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Database: UniProt
Entry: A0A3L8RXK1_CHLGU
LinkDB: A0A3L8RXK1_CHLGU
Original site: A0A3L8RXK1_CHLGU 
ID   A0A3L8RXK1_CHLGU        Unreviewed;      4198 AA.
AC   A0A3L8RXK1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Polycystin-1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DV515_00014784 {ECO:0000313|EMBL:RLV89606.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV89606.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV89606.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV89606.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV89606.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the polycystin family.
CC       {ECO:0000256|ARBA:ARBA00007200}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV89606.1}.
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DR   EMBL; QUSF01000142; RLV89606.1; -; Genomic_DNA.
DR   STRING; 44316.ENSEGOP00005016113; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001822; P:kidney development; IEA:InterPro.
DR   CDD; cd00037; CLECT; 1.
DR   CDD; cd00146; PKD; 13.
DR   CDD; cd01752; PLAT_polycystin; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000434; PC1.
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; IPR042060; PLAT_polycystin1.
DR   InterPro; IPR006228; Polycystin_cat.
DR   InterPro; IPR046791; Polycystin_dom.
DR   InterPro; IPR014010; REJ_dom.
DR   InterPro; IPR002889; WSC_carb-bd.
DR   NCBIfam; TIGR00864; PCC; 1.
DR   PANTHER; PTHR46730; POLYCYSTIN-1; 1.
DR   PANTHER; PTHR46730:SF3; POLYCYSTIN-1; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00801; PKD; 15.
DR   Pfam; PF08016; PKD_channel; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   Pfam; PF20519; Polycystin_dom; 1.
DR   Pfam; PF02010; REJ; 1.
DR   PRINTS; PR00500; POLYCYSTIN1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00308; LH2; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00089; PKD; 15.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   SUPFAM; SSF49299; PKD domain; 14.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50093; PKD; 11.
DR   PROSITE; PS50095; PLAT; 1.
DR   PROSITE; PS51111; REJ; 1.
DR   PROSITE; PS51212; WSC; 1.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023069};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2929..2951
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3131..3152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3172..3194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3413..3435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3441..3460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3528..3547
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3767..3786
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3806..3826
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3846..3869
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3895..3917
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        3954..3979
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..200
FT                   /note="WSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51212"
FT   DOMAIN          234..266
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          344..458
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          860..922
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          954..1023
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1041..1103
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1137..1194
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1211..1284
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1308..1368
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1386..1443
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1622..1708
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1735..1785
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          1962..2045
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          2048..2704
FT                   /note="REJ"
FT                   /evidence="ECO:0000259|PROSITE:PS51111"
FT   DOMAIN          2974..3089
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   REGION          4032..4063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4121..4198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4036..4063
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4181..4198
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4198 AA;  462893 MW;  3A280648715994DB CRC64;
     MLCAPPELSQ LLQDRDRCRD RIFLLMDLSN NRISGLDVEL FRSLTSLAKL NLSWNPFVCD
     CKLSWLPRWV EDRKVTVLEA SDTRCAHPPE VANLSLFDVL FLNATCGAQY ITCLTGNYTE
     EAEFIILFTS VHPGNLSEET CSALCYSQEQ EYGAFSPQGQ CVCGTAYETN SSSGCLPFCT
     EHLSGQGCDG PSLIPLPFQA QLPVSFTGLQ PRYSLHQPVL FNVSIPIAAS TLLWEFGDQS
     EVLNTTGHTA VHSYALPGHY NVTATLLVGS RLLQEQAEIE VVASPQQLEL QCPSLVVANE
     SLDIRIRNRG GTGLAVLYGI TAEHGQLGRA VHPMCPPEGL VFPGNNHCYQ LVVEKAEWLE
     AQRHCQELGN GDLAFVSSPD IQSFLVAHVI RSLDVWIGFN DFASSGAQQR GEGFNLESCQ
     NWLPGEPHPS NADHCVRMGP TGQCNTDLCM AKHSYVCEYK PPGVLLNAEN FFEGDAELAT
     EEAVRSVSEA VLADPWQAEE VLEFPELAFR HQGFLTALEF VTQELHQPVQ VRFQVHRLMD
     GEDYQEENNA TEPFPSAQDD GNWTLLECPP GFQWCPLTSL CSSHNSCCNG TECANSSSGS
     SPAPGSLQPS HELLKELLFT VPAGPSSQYQ VAFKKENIFV RPGDVFSIQH NAASGSFLRC
     RRRAPSLGGG SRSACSLRVR YAEEQLVPVL RPHNAGLERP GGYALRAAVA NGLFSANLSC
     AFRVASRVSG LRVLHPAPQG SRVYLPANRT ALLLKISSGL NATARCLGDD RTVPFVAACP
     PAVASLCARE TNDTWFAVLQ LGGLGEGVST HVLVAENSVS SQNITVTVKV EEPIRGLRAT
     PDPESRVLLN TRVSYIPVME AGSDVTFRWT VDDKPSFTFY NVVFNVIYQS PAVYKLSLTA
     SNHVSNFTVN YNVTVEMMNR MRNLSVVALP VVPQNTSVEF SARVHVDSAV EALFLWDFGD
     GVQETYLFKP PYNKSFLVPD PSVHEVVIEH NVSHIYQDPG EYALMVVVSN QYENLTHLSP
     VQVHSYLTDV KVEAEEDVLV VGRPVTFRAT PLPSPCGVVY TWDFGDGSSL LTESQPSATY
     SYRCRGVYNV TVTANNTVSS VETVECYQVF EEIMGLRVSA AEAAEQGAAV TINASVETGD
     GITWIFDMGD GTVLRSQVPV VEHVYIKDIN CTVNVTAVNP VNSVSQAVPV RIFVLEILKI
     EPTSCILEHP DVQLTAYVTG NPEEYIFDWT FGDGSSNVTV SGDPVVVHNF TRSGTFPLTL
     TLSSSFNKAN YFTSVCVEPE ILNVTLLPSK RFVRLGEETS FQVSAVPPYH YRYRWDFGNN
     ESTRSSGTEV TYTYKNTGVF LVTVTVSNNV SFNNDTAFVE VQEPVGVAKI EYNGTDVLEL
     NQIYLFSASM NGTKVSYCWD FGDGTVQPGQ VATHSYNSTG HYSITVMGQN DVSSNETTID
     VTVKRRLFGL TVNASRTVVP LNGSVSFVAS LVAGTAIRYS WILCDRCTPI QGSSTISYTF
     RSVGTFNVIV TAENKISSLQ DSIYVYVLEQ IEGLQVASTD LVEDMYFPTN KTLHLQAVVR
     EGTNISYSWV VQWDGNAVQT FTGKTFPLSI LEAGNYTVYL KATNMLGCAT ANRTLEFMES
     LGVLKPYAFP NPAAINASVN ISATITSGTG VTYVWYLEDG SSPVTSEPFI IHSFQSSGMI
     EIIVGAENKL NSTNATVSVC VEEVIEGLTI GTAELDCRYV SSGSTVVFEG ELQRGTEVTW
     LWQVPNGTLS GQSVAVTFPT AGLYTVHLNA SNHISWAVAS RNISVLDRIQ GLEVVASKKV
     VKPGEQVTFE IRMLSGTSVS YLVSISGDYS VVLNSSRYSH EFTKSGDYLV TVTVQNQISI
     AHAQVLISVL EPIQDVRLLN CCEEGIPTGT KKSFSARVGS GSRVSFSWQF CLWKERGRSV
     VAASGERVSY APEAAGLLEI HLTAFNDLGS VNITRTMQVQ DPIVQVSLSA TNAFVNRTAL
     FEAVVVPSNR SVEFLWSFGD GSSTQTTRVA VANYSYLSPG DYLVEVNATN LISFFIAQLT
     VTVKVLECEE PEVELALPPQ VVMKRSQRNY LEAQIDLRGC IKYQTEHLWE IYRAPSCMNL
     DDSSRIRLPN VDVNRPQLVI PKLGLEVGSY CFMFIVSFGD TPLSKSIFAN VTVIPSKLVP
     IIDGGSYRVW SNTQDLVLDG EKSYDPNLDD GEQTPLLYEW SCTSSSKSSA AGCSLNFSAK
     EGIVTISKAL LEADVEYTFD LTVRKEGMSP EATNQTVFIK RGGVPIVSLE CVSCKAQSVY
     EVSKSSYVYL EGTCQNCHND SKLGRWAAHS FKNKSLILDR TTTSTGDTGM NLVLRPGALR
     DGEGYTFTLH ITDLTTGEEG FASIDLLPNQ PPVGGSCRLS PEGPLRALVT KFCVYKGSRA
     EHGAFLPPGF HESGFQVSVA VLVQDQLGAT VVALNRSMEI GLPEGFPSLS HWLYNQTDTV
     LQGLVKQGDP QQVIEYSLAL ITILNEYERS VLLEPEAGQE FELRTWTRNN ITETLNSLKV
     NTVDDIQQIS AALAQCTVVS KELVCKSCLT RTLNKLETMM AILQGETTQG TVTPTGIADN
     ILNITGDLIH LVNTVSQESK PQELLADSHN LLLAPKAYNL SSSLMRILMK SRVLNEEPLE
     LVGGEIKATG KRSDPFNLLC YENTPNCQFS IPQAFNSTLS NLTDVIQVMF QVDSNPFPFG
     YISNYTVSTK VASMEFQTHN GVQIPIGSLD SEKAITVMVS NSTEPENLVA GTEVIEARTS
     VNLIVIMESN NREAGLHFQL TYRVLNEHYL ASEPEPFIMA YLHHEPEPNE HNCSATKRIS
     LDALAGSDHK LYTFFTSPRT DDPIQKYYLN ITNHFSWSAV EVTLGLYTSL CQYFSEQEKR
     WKTEGIVPLE ETRPDQAVCL TQHLTAFGAS LFVPPNSVQF IFPAPGPGLN YIVLLTCAVC
     FVTYSVAALI VHKLDVIDMN RVGVIPFCGK NGLYKYEILV KTGWGRGSGT TAHVGIALYG
     VENKSGHRHL DGDNAFHRNS LDVFQIATER SLGSVWRIRI WHDNKGLSPS WYLQHVIVRD
     LQSSKSYFFL VNDWLSVESE DNDGLVERES ELRSFWRIFV AELQRGFFEK HVWLSLWDRP
     PRSRFTRVQR ATCCCLLIFL FLCANAVWYG VVGSVHLSNV AVSSLIPVSV DTVAVGLVSS
     VVVYPLYLVI LFLFRMARGK VSISHTVTHS DQQSLEIDNY LDSSILDSSF PTFPGLQAEA
     FSEQTKTDLF LEDPKSLVPW PSSEALLSWP DLLSDPSIMD NTIQKLKRGR ASRHLGLEAP
     LATEEDTLSL GIHQGQPRYF SASDEDLIRQ ILADGASGIS QDLGPYMRAE TDLISGLSSV
     FGEKVETVMM QRLNDKGQSV APPPREVSRS AKSTWTVADQ TFRKRLLPPW CSLLAHGISL
     LLLATAAGVS AWIGVGFSSS VALMWLISGI FSFLASFLLW EPLKVLLEAL YFSLVAKRLH
     PEEDDTLVEQ PCVEHVSERI SKVRPPQGFA LFQAKEEARK VKLLHRMLKN FLIYMMFLLV
     VLLTNYGDAS RTSRAFLLQS SIKQQLGSSD FLLIKRSDQF WVWMSQVFLP YLYNNGSGQE
     SHSTTLGTAR LRQLRLRGAE CQQSAQDILQ GMGSAQRSCT DQHSFATADY GVGWESTAGN
     GTAAWAHSAP DLAGIWYWGY ISFYDSSGYV QELGPSLEES RAQLEFLQQH TWIDNMSRAV
     FVELLQYNPS VDLHVALTLR LEFPGAGQAM AAVAISPFPL LRLSGGVTLQ LLMMVFLMLF
     VVYFVVSESL AIKKEGRAYF TLWGNYTQWV FILLTTCTVL VHLSQATLAD QQWLRYLSNR
     RGFTNFYQVA FLSSIFSSLA ASLLFLLTVQ AAQQLRFVRQ WSVFGKTFQK SMKELMAAGV
     AFALLLLAYA QLGFLLFSSS SEPFRSVGSS LLLLLALLRG GASLRPCLPE ASGLFCLFCT
     SYVVLEVWIV LRLLAAVLIH SYREMHFELY RPAFEPQDYE MVELFVRRLK MWMGFSKAKE
     FRHKVRFEGM EPLPSRDSSD SKSFRGATPS AASDSSRTST SSSQLDGLSL VLSARDSLEV
     DADIQRLLSL FEMLLAQFDR VNQVTEDVSR IEHLLEFSRG RRARRRPRGP EAGGSEQGPS
     PEVPDAAPLS PRRAGAVPGR LLRASRGVSA AAGAAGKPCA ARRKRPLRAK NRVHPAVK
//
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