ID A0A674GJW3_TAEGU Unreviewed; 4132 AA.
AC A0A674GJW3;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Polycystin 1, transient receptor potential channel interacting {ECO:0000313|Ensembl:ENSTGUP00000022675.1};
GN Name=PKD1 {ECO:0000313|Ensembl:ENSTGUP00000022675.1};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000022675.1, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000022675.1, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000022675.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR Ensembl; ENSTGUT00000025418.1; ENSTGUP00000022675.1; ENSTGUG00000006371.2.
DR GeneTree; ENSGT00940000158702; -.
DR Proteomes; UP000007754; Chromosome 14.
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; 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 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; 14.
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.
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:UP000007754};
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 2910..2932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3117..3138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3158..3180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3316..3333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3353..3375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3387..3412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3418..3437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3505..3524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3726..3745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3765..3785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3805..3828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3854..3871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 188..220
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 295..409
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 805..867
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 900..969
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 987..1049
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1083..1140
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1157..1230
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1254..1314
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1332..1389
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1568..1654
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1681..1731
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1908..1991
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1994..2685
FT /note="REJ"
FT /evidence="ECO:0000259|PROSITE:PS51111"
FT DOMAIN 2955..3070
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT REGION 3984..4015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4107..4132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3988..4015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4115..4132
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4132 AA; 454798 MW; 406FED2E8B4A23ED CRC64;
EGCRGPGLRP RELFLLSLVN LSWNPFVCDC KLSWLPRWVE ERKVRVLEAS DTRCAHPPEV
ANLSLFDVLF LNATCAELII LFTSVHPGNL SEETCSALCY SQEQEYGGFS PQGQCVCGAA
HETNSSSGCL PFCTEHLSGQ GCGGPSLVPL PFQAQLPVSF TGLQPRYSLH QPVLFNVSIP
IAASTLLWEF GDRSEVLNTT AHTAVHSYAL PGRYNVTATL LVGSRLLQEQ AEIEVVASPQ
QLELQCPSLV VANESLDIRI RNRGGTGLAV LYGITAEPGQ LVHPMCPPEG LVFPGNNHCY
QLVVEKAEWL EAQRHCQELG DGDLAFVSSP DIQSFLVAHV IRSLDVWIGF NDFASSGAQQ
RGEGFNLESC QNWLPGEPHP SNADHCVRMG PTGQCNTDLC MAKHSYVCEY KPPGGLCWPS
VRVLQVLEFP ELAFRHQGFL TALEFVTQEL HQPVQVRFQV HRLMDGEVLP DYQEENNTTE
PFPSAQDDGN WTLLECPPGF QWCPLTSLCS SHNSCCNGTE CANSSFGSSP APGAPQPSDS
QPSRELLKEL LFTVPAGPSS QYQVSVDVPA HGRGIQHSAA SGSFLRCRRR AASAGRGNCS
AWAAGSCHSP AGAPRANSSA CSLRVRYAEE QLVPVLSPHN AGLERPGGYA VRASVGNGLF
SANLSCGFRV ASRVSGLRVL HPAPQGSRLY LPTNHTALLL KLSSGVNATA SCLGDNRTVP
FVATCPPALA PLCARETNDT WFAVLQLGGL GHGLSTHVLV AENSVSSQNI TVTVKVEEPI
RGLRATPDPE SRVLLNTRSY IPVMEAGSDV TFRWTVDDKP SFTFYNVVFN VIYQSPAVYK
LSLTASNHVS NFTVNYNVTV EMMNRMRNLS VVGALPVVPQ NSSVEFSARV HVDSAVEALF
LWDFGDGVQE TYLFKPPYNK SFLVPDPSVH EVVIEHNVSH IYQDPGEYAL MVVVSNQYEN
LTHLSPVQVH SYLVDVKVEA EEDVLVVGRP VTFRAAPLPS PYGVVYTWDF GDGSSLLTDT
QPSVTYSYPR RGVYNVTVTA NNTVSSVETV ECYQVFEEVT GLRVSTAEAA EQGAAVTINA
SVETGDSITW IFDMGDGTVL RSQVPVVEHV YIKDINCTVN VTAVNPVNSV SQAVPVRIFV
LEILKIEPTS CILEHPDVQL TAYVTGNPEE YIFDWTFGDG SSNVTVSGDP VVVHNFTRSG
TFPLTLTLSS SFNKANYFTS VCVEPEILNV TLLPSKRFVR LGEESSFQVS AVPPYQYRYR
WDFGNNESTR SSGTEVIYTY KNTGVFLVTV TVSNNVSFNN DTAFVEVQEP VGVAKIEYNG
TDVLELNQIY LFSASMNGTK VSYCWDFGDG TVQPGQVATH SYNSTGHYSI TVMGQNDVSS
NETTIDIAVK RRLFGLTVNA SRTVVPLNGS VSFVATLVAG TAIRYSWILC DRCTPIQGSS
TISYTFRSVG TFNVIVTAEN KISSLQDSIY VYVLEQIEGL QVASTDLVED LYFPTNKTLH
LQAVVREGTN ISYSWVVQRD GNAVQTFTGK TFPLSILEAG NYTVYLKATN MLGCATANRT
LEFMESLGVL KPYAFPNPAA INASVNISAT ITSGTGVTYV WYLEDGSSPV TSEPFILHSF
QSSGMIEVIV GAENKLNSTN ATVSVCVEEV IEGLTIGTAE LDCRYVSSGS TVVFEGELQR
GTEVTWLWQV PNGTLSGQSV AVTFPTAGLY TVHLNASNHI SWALASRNIS VLDRIQGLEV
VASKKVVEPG EQVTFEIRML SGTSVSYLVS ISGDYSVVLN GSRYNHEFTK SGDYLVTVTV
QNQISIAHAQ VLISVLEPIQ DLRLLNCCEE GIPTGTEKSF SARVGSGSRV SFSWQFCLWK
ERGRSVVAAS GERVSYAPEA AGLLEIHLTA FNDLGSVNIT RTMQVQDPIV QVSLSATNAF
VNRTALFEAV VVPSSRSVEF LWSFGDGSST QTTRVAVANY SYLSPGDYLV EVNATNLISF
FIAQLTVTVK VLECEEPEVE LALPPQVVMK RSQRNYLEAQ IDLRGCIKYQ TEHLWEIYRA
PSCMNLDDSS RIRLPNVDVN RPQLVIPKLG LEVGSYCFMF IVSFGDTPLS KSIFANVTVI
PSKLVPIIDG GSYRVWSNTQ DLVLDGEKSY DPNLDDGEQT PLLYEWSCTS SSKQSSAAGC
SLNFSAKEGI VTISKALLEA DVEYTFDLTV RKEGMSPEAT NQTVFIKRGG VPIVSLECVS
CKAQSVYEVS KSSYVYLEGT CQNCHNDSKL GRWAAHSFKN KSLILDKTTT STGDTGMNLV
LRPGALRDGE GYTFTLHITD LTTGEEGFAS IDLLPNQPPV GGSCRLSPEG PLRALVTKVH
FECAGWRDTE DAEGPLVFIL LASRHRPGHF HEFCVYKGSR AEHGAFLPPG FHESGFQVSV
AVLVQDQLGA TVVAVNRSME IGLPEGFPSL SHWLYNQTDT VLQGLVKQGD PQQVIEYSLA
LITILNEYER SVLLEPEAGQ EFELRTWTRN NITETLNALK VNTVDDIQQI SAALAQCTVV
SKELVCKSCL TRTLNKLETM MTILQGETTQ GTVTPTGIAD NILNITGDLI HLVNTVSQES
KPQELLADSH NLLLAPKAYN LSSSLMRILM KSRVLNEEPL ELVGGEIKAT GKRSDPFNLL
CYENTPNCQF SIPQAFNSTL SNLTDVIQVM FQVDSNPFPF GYISNYTVST KVASMEFQTH
NGVQIPIGSL DSEKAITVMV SNSTEPKNLV AGTEVIEART SVNLIVIMES NNREAGLHFQ
LTYRVLNEHY LASEPEPFIM AYLHHEPEPN EHNCSASKRI SLDALAGSDH KLYTFFTSPR
TDDPIQKYYL NITNHFSWSA VEVTLGLYTS LCQYFSEQEK RWKTEGIVPL EETRPDQAVC
LTQHLTAFGA SLFVPPNSVQ FIFPAPGPGL NYIVLLTCAV CFVTYSVAAL IVHKLDVIDT
NRVGVIPFCG KNGMYKYEIL VKTGWGRGSG TTAHVGIALY GVDNKSGHRH LDGDNAFHRN
SLDVFQIATE RSLGSVWRIR IWHDNKGLSP SWYLQHVIVR DLQSSKSYFF LVNDWLSVES
EDNDGLVERE VFAASDELRS FWRIFVAELQ RGFFEKHVWL SLWDRPPRSR FTRVQRATCC
CLLIFLFLCA NAVWYGVVGS VHLSNVAISS LIPVSVDTVA VGLVSSVVVY PLYLVILFLF
RMARGKVRRR GMVADQQSLE IDNYLDSSIL DSSFPTFPGL QAEVTASLPA AGQALEVLVP
WPSSEALLSW PDLLSDPSIM DNTIQKLKRG RASRHLGLEA PLAAEEDALS LGIHQGQPRY
FSASGEPWGR AGAAELLPSP LAVLWVVSAP VFGEKVETVM MQRLNDKGPA LPVPTGPFAV
VFTLLSLLLL LLPVADQTFR KRLLPPWCSL LAHGISLLLL ATAAGVSVWI GVGFSSSVAL
MWLISGIFSF LASFLLWEPL KVLLEALYFS LVAKRLHPEE DDTLVEQPCV EHVSERISKV
RPPQGFALFQ AKEEARKVKL LHRMLKNFLI YMMFLLVVLL INYGDASRTS RAFLLQSSIK
QQLGSSDFLL IKRSDQFWVW MSQVFLPYLY NNGSGQESHS TTLGTARLRQ LRLAQRSCTD
QHSFATADYE VGWESTAGNG TAAWAHSAPD LAGIWYWGYI SFYDSSGYVQ ELGPSLEQSR
AQLEFLQQHT WIDNMSRAVF VELLQYNPSV DLHVALTLRL EFPGAGQAMA AVTVSPFPLL
RLSGGVTLQL LMMVFLMLFV VYFVVSESLA IKKEGRAYFT LWGNYSQWVF ILLTTCTVLV
HLSQATLADQ QWLRYLSNRR GFTNFYQVAF LSSVFSSLAA SLLFLLTVQA AQQLRFVRQW
SVFGKTFQKS MKELMAAGVA FALLLLAYAQ LGFLVTTPVG SSLLLLLALL RGSASLRPCL
PEASGLCCLF CTSYVVLEVW IVLRLLAAVL IHSYREMHFE LYRPAFEPQD YEMVELFVRR
LKMWMGFSKA KEFRHKVRFE GMEPLPSRDS SDSKSFRGAT PSAASDSSRT STSSSQLDGL
SLVLSARDSL EVDADIQRLL SLFEMLLAQF DRVNQVTEDV SRIEHLLEFS RSRCVPDTEP
LSPRCARAVP VPGRLLRASR GVSAAAGTAG KPCAARRKRP LRAKNRVHPT VK
//
