PKDRE_MOUSE
ID PKDRE_MOUSE Reviewed; 2126 AA.
AC Q9Z0T6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Polycystin family receptor for egg jelly {ECO:0000312|MGI:MGI:1338786};
DE AltName: Full=PKD and REJ homolog;
DE AltName: Full=Polycystic kidney disease and receptor for egg jelly-related protein;
DE Flags: Precursor;
GN Name=Pkdrej;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9949214; DOI=10.1093/hmg/8.3.543;
RA Hughes J., Ward C.J., Aspinwall R., Butler R., Harris P.C.;
RT "Identification of a human homologue of the sea urchin receptor for egg
RT jelly: a polycystic kidney disease-like protein.";
RL Hum. Mol. Genet. 8:543-549(1999).
CC -!- FUNCTION: May have a central role in fertilization. May generate a
CC Ca(2+) transporting channel directly involved in initiating the
CC acrosome reaction of the sperm.
CC -!- SUBUNIT: May form homomultimers or heteromultimers in combination with
CC an as yet unidentified subunits.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at about 2 weeks and continues
CC into adult life, mirroring the production of mature spermatozoa.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
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 EMBL; AF116459; AAD18022.1; -; Genomic_DNA.
DR CCDS; CCDS27723.1; -.
DR AlphaFoldDB; Q9Z0T6; -.
DR STRING; 10090.ENSMUSP00000086352; -.
DR GlyGen; Q9Z0T6; 18 sites.
DR iPTMnet; Q9Z0T6; -.
DR PhosphoSitePlus; Q9Z0T6; -.
DR PaxDb; Q9Z0T6; -.
DR PRIDE; Q9Z0T6; -.
DR ProteomicsDB; 289439; -.
DR MGI; MGI:1338786; Pkdrej.
DR eggNOG; KOG3599; Eukaryota.
DR InParanoid; Q9Z0T6; -.
DR PhylomeDB; Q9Z0T6; -.
DR ChiTaRS; Pkdrej; mouse.
DR PRO; PR:Q9Z0T6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z0T6; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0097524; C:sperm plasma membrane; IDA:MGI.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR GO; GO:0060046; P:regulation of acrosome reaction; IMP:MGI.
DR CDD; cd01752; PLAT_polycystin; 1.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR042060; PLAT_polycystin1.
DR InterPro; IPR014010; REJ_dom.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF02010; REJ; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS51111; REJ; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..2126
FT /note="Polycystin family receptor for egg jelly"
FT /id="PRO_0000024300"
FT TOPO_DOM 19..1068
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1069..1089
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1090..1273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1274..1294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1295..1311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1312..1332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1333..1449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1450..1470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1471..1483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1484..1504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1505..1580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1581..1601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1602..1838
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1839..1859
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1860..1875
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1876..1896
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1897..1918
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1919..1939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1940..1964
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1965..1985
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1986..2019
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2020..2040
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2041..2126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 102..797
FT /note="REJ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00511"
FT DOMAIN 1114..1231
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 20..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 888
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1063
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2126 AA; 241390 MW; A0CEDAA0D8219A84 CRC64;
MWPGPALLLL GLGLGLGSQP PPTGPRGLPG VLRGAPGLGQ GAESSVRGGD TGGLSPRAAP
RHASPTPPRR CPSGAAARVL LKVNSSDPAA AKANVSCQTA PCIMQPVKIN RKDQNAPLIL
SRDEEATLNI TVRWYCPDAL VIRKSWVYFS VASVNDTPDW NRPVLLPQVA VSKGFSLHIP
KYALPYGVYV FNFTLSIFRW DLAWPTVTGS DIIYIWVRKR PLKAVLLGAP RVTVKFSDEL
ILNGSMSYDP EADIPTWGLQ FFWYCTTNPR YYSGNYVLVI NQAVCHPEQD SLNWPWAVGS
VLTIPPKTLR GNGVYYFRMV VQKQNRTAFS DKTVHVLQGL QPKAHISCIE NCGPTLGVSD
RFSLFLNCPS CGRQDLYSWS ILSLTGHEVM FDWAGQAITR RNGPYLSIKA FAFRNFLENR
VWVSLILKSW SGMTTTLRHP VVINHGPRVG KCKINPASGI SMVTKFAVEC SDFKDENLPL
KYKIIVSELD SIGAISSVEE NTLGSVVYSG AEPITPAFFL PVGTVTDEYN VRLYVQVYDS
LGTFSQVTLQ ATVTAPTVRD SSKDVLQQLL NVTMKPTSLL STLLQKQDWL QAGYLTYVVI
SVLNNIKGEQ ELQDDRARLL EHLVKQSLTF AMNTADEIGQ SVMVITKLTQ KASDLSQADL
EATSFRLRQA SQDLQEYQHR HKHLQQVEVV GTGILTSLSN LLKLINPYYT LQDPLFVVES
LSDTILANKV PGSKTTALRT SYFNMYVEKV ENWNVFKAFR NDSLCPNCLR ATLNASTVPR
LPAKAPISMM FCEFADDPFP WLTYPENISV DVVGFRMTGV ADNNKVIEIT PDIAEVYLVR
KDLTPSSFNL TVGPGIKSDG FSKVTTGGIS FEVDSRWTGE LLIHIVTNVT VLFEALVYEG
CQLTPTNLMA TFLVPNDIPP IVKWSGLFDP TCSVKEARVV CLSSSLLRSI AQRRFSFKYN
ISMVLQASRF VLKPTNKLVR IALFMVHCLD MYGIQSDWQQ STCVLGEKTT WKTVHCVCRN
GRRSRRQLTS VKLTYHHLHT HFVTAKVIVV PNPVDLRLAI ISNLTQNPAT FLAVLFIMIL
YAILAFWALH RDVIDLYFRD NVVILTDNDP FDTLCYLVTI FTGSRWGSGT RANVFIQLMG
TEGTSDVHCL SHPYFKTLYR GSINTFLLTT KNDLGDIHSI RVWHDNSGEA PSWYLSRIKV
ENLFNKRIWL FVCRRWLSVD TTLDATFSVT NPDEPLKRTD FFMIDVRDKL RKNHMWISIF
TEIVPKPFNR LQRLSCCLAM LLSSLVCNIM FFNLNQKEKI ESRHMHIIRS MLIGIESVVI
TIPVQLLITF FFTYSQKNLK MNLDKVAPQK HPLMSEEGLS WKERLHKWHE YEMKALPRRA
AVSTSAPEEK EAFETSQKHE KADTQMSNKN SSNNNQEASE GVPPKAFSSQ PHTTESVQKK
TQIILPRWCV YIAWFLVFAT SGISSFFIVF YGVTYGYAKS IEWLFASFCS FCQSVFLVQP
CNILLRSGTR SYKPKYCKNL SWSSKYHYSE IRLQGLTMTQ EEMEQLHEDI AYVRSLSMYQ
PITEDKIQIL RRENRIRRRS FLFLSYLVTH FIFLTLLLLL IFSLRHNDSF YYNQFIRHRF
SVDLATVMKL GDIYTWLHGV FLPLLHNDPN PTFLPDSSSK ILGLPLVRQV RARPSNKTCL
LAKKFVQSSV AGEIHCHPQY GIDPEDTQHY SSVWSKAGKQ STDKASHGFT YKPPGKRWVY
HSYGVLNTYG SGGYVFYFFP GQQMFNSTVR LKELEGKNWL DELTWAVIVE LTTLNPDTSL
MCSISVVFEV SPLGVVNSSL SVYSFSLADF NRKTSSEIYL YAAILIFFCA YVVDEGYIIR
QERASYIRSV YNLLNFSLKC MFALLIVLFF WKYFLATKMV QLYLADPEAF IPFHAVSRVD
HFMRIILAFL LFLTILKTLR YSRFFYNVRL AQKAIQAALP GICHTALVVS IYSFMYVAFG
YLVFGQHEWN YSNMIHATQT IFSYCVSAFQ NTEFSGNKVL GVLFLSSFML VMICIFINLF
QAVILSAYDE MKQPVYEEPS DEAEAVTYLC NRLKSGFDFL TTRSRDKDQS NFFVDMLYGQ
PEKNTRRFLG LKARNINGKK MIYLVV
