PK1L1_MOUSE
ID PK1L1_MOUSE Reviewed; 2615 AA.
AC Q8R526; F6VYK1; J3QMZ2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Polycystic kidney disease protein 1-like 1;
DE AltName: Full=PC1-like 1 protein;
DE AltName: Full=Polycystin-1L1;
DE AltName: Full=Protein rikishi;
GN Name=Pkd1l1; Synonyms=Rks;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1504-2034.
RC TISSUE=Testis;
RX PubMed=11863367; DOI=10.1006/geno.2002.6719;
RA Yuasa T., Venugopal B., Weremowicz S., Morton C.C., Guo L., Zhou J.;
RT "The sequence, expression, and chromosomal localization of a novel
RT polycystic kidney disease 1-like gene, PKD1L1, in human.";
RL Genomics 79:376-386(2002).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=20080492; DOI=10.1177/0300985809353553;
RA Vogel P., Read R., Hansen G.M., Freay L.C., Zambrowicz B.P., Sands A.T.;
RT "Situs inversus in Dpcd/Poll-/-, Nme7-/-, and Pkd1l1-/- mice.";
RL Vet. Pathol. 47:120-131(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PKD2, MUTAGENESIS OF
RP ASP-411, AND TISSUE SPECIFICITY.
RX PubMed=21307093; DOI=10.1242/dev.058149;
RA Field S., Riley K.L., Grimes D.T., Hilton H., Simon M., Powles-Glover N.,
RA Siggers P., Bogani D., Greenfield A., Norris D.P.;
RT "Pkd1l1 establishes left-right asymmetry and physically interacts with
RT Pkd2.";
RL Development 138:1131-1142(2011).
RN [5]
RP FUNCTION.
RX PubMed=24336289; DOI=10.1038/nature12832;
RA DeCaen P.G., Delling M., Vien T.N., Clapham D.E.;
RT "Direct recording and molecular identification of the calcium channel of
RT primary cilia.";
RL Nature 504:315-318(2013).
CC -!- FUNCTION: Component of a ciliary calcium channel that controls calcium
CC concentration within primary cilia without affecting cytoplasmic
CC calcium concentration. Forms a heterodimer with PKD2L1 in primary cilia
CC and forms a calcium-permeant ciliary channel that regulates sonic
CC hedgehog/SHH signaling and GLI2 transcription. Does not constitute the
CC pore-forming subunit. Also involved in left/right axis specification
CC downstream of nodal flow: forms a complex with PKD2 in cilia to
CC facilitate flow detection in left/right patterning.
CC {ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:24336289}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with PKD2 proteins to form a
CC calcium channel. Interacts with PKD2L1; to form ciliary calcium
CC channel. Interacts with PKD2. {ECO:0000269|PubMed:21307093}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000269|PubMed:21307093}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21307093}.
CC -!- TISSUE SPECIFICITY: In testis, strong expression in Leydig cells, low
CC level in seminal ducts, myoid cells and tunica vaginalis. Other
CC tissues, including adrenal gland and heart myocardium, also show low
CC expression. In embryo, highly expressed in the node.
CC {ECO:0000269|PubMed:21307093}.
CC -!- DISRUPTION PHENOTYPE: Situs inversus in approximately one third of the
CC homozygous mutant mice. No other notable phenotype (such as espiratory
CC tract lesions, hydrocephalus, and male infertility) is observed.
CC {ECO:0000269|PubMed:20080492}.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
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DR EMBL; AL645571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB061684; BAB85808.1; -; mRNA.
DR AlphaFoldDB; Q8R526; -.
DR STRING; 10090.ENSMUSP00000120803; -.
DR GlyGen; Q8R526; 9 sites.
DR iPTMnet; Q8R526; -.
DR PhosphoSitePlus; Q8R526; -.
DR PaxDb; Q8R526; -.
DR PRIDE; Q8R526; -.
DR MGI; MGI:2156538; Pkd1l1.
DR eggNOG; KOG3599; Eukaryota.
DR InParanoid; Q8R526; -.
DR TreeFam; TF316484; -.
DR ChiTaRS; Pkd1l1; mouse.
DR PRO; PR:Q8R526; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R526; protein.
DR GO; GO:0034704; C:calcium channel complex; ISS:UniProtKB.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IMP:BHF-UCL.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; ISS:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR GO; GO:0003127; P:detection of nodal flow; IMP:BHF-UCL.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0070986; P:left/right axis specification; IMP:BHF-UCL.
DR GO; GO:0060972; P:left/right pattern formation; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR014010; REJ_dom.
DR Pfam; PF00801; PKD; 1.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF02010; REJ; 1.
DR SMART; SM00308; LH2; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF49299; SSF49299; 2.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS51111; REJ; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Cell projection; Cilium; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..2615
FT /note="Polycystic kidney disease protein 1-like 1"
FT /id="PRO_0000164359"
FT TOPO_DOM 1..1524
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1525..1545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1546..1732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1733..1753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1754..1772
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1773..1793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1794..1905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1906..1926
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1927..1950
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1951..1971
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1972..2057
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2058..2078
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2079..2288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2289..2309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2310..2332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2333..2353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2354..2379
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2380..2400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2401..2405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2406..2426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2427..2483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2484..2504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2505..2615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 291..373
FT /note="PKD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 375..456
FT /note="PKD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 457..1349
FT /note="REJ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00511"
FT DOMAIN 1465..1511
FT /note="GPS"
FT DOMAIN 1573..1690
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 17..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1807..1840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2589..2615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 411
FT /note="D->G: In rks; mice exhibit gross left-right
FT abnormalities. Embryos do not show defects in kidney
FT development. The nodes appear normal."
FT /evidence="ECO:0000269|PubMed:21307093"
FT CONFLICT 1680..1681
FT /note="KL -> RQ (in Ref. 2; BAB85808)"
FT /evidence="ECO:0000305"
FT CONFLICT 1699..1700
FT /note="WK -> LQ (in Ref. 2; BAB85808)"
FT /evidence="ECO:0000305"
FT CONFLICT 1789
FT /note="L -> F (in Ref. 2; BAB85808)"
FT /evidence="ECO:0000305"
FT CONFLICT 1833
FT /note="Q -> H (in Ref. 2; BAB85808)"
FT /evidence="ECO:0000305"
FT CONFLICT 1846
FT /note="N -> T (in Ref. 2; BAB85808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2615 AA; 290844 MW; EBA1538C9D3AB74C CRC64;
MDVDEDQHAV AVLHHKIQAN PELCVSDEQD SCPSDAPKGT ARDPESQKPS SPAPWDKNVL
NTGSEERLSF INGEPQAPPN WDEGTNSFSN PPPGISHTCN LSASWYHPES SSPLTQHPPR
ATLVTQPENV EHFAICCFPE TDAQALPALG IRVHVASGTA LCLLLDFGDN CGAQMRLCTL
AGATTVTGYH QYRKEGVYEL KAVVHDFHRA EELGPYYVDI SHGNVSVFMN SSSIHDSEAL
SFADSLPQQR GTVVVHCFSS ISSYNVSFIS QTQVASGQAW CGVTVGYKMQ SVSVYTNGTV
FAANTNITFV AITEETIPLE FAWYFGENPP VMTTSRSIRR RLSVPQWYRV KVKATSRIGS
VVSEPHLIRV QKRIMANRLV STASALVNAN VSFECRLNFG TDVAYLWNFG DDTIELGSSS
SSHVYSREGE FTVEVLAFNN VSSTTLRKQL FIVREPCQPP PVKNMGPAKV QIWRSQPLRL
GVTFEAAILC NISQGLSYTW SFVSAEMTTV TLPTAVNTRR QTIMLPSYTL ECGNYTAIAK
VQIKGSMVYS NYCVGVEVRA RAPVSVISEG THIFISTATS TFIILRGAQS YDPDNPGAAL
RYHWTCTAAS SPRWPCFDNS TSYQVDTQAP AISFPAKWLS ECCDQFLVTL TVSSRGQNSS
QALMFLSTRP DLAFRFVHIS WVNFRDISVN WNEEVSLRAV CEDCGDVPDL TYSWDLFLVN
ATEKSAVEVP FCSTVGLLGA LALGTSLKSS KSDLPSNLRA PLTPHSPEPS PTPLGWTALS
NLGSISAEST AGGHHVPASG AVAGSGEPME EYSSLSSLAE EALMTNSSEG SWPSPSSSTD
FDDFEAYYSD IQEAVLSLGR QPGTSTNFQE AGPSLSAEES ASYGDNLLGP FLHTGRAKPT
LMIDWPKALV SQAAFHGYTT SGIMGPAVTI KPFSLSSGKT YVLQASVASK HVLLGKAQLY
LTVNQAPQDM SCQVRPHHGM EAYTIFSVFC MSGKPDFHYE FRYRIGNTSS HTLYRGQDTQ
HYFLLPAGDS SDNYKVIVST EITDGHGSKV QPCTVAVTVL PRYHGNDCCD KELYNSTLES
LSTLRLAGSY METRNYITMI TGILSRLYVE SRNTSSCGQW SQIQDVLISS ACKVPYTDQE
GMMDSIHILR DLISFPNKLS LTSAMCIFKY TKMFLAQGQF SRRLLVDKKL RVEFVLLISG
VWEAAKEDAR DGDYLQEEGM KIISDMLLAC LSDEHQIHVS TGQMEFQTLL HRSPQSSIQN
LGFVQVHFPS DLASLHSTTQ EATQSSCYIS QLMFFMKSPY LGGQVPGQVG GVMIPRLYSC
ESRRPILRGQ LETPVTMEFG EEDYLHKRNP AMFVLLRDEV NVHRFTGLSE NSQESLQIHI
KFSKPVTRPF PIILLVRFSE KATPSDFLVK RVYFWDEQTV QMYVPAAPWK GANVGYLSLL
DADYDRKPPN KYLAGAVNYT VHFQWIQCVF WDKTEWRSEG PYPQPGSSPE KVNCSYHHLA
PVSVLRRKLN ATLEVSSISE FQSHPHNLLP GIFSAFLLVL YGILVSKSRY VDCHEKKNPG
FIFLEEDTLP GYQLYAVVID TGFRSPVRFT SKVFIVLCGE NGCSETKELC CPEKPLFGRN
SRHTFILSIP NQLGPLQKIR LWHDSSGSSP CWFISHVMVK ELCSGQAWFF SAQCWLAVSK
LGGHVLREFF CLSHGLGFWK LFYSKFTEYL EDFHIWLSLY SQPPSRSYLH TQRLAVSFCL
LCVYSCLTAL VTVRDHQQRP LDVGPTAITL EPFCMALLCT LLACPVAQLL SLLFRCSKEA
RGDMQASTQW PLRGVKTETP QGHDSSGRPD SRQPSPHPTS DLLPWNDQAW RIAASSSAVV
CSPFPMEACS HKHHDLREKS HYSPPSSQAP GSGFEELGSQ KSRVCLLWSS SVAWAISGSA
SLACGLGTGF LGYWFVPAQC MWWLYLLLLS LVCCAFITQP LMICLAALVF AWKRKHDSKF
FTESLQDATK GLDLELEEHS RTRVPLSPIS YSPDTAEEAE RVLATRQRER HLRWAQTPSK
AKLRVTGERL RRESIMQAAL RDMTTHSIML LLLLFIAYGR FCPGEISLNH AIRKAFTRKA
NHSLGDLSST EDWWDWTLST LLDELYPERT SARAWGAQPG ALGGQCHLIG PPVVKLLKIS
AGTACTPPRP FSELVEDVLP MHSNDLDLEN QNVSPGGPET CGVKKESYMH SLGKTRHEAH
AALTALRASK WIDHSTRAMS VHFTLYNPPT QLFTSVILGT ECLPSGGLVP SFLVESFRIF
YSDSALKYLL MLSELLFLVL NVIHLCFQLW GMTTKGILSY WRKPRHWLEL SMVGVAIAYY
AASGHLTTLA VNITDQFHKG LYQRLVDIGL MVSWHQRARC LQGILLFLWM LKYVHLLSSL
STMTPFSAVT CFPLFRVLLV GALLLAAHYH SRWFLLFTGT LSHGTSAEAF PGLLLQFPGR
SKKDSWHNCL KSDHGVMRCY YGTLFLLLAT LGFRMLRATF LTVFQNRKSS HRKPLVTLKD
IAVYTWHKVL TLLGLETTLE ETEVATDHIY YLDEFSSLLD ELLMKIDGLS DSLELSILEN
QWKRALESRA GDSPPVGSSE YQATGVSGPL AAESE
