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Database: UniProt
Entry: A0A087VJM6_BALRE
LinkDB: A0A087VJM6_BALRE
Original site: A0A087VJM6_BALRE 
ID   A0A087VJM6_BALRE        Unreviewed;       770 AA.
AC   A0A087VJM6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Polycystin-2 {ECO:0000256|ARBA:ARBA00040113};
DE   Flags: Fragment;
GN   ORFNames=N312_00842 {ECO:0000313|EMBL:KFO12818.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO12818.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO12818.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO12818.1};
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; KL495843; KFO12818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087VJM6; -.
DR   Proteomes; UP000053309; 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   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:UP000053309};
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        26..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        223..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        361..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        400..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          553..588
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          567..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         572
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT   BINDING         577
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT   DISULFID        133..146
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO12818.1"
FT   NON_TER         770
FT                   /evidence="ECO:0000313|EMBL:KFO12818.1"
SQ   SEQUENCE   770 AA;  89171 MW;  37DD55F1D86C7729 CRC64;
     GLWWTRLMEE SNTSRERYLK SVLRELVTYI IFLVVLCVLT YGTVSSSMYY YTRVMSQLFL
     ETPVSKMEKT DFKTLSTMDD FWKFTEGPLL DGLYWEMWYN NKTMAENKSF IYYENLLLGV
     PRIRQLKVRN GSCAIPEDLK DEIKDCYDVY SVANEDTAPF GLRNGTAWTY TNEKDLNGSS
     HWGLIATYSG AGYYQDLSRT REMTAVQIAS LKKNLWLDRG TRAAFIDFSV YNANINLFCV
     VRLLVEFPAT GGLVTSWQFQ PVRLIHYIST FDFFLAACEM AFCLFVLYYM VEEILEIHIH
     RLHYFRSLWN CLDILIIVLS VVAIGISIYR TSTVDMLLKK LLEDQNSFPN FEPLAYWQMQ
     FNNIAAVTVF FVWIKLFKFV NFNRTMSQLS TTMSRCVKDV IGFAIMFFII FLAYAQLAYL
     VFGTQIDDFS TFQDCIFTQF RIILGDFNFT EVEEANRILG PIYFTTFVFF MFFILLNMFL
     AIINDTYSEV KSDMAQQKAE MELSDLIRKG YNKAMIKLKL KKTTVDDISE SLRQGGGKLN
     FDELRQDLKG KGHTDAEIEA IFTKYDQDGD QELTEHEHQQ MRDDLEKERE DLDLDRSSLP
     RPLSSRSFPR SLDDSEEDED EDSGHSSRRR GSSSSGVSYE EFQVLMRRVD RMEHSIGSIV
     SKIDAVIVKL EVMERAKLKR RDMLGRLLDG VTEDERLGRD NEIHREQMER LVREELERWE
     SDDTASQMSH RLGTPLGLNG QPRSRNSRPS SSQSDGIDGG GGNGGNNIHV
//
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