ SEQUENCE 771 AA; 89011 MW; CED95F85C3F09864 CRC64;
QGLWGTRLME ESNTSRERYL KSVLRELVTY VIFLVVLCVL TYGTVSSSMY YYTRVMSQLF
LETPVSKMEK TDFKTLSTMD DFWKFTEGPL LDGLYWEMWY NNKTMAENKS FIYYENLLLG
VPRIRQLKVR NGSCSIPEDL KDEIKDCYDV YSVANEDTTP FGLRNGTAWT YTNEKDLNGS
SHWGLIATYS GAGYYQDLSR TREVTAVQIA SLKKNLWLDR GTRAAFIDFS VYNANINLFC
VVRLLVEFPA TGGLVTSWQF QPVRLIHYIS TFDFFLAACE VAFCLFVLYY TVEEILEIHI
HRLRYFRSLW NCLDILIIVL SMVAIGISIY RTSTVDTLLK KLLEDQNSFP NFEPLAYWQM
QFNNIAAVTV FFVWIKLFKF VNFNRTMSQL STTMSRCVKD IVGFAIMFFI IFLAYAQLAY
LVFGTQIDDF STFQDCIFTQ FRIILGDFNF TEVEEANRIL GPIYFTTFVF FMFFILLNMF
LAIINDTYSE VKSDMAQQKA EMELSDLIRK GYNKAMIKLK LKKTTVDDIS ESLRQGGGKL
NFDELRQDLK GKGHTDAEIE AIFTKYDQDG DQELTEHEHQ QMRDDLEKER EDLDLDRSSL
PRPLSSRSFP RSLDDSEEDE DEDSGHSSRR RGSSSSGVSY EEFQVLMRRV DRMEHSIGSI
VSKIDAVIVK LEAMERAKLK RRDVLGRLLD GVTEDERLGR DNEIHREQME RLVREELERW
ESDDAASQMS HRLGTPLGLN GQPRSRSSRP SSSQSDGIDG GGGNGGNNIH V
//
