ID A0A218V749_9PASE Unreviewed; 2374 AA.
AC A0A218V749;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Polycystic kidney disease protein 1-like 2 {ECO:0000313|EMBL:OWK61648.1};
GN Name=PKD1L2 {ECO:0000313|EMBL:OWK61648.1};
GN ORFNames=RLOC_00000363 {ECO:0000313|EMBL:OWK61648.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK61648.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK61648.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK61648.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OWK61648.1}.
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DR EMBL; MUZQ01000037; OWK61648.1; -; Genomic_DNA.
DR STRING; 299123.ENSLSDP00000022578; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd22831; Gal_Rha_Lectin_PKD1L2; 1.
DR CDD; cd00146; PKD; 1.
DR CDD; cd01752; PLAT_polycystin; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR042060; PLAT_polycystin1.
DR InterPro; IPR046791; Polycystin_dom.
DR PANTHER; PTHR10877:SF134; POLYCYSTIC KIDNEY DISEASE PROTEIN 1-LIKE 2; 1.
DR PANTHER; PTHR10877; POLYCYSTIN FAMILY MEMBER; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF20519; Polycystin_dom; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
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 1194..1213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1401..1421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1486..1507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1738..1762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1774..1805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1864..1886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2109..2129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2149..2166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2198..2218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2238..2262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2300..2325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..182
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 190..281
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 1238..1355
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT REGION 1514..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1960..1973
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ SEQUENCE 2374 AA; 266567 MW; 8A9638AE14BA5ACA CRC64;
MISEAFEEGS KKSVVLVSKT SGMHGTELRM WLGLTVLISL AVSLAVEETT DGGIPCSKYQ
QAFNHSCYEF VRLQQTFTGA QSWCERGGGH LVFIHSEETQ EFLQKHIAED QEWWIGLISN
SLLNETTDGS ITWLDTSNII YTNWYKDQPS PFSSTCGYIL KNAKYQWGVT ENCSQEFDFI
CEFESGQSIA CDNYNATVQC GSGEVIQIEE SFYGRKTPHY CVSETPLQFE RDEGCSWSSV
KDEVAGQCHG LQACQVAADG TFFGDPCPAL GSYLSIQYHC KEGLQLVMTD TCFVFENITV
TLTWLLSPYS GNLSCTISTG DGHTIDPYYP PTLVSNLTYR YSSPGEFTVF VECTTSEWHV
LAQRQVTVQD QVDQLSITGC YSHYETGNSS RCRTLYGEVL WIQVQLSGGN EVTYSMLAGN
MTLSESSAKE GLVSHNLTLS SASQELIGPG MHQLEIRASR TTMASEISGT IAVHLIEPVS
GIQAAVASHT LQLGEDLEVN VSVTHGAPEK LMFEVTGSNQ TQWHKADGPR GEPRTYGVPL
PREGTFLVKV VAMNDFSNMS LDLGFITVLA NSSHIKDSDK EEGSYKANTR KKNDHKMYIK
PSRHVDPFTT VTLGWPDNNN NSSFLWTCGA CWPAWNECVK QQIILINQSE VQIPPSCLPP
PKSAVTVRIT IQNHGNEERQ DEQCLYVTAK QELQLEIRCE ANCKPVNVSD EVVLSVSEQE
DSQAIYYNWY LDNTFQNKPF FPVPDSLLDC SPDPELFPVY LPLGEEEDNF ILHLTIIVSN
NVGDTVQTNT SVKVGPADMM DGNLTLQAVV SEKANTILKD GNNSMSLFQL YKSVTSVLNQ
QIQEESFNMS LPTNTRKELR GLMLTTLSVV NITSMQTALK MSEVLKEITY RSEELSVSAQ
VEASSTLKHV SASLLAVSTE HSRDGQELKE AANYLFNAVS SVLKASVEIR AGNTSVPEAK
QMVSFAMNPF FSSDSSFDIS GTVGGLSLTG VDGLIIPVSN LKENIEIMLP RLSAIQEDKI
LLNLGNYSTF QVNVTSENTS LVIHLESEHD IPLILYLGYG YHPNETNYDM KNHLFYKKTS
GGEMNSWVLR PEELIFGEGT YYFMVLQDMG MDSTVYEGLT INATCFASRC VFWDEQQGGW
NSYGCHVGPK TNPSSTQCLC NHLTFFGSSF FVIPNAIDVS KTAQLFGTFV DNPVVVTTVG
CIFLIYVLVV IWARRKDIQD DAKVKITVLE DNDPFAQYRY LVTVFTGHRR GAATTSKVTL
TLCGLDGESE PHHLNDPDTP VFERGGVDVF LLCTFFPLGE LQSIRLWHDN SGDSPSWYVN
RVLVHDLAWD QKWYFLCNSW LAIDIGECVL DKVFPVATEK DMKQFSNLFF METSKGFQDG
HIWYSVFSRS PRSSFTRAQR VSCCFSLLLC TMLTSIMFWG VPKDPAEQKM DLGNNPHHCL
GRQIERQQNL EADFERLDGL FCLGLFFPSL LCLTLTGKIE FTWQEVMIGF ESSLLMFPIN
LLIVQIFRNV RPRPAQQGRE KKPGKNGRVS PSLPPTPGAT QAASLTPEAV TKASPTCLKR
KANFPWCKDI RRIANSLFKA LKTPSLTSAL DLEKSANINT LLSLVEDVIC QQNRAGQGFY
DEIKKDGPII VTLGAMDIQE KTRNLTPEKR ICDQLKCNDY HRCLYMQLQH IEMELELLGP
HKFQMPQSYT QAVCQVQHMK NLLENQICSS ASISEGWSHT LNLSNDDKKS SSSRGLPWWF
VFIAWFLVAA TSSVSGFFTM LYGLHYGKEN SIKWLISMVI SFLESLFITQ PLKVLGFAAF
FALVLKKVEH EDEENTAIDG PLSAPGDSHP LFGVRRDSRS NIYRPPPAAD VEKMKISYMK
EQKAFALIRE ILAYVGFLWM LLLVAYGQRD PNSYYLNKHI EDSFTDGFHD VYSYQDFFTW
ANTTLLKNLY GSYKGFITDG NSKLVGSARI RQVRVKGDSC PISPRLQHIV EECHAPYSLQ
TEDTSAYGEH WNASALDNSS DLSSAWQYQS QSKLRGHPSW GKLAIYSGGG YVIHLGTDPK
NASRILQYLF NNVWLDTFTR AVFVEFTVYN ANVNLFCIIS LMFESNALGA FFTSAELQSV
RLYPYTNSLH IFVVAAEVIY FLFIVYYMIV QGKLLKSLRW RYFHSKWNLL EMAIILISWS
ALSVFVKRTV LGTRDISYYQ EHKEDSISFS ETARADAVLG YLIAFLVLLS TVKLWHLLRL
NPKLNMITST LRRAWGDISG FITVIAIMFL AYSIAANLIF GWKLCSYKTL LDSAETMVSL
QLGIFNYEEV LDYNPVLGSF LIGSCIIFMT FVVLNLFISV ILVAFSEEQK HYQASEEEEI
VDLMLMKVFS FFGIKCKKEE KPVAGEQLEQ SASE
//
