ID A0A452IBC4_9SAUR Unreviewed; 804 AA.
AC A0A452IBC4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Polycystin-2 {ECO:0000256|ARBA:ARBA00040113};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000025036.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000025036.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452IBC4; -.
DR Ensembl; ENSGAGT00000028503.1; ENSGAGP00000025036.1; ENSGAGG00000018277.1.
DR Proteomes; UP000291020; 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:UP000291020};
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 59..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 495..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 586..621
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 600..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 599
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 601
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 603
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 605
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT DISULFID 166..179
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ SEQUENCE 804 AA; 92423 MW; D4DB19AD1CB9D484 CRC64;
STAKRQCWQC TNAGSYTPHG GSFSAATTQA TLKHCLWGTR LMEENTSRER YLKSVLRELI
TYVIFLVVLC VLTYGMVSSS MYYYTRVMSQ LFLETPLSNM EKTNFKTLST MEDFWKFTEG
PLLDGLYWEM WYNNKTMAEN KSFIYYENLL LGVPRVRQLK VRNGSCSIPE DLKDEIKECY
DVYSVANEDT APFGLQNGTA WTYTNEQDLN GSSHWGLIAS YSGAGYYQDL SRSREETAAQ
IANLKKHLWL DRGTRAAFID FSVYNANINL FCIVRLLVEF PATGGLITSW QFQPVKLIHY
ISTFDFFLAA CEVAFCLFTL YYVIEEILEI HIHKLHYFRS LWNCLDILII VLSIAAIGIN
IYRRSTVDML LKKQLEDQNA FPNFEPLAYW QIQFNNIAAV TVFFVWIKLF KFVSFNRTMN
QLSTTMSRCA KDVIGFAIMF FIIFLAYAQL AYLVFGTQVD DFSTFQECVF TQFRIILGDF
NFTEVEEANR VLGPIYFTTF VFFMFFILLN MFLAIINDTY SEVKSDMAQQ KAEMELSDLI
KKGYNKAMIK LKLKKTTVDD ISENLRQGGG KLNFDELRQD LKGKGHTDAE IEAIFTKYDQ
DGDQELTEHE HQQMRDDLEK EREDLDLDSS LPRPMSGRSF PRSLDDSEED DDEDSGHSSR
RRGSSSSGVS YEEFQVLVRR VDRMEHSIGS IVSKIDAVIV KLEAMERAKL KRRDVLGRLL
DGVTEDERLG RDNEIHREQM ERLVREELER WESDDTASQM SHRLGTPLGL NSQPRSRSSR
PSSSQSTEGI DGSGGGNGGS NIHV
//
