GenomeNet

Database: UniProt
Entry: E7FKV8
LinkDB: E7FKV8
Original site: E7FKV8 
ID   PK1L1_ORYLA             Reviewed;        2742 AA.
AC   E7FKV8;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   10-APR-2019, entry version 33.
DE   RecName: Full=Polycystic kidney disease 1 like 1;
DE   AltName: Full=Protein abecobe;
GN   Name=pkd1l1; Synonyms=abc;
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae;
OC   Oryziinae; Oryzias.
OX   NCBI_TaxID=8090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH PDK2.
RX   PubMed=21307098; DOI=10.1242/dev.058271;
RA   Kamura K., Kobayashi D., Uehara Y., Koshida S., Iijima N., Kudo A.,
RA   Yokoyama T., Takeda H.;
RT   "Pkd1l1 complexes with Pkd2 on motile cilia and functions to establish
RT   the left-right axis.";
RL   Development 138:1121-1129(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR;
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B.,
RA   Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D.,
RA   Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A.,
RA   Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K.,
RA   Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F.,
RA   Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H.,
RA   Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome
RT   evolution.";
RL   Nature 447:714-719(2007).
CC   -!- FUNCTION: Component of a ciliary calcium channel that controls
CC       calcium concentration within cilia without affecting cytoplasmic
CC       calcium concentration. Forms a heterodimer with pkd2l1 in cilia
CC       and forms a calcium-permeant ciliary channel that regulates sonic
CC       hedgehog/SHH signaling and gli2 transcription. Does not constitute
CC       the pore-forming subunit (By similarity). Also involved in
CC       left/right axis specification downstream of nodal flow: forms a
CC       complex with pkd2 in cilia to facilitate flow detection in
CC       left/right patterning. {ECO:0000250, ECO:0000269|PubMed:21307098}.
CC   -!- SUBUNIT: Heterodimer; heterodimerizes with PKD2 proteins to form a
CC       calcium channel. Interacts with pkd2l1; to form ciliary calcium
CC       channel (By similarity). Interacts with pkd2. {ECO:0000250,
CC       ECO:0000269|PubMed:21307098}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC       {ECO:0000269|PubMed:21307098}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:21307098}.
CC   -!- TISSUE SPECIFICITY: Expressed in Kupffer's vesicle, an organ
CC       equivalent to the node. {ECO:0000269|PubMed:21307098}.
CC   -!- DISRUPTION PHENOTYPE: Defects in left-right axis patterning, while
CC       nodal flow is normal. {ECO:0000269|PubMed:21307098}.
CC   -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
DR   EMBL; AB573426; BAJ65629.1; -; mRNA.
DR   EMBL; BAAF04039115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BAAF04039116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BAAF04039117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   UniGene; Ola.29081; -.
DR   PRIDE; E7FKV8; -.
DR   Proteomes; UP000001038; Unplaced.
DR   Proteomes; UP000265180; Chromosome 9.
DR   Proteomes; UP000265200; Chromosome 9.
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; IDA:UniProtKB.
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; IMP:UniProtKB.
DR   GO; GO:0003127; P:detection of nodal flow; IMP:UniProtKB.
DR   GO; GO:0070986; P:left/right axis specification; IMP:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR000203; GPS.
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; PF01825; GPS; 1.
DR   Pfam; PF00801; PKD; 2.
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; PS50221; GPS; 1.
DR   PROSITE; PS50093; PKD; 2.
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; Complete proteome; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   2742       Polycystic kidney disease 1 like 1.
FT                                /FTId=PRO_0000425550.
FT   TOPO_DOM      1   1602       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1603   1623       Helical. {ECO:0000255}.
FT   TOPO_DOM   1624   1812       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1813   1833       Helical. {ECO:0000255}.
FT   TOPO_DOM   1834   1851       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1852   1872       Helical. {ECO:0000255}.
FT   TOPO_DOM   1873   2005       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2006   2026       Helical. {ECO:0000255}.
FT   TOPO_DOM   2027   2040       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2041   2061       Helical. {ECO:0000255}.
FT   TOPO_DOM   2062   2151       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2152   2172       Helical. {ECO:0000255}.
FT   TOPO_DOM   2173   2344       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2345   2365       Helical. {ECO:0000255}.
FT   TOPO_DOM   2366   2378       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2379   2401       Helical. {ECO:0000255}.
FT   TOPO_DOM   2402   2442       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2443   2463       Helical. {ECO:0000255}.
FT   TOPO_DOM   2464   2467       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2468   2488       Helical. {ECO:0000255}.
FT   TOPO_DOM   2489   2528       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2529   2549       Helical. {ECO:0000255}.
FT   TOPO_DOM   2550   2742       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      286    372       PKD 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00151}.
FT   DOMAIN      370    454       PKD 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00151}.
FT   DOMAIN      452   1338       REJ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00511}.
FT   DOMAIN     1538   1586       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   DOMAIN     1648   1769       PLAT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00152}.
FT   CARBOHYD     35     35       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    133    133       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    149    149       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    220    220       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    267    267       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    383    383       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    397    397       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    486    486       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    545    545       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    693    693       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    709    709       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    735    735       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1080   1080       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1101   1101       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1201   1201       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1318   1318       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1437   1437       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1490   1490       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1568   1568       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2218   2218       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT    847    847       L -> R (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT    974    974       L -> F (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1064   1064       K -> T (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1245   1245       R -> G (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1263   1263       T -> K (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1328   1328       L -> S (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1360   1360       S -> P (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1467   1467       I -> L (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1513   1513       L -> F (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1616   1616       N -> Y (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1814   1814       C -> Y (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1833   1833       Q -> K (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   1924   1924       T -> Q (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2014   2014       F -> L (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2036   2036       H -> L (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2182   2182       F -> I (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2189   2189       A -> G (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2192   2192       D -> E (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2195   2195       M -> T (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2257   2257       R -> C (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2348   2348       Y -> C (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2425   2425       V -> I (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2567   2567       V -> I (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2647   2647       L -> S (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
FT   CONFLICT   2665   2665       D -> V (in Ref. 1; BAJ65629).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2742 AA;  308537 MW;  FD9D7BD479F71201 CRC64;
     MFCLWIFSLA FLHLHLCSVS SSSLEGSGFF VGWINASSLQ LFASIGGCDL SPCMDEGQEG
     MEALYRSEEP FQCSIRASAS PGRRQAGRTC VRKVPGNLAV HCHLLSENEG LEEEDLLRIT
     VMTPRGQSSL QVNVSHGGLL TACSDWIWNT SEKHKNNVPA SGLHLGISLE VPCCTSCTRF
     GSDSELVEEQ CSALHVSVSD VLVKDYICCL TPRDKDKTLN RTETPCLYSS NSLKDSLVRG
     RVYQMSFEEC FRWHLLVVLL MLEAQYNHSQ EVHEDPSSTV KLCDYAVRIH AEKQAYSTNT
     DIPLLAVVDI LDPVEFLWDF GDFTSARANS RTITKRYTNP GIYKLVVVAS WGQMSVRSHV
     LSLVVQRAVK LNRLVHEPSV LQNHTVTVSC RVNVGTNLTF LWNFGDGTVR TGLSTEQHVF
     TRTGEFRVMV IASNLVSSAS LSSYLFVVDR PCQPPPVKNL GPPNIQVRRN EVVFLGVTFE
     SELNCNVSRE LHYSWTVYDS AGLTFPLPLT NTHRQSLVLQ SYTLPYGIYK AIARVQIVGS
     VVYSNYSVRL QVVPNSVVVV IQGGTNIYVN TKSSNEVTLD GQASYDPDFP LNPLRYSWTC
     QPVSTISSSC FSQSIPTSYP VLKFPTSLLK SNFDQFKFTL TVHSGERSAS SEIFLTLTSH
     LAGKLFVHCP ECQGDQVSWD QSFSVRAECE DCNVSAEFIQ YSWSLFRVNA SSKPVAEIPF
     CYTVDLNAPS AVLENASTPT PAPEMSPSHH FNADWTRFTE DSLASSSPSR IYKSKNRNSE
     LTDSPVSSVT VGFSGSESFN GPPGVDRGSS QFSNFPGQRD MFSEFQSDPE SSAEWEFTFP
     YLESEDLRGQ RGDSRVPFPR PEEGDPGISA GRPKETDMES FPSDSDSFSH SSSNKGEGSN
     LVDPRPSVRL QKPGLLDLHR DSVDKSLFES YTYTGISSCF LSFRSFSLKP SSTYMLELTA
     KSQRRFYGQT QLFLKVKPVP KGVACQVQPV RGIELYTHFS IFCTSGREDL IYTYSFSVGG
     RMPRILYQGR DFLYYFSLPS GDPTDDYKVI IYTEIRSSMY GSAKKLCPVT VRVEPSFVRN
     ASSSYSHHEP DLMISDSGLR NVSVLVQLGN IAEIYNYISL LSTILNRLSL DSQANTHALK
     HLRNVLICIV CKLEYSAQAS PADGIFILNE LLRVTSQVTV QSARWVTAHV GALSVQFSES
     NRSILSALVS LLSSSLQVVT SSPETSDSAD SPQPLESHLV TGKSRNAFVD DADHCITDLS
     ETTYNKQSEP VPKRLMMRLV NDLLQTTSDL MLRNFDLQKT KELQVQSDLI TLCAGFLNKT
     STAINCGLIT FFLPASLIKM LLLHDGISAK RGFSQREQPS CVQRIGMELL HNPYEWGRYP
     IQLKGPVADL SLYSCKTRRK IPVHSFLQPI TVELRHPQKT SSMSEYTLLR SQINYHNFSI
     TQEHLQQAVQ VTVVFTAPPH MAFPVKILFR MFERPTPSMH HLHRLLNWRN NTILLTLPPS
     YLSAAGVGHL ALLDANFGKT PTRRHLAEQI SYSLTVESSL CLSWEDQQGS WTQNGCRAQT
     NDKTSAVNCS CHHLKPLKVL QQQIQSSHFR ADLDQFLSVS RDLTVVFVLL LCVSLNIPVL
     VWCKKTDATS EENNRAHFLP DNSATDQHFY AVTVHTGLCS AARMSARVYV VLHGEDGCSQ
     TKELHVPGCT LFRRNSQNTF ILSVADSLGS VQGVHIWHNN SGPSPEWYLK QVQVSELMPG
     HMEGRSWQFI SQCWLAVNKG DGQVERMLRV STHGLTFSKM LFLKLFEYMP DYHIWMSVYT
     CPSPHLFTRA QRLCVCLLLF LGYACVNIII THQRDDQLPF DLGVIDVTSV SIATGLVSVV
     AVLPVAMVIS FLFRVKSGRM TLENYDNVFS KRPSGKTKYQ DTDFLSVSTT NLENKDADDK
     EAVTPQRNKR RKDSVSFESI HELLFQEVLQ VSRRRSLFLK KSKGNDSELS PQSSEFCGAL
     KATKNEAQSV RVKRRYRLAS LLYHCVAWTL CLLFCLSCLI LSAVLGTRLN SGKILHWIHS
     LFVSLTFCFF VIHPATILVL AAVVSWRFKR SQDFHCFFNK MNSHLEDLKH QDPDQLRPSA
     FTRTRAPNAE KILEARQRAR YLRRVHPPTR AELRKTRTKR KKQAVIHKML RDLCLCGSMF
     FLMVCITYGS PVDEHYPLNA AFRRHFIRAH GDDFMSIKKY EDWWKWAQTS LLSSLYYNES
     ENPQMSFISI GAPLVQKTEV CGTFHSQVSM VTPPRPRYHT GSSSKQEVTV GLGYTRSEGA
     SKLRLLHLSG WLSEQTVALK VQFSLYSPAP NLFSSVTLLS EQSSTGLLQS SATVQSVRLY
     HSPSMLDYTV MVWQLLFLLL SLVNLYHQTS TAAQHGLMGY WKTTSISVEV SLVIVSLVYY
     VHYVYHPTMV MEVAEQLRRN HREHVDVSTL ANSEQFSRTL RGIILFLLAV KCVTVVRLNR
     ILAPSMPLLS LSSLLWPAIS GLLLLSIFSC MGRLLYIERT FHSIQTVLWH FWSLRKSRDL
     ISLWRDFYYF GLLYASSAML TTMVFAVMIR KAKRSPSTKN DPTIREVLGC ISQKFTGMKT
     QIPDCHTQKT YFLEECESLV DELLFKLNAL SNSLHHTLPP KLHTYTDKDS PDASSTTELC
     KERLQDLVRS LSVGQGEAAL TFPHDRSLLE LQEEEEVKHQ EGRCSVGCKE SRLPETLWTA
     DYRESMDEHW TEKKSSNGLG GATYSHVVVV EALVHHEQGT KN
//
DBGET integrated database retrieval system