ID M4A6D1_XIPMA Unreviewed; 893 AA.
AC M4A6D1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Polycystin-2 {ECO:0000256|ARBA:ARBA00040113};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000010025.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000010025.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000010025.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005797652.1; XM_005797595.2.
DR AlphaFoldDB; M4A6D1; -.
DR STRING; 8083.ENSXMAP00000010025; -.
DR Ensembl; ENSXMAT00000010039.2; ENSXMAP00000010025.1; ENSXMAG00000009982.2.
DR GeneID; 102220672; -.
DR KEGG; xma:102220672; -.
DR CTD; 5311; -.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00940000159025; -.
DR HOGENOM; CLU_012097_0_0_1; -.
DR InParanoid; M4A6D1; -.
DR OMA; RHEHRSC; -.
DR OrthoDB; 56358at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
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:0003171; P:atrioventricular valve development; IEA:Ensembl.
DR GO; GO:0097704; P:cellular response to oscillatory fluid shear stress; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR GO; GO:0003146; P:heart jogging; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0070121; P:Kupffer's vesicle development; IEA:Ensembl.
DR GO; GO:0001946; P:lymphangiogenesis; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0051284; P:positive regulation of sequestering of calcium ion; IEA:Ensembl.
DR GO; GO:0072114; P:pronephros morphogenesis; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0072019; P:proximal convoluted tubule development; IEA:Ensembl.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IEA:Ensembl.
DR GO; GO:0032965; P:regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0003173; P:ventriculo bulbo valve development; IEA:Ensembl.
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:UP000002852};
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 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 688..723
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 701
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 703
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 705
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 707
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT BINDING 712
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-1"
FT DISULFID 268..281
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ SEQUENCE 893 AA; 101659 MW; 36C3E92D4A8F5168 CRC64;
MSSSRVRPQS QSGRSAQGPD SSEGIEMENI QHQDLGLGGV IGTPSPQSRQ AWSRDNPVFE
PEEEIMEADW PQASPGRRSV STASSGSSSS YNRGGSSAQI PRGGLYPTPT PTINARQQDR
HEHRSCLKQI LQKIRILWGT ELMEDSDSSR ERYLRNVLRE MLTYVGFLIT VCVLTYGMVN
SNMYYYTKVM SQLFLDTPLS PGDQTTFRSL STMEDFWKFT QGPFLGGMYW DVWYNNNSLP
ENQSFIFYEN LLLGVPRLRQ VKVRNESCSV HEDLRDEVQD CYNIYTPSNE DTAPFGPKNG
TAWVYTTESE MNSSSHWGQV SKYGGGGYYL DLSQTKEESS NRLQFLKDHL WLDRGTRAVF
LDFSVYNGNI NLFCIGRLLV EFPATGGAVT SWHFQTVRLI RYVSSWDYFV GMCEVAFCLF
ILYYVVEEVL EVHIHRLHYF KSMWNCLDVL IVVLSIVAII MNITRTAMAR NLLSGLLENY
TAHPSFEPLA SLQVQFNNLA AVIVFFSWVK LFKFINFNKT MSQLSTTMSR CAKDLTGFAI
MFFIIFLAYA QLAYLVFGTQ VNDFSTFQAS VFTQFRIILG DFGFSEIEES NPVLGPVYFT
TFVFFIFFIL MNMFLAIIND TYSEVKADMS QQRCEMEMTD LIKKGCNKAL MKLRLKKTPV
DEISSGLQQA SSKMNFDELR QDLKGKGHTD AEIQAIFAKY DQDGDPELTE HEHQQMRDDL
EKEREDLELE RNSLTRPSSG RSFPRTQDDS EEDDDEDSGH SSRRRGSSSG GVSNEELQVL
VRRVDRMEHS IGSIVSKIDA VIVKLEGMER AKLKRKDVLG RLLDGVMEDE RLGRDTDVHR
EQTERLVREE LERWESDDLG SQVSHTPVGP RARPPSSLSV DGLDVSSNGA VHV
//
