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
//