CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015925
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polycystic kidney disease protein 1-like 2 
Protein Synonyms/Alias
 PC1-like 2 protein; Polycystin-1L2 
Gene Name
 PKD1L2 
Gene Synonyms/Alias
 KIAA1879; PC1L2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
2428ILSFLGIKSKREEPGubiquitination[1]
Reference
 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 May function as an ion-channel regulator. May function as a G-protein-coupled receptor. 
Sequence Annotation
 DOMAIN 35 153 C-type lectin.
 DOMAIN 161 252 SUEL-type lectin.
 DOMAIN 422 1123 REJ.
 DOMAIN 1279 1328 GPS.
 DOMAIN 1390 1507 PLAT.
 REGION 2340 2362 Channel pore-region.
 REGION 2379 2459 Interaction with GNAS and GNAI1.
 MOTIF 2024 2035 Polycystin motif.
 MOTIF 2119 2129 Polycystin motif.
 CARBOHYD 96 96 N-linked (GlcNAc...) (Potential).
 CARBOHYD 110 110 N-linked (GlcNAc...) (Potential).
 CARBOHYD 268 268 N-linked (GlcNAc...) (Potential).
 CARBOHYD 307 307 N-linked (GlcNAc...) (Potential).
 CARBOHYD 441 441 N-linked (GlcNAc...) (Potential).
 CARBOHYD 536 536 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1176 1176 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1186 1186 N-linked (GlcNAc...) (Potential).
 DISULFID 56 152 By similarity.
 DISULFID 128 144 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein; Ion channel; Ion transport; Lectin; Membrane; Polymorphism; Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2459 AA 
Protein Sequence
MSAVGLVLLV LALRLRATTV KPEEGSFCSN SQVAFRDACY EFVPLGRTFR DAQSWCEGQG 60
GHLVFIQDEG TQWFLQKHIS QDREWWIGLT WNLARNGTTE GPGTWLDTSN VTYSNWHGGQ 120
AAAAPDTCGH IGRGPSSEWV TSDCAQTFAF MCEFRVGQSL ACEGLNATVH CGLGQVIQVQ 180
DAVYGRQNPH FCTQDAGRPS DLEQGCSWAN VKEEVAGQCQ ELQSCQVAAD ETYFGNLCPT 240
QGSYLWVQYQ CREALQLMVS SESFIFDNVT ISLTWLLSPY IGNLSCIIST GDSHTFDPYN 300
PPSVSSNVTH QFTSPGEFTV FAECTTSEWH VTAQRQVTVR DKMETLSVTA CSGLSQSGAG 360
PLCQAVFGDP LWIQVELDGG TGVTYTVLLG DITLAESTTQ KGSLPYNLIL DRETQKLMGP 420
GRHRLEIQAT GNTTTSTISR NITVHLVELL SGLQASWASD HLELGQDLLI TISLAQGTPE 480
ELTFEVAGLN ATFSHEQVSF GEPFGICRLA VPVEGTFLVT MLVRNAFSNL SLEIGNITIT 540
APSGLQEPSG MNAEGKSKDK GDMEVYIQPG PYVDPFTTVT LGWPDNDKEL RFQWSCGSCW 600
ALWSSCVERQ LLRTDQRELV VPASCLPPPD SAVTLRLAVL RGQELENRAE QCLYVSAPWE 660
LRPRVSCERN CRPVNASKDI LLRVTMGEDS PVAMFSWYLD NTPTEQAEPL LDACRLRGFW 720
PRSLTLLQSN TSTLLLNSSF LQSRGEVIRI RATALTRHAY GEDTYVISTV PPREVPACTI 780
APEEGTVLTS FAIFCNASTA LGPLEFCFCL ESGSCLHCGP EPALPSVYLP LGEENNDFVL 840
TVVISATNRA GDTQQTQAMA KVALGDTCVE DVAFQAAVSE KIPTALQGEG GPEQLLQLAK 900
AVSSMLNQEH ESQGSGQSLS IDVRQKVREH VLGSLSAVTT GLEDVQRVQE LAEVLREVTC 960
RSKELTPSAQ WEASLALQHA SEALLTVSAK ARPEDQRRQA ATRDLFQAVG SVLEASLSNR 1020
PEEPAEASSS QIATVLRLLR VMEHVQTTLL LGKLPGGLPA MLATPSISVY TNRIQPWSWQ 1080
GSSLRPDAAD SATFMLPAAS SLSSLEGGQE PVDIKIMSFP KSPFPARSHF DVSGTVGGLR 1140
VTSPSGQLIP VKNLSENIEI LLPRHSQRHS QPTVLNLTSP EALWVNVTSG EATLGIQLHW 1200
RPDIALTLSL GYGYHPNKSS YDAQTHLVPM VAPDELPTWI LSPQDLRFGE GVYYLTVVPE 1260
SDLEPAPGRD LTVGITTFLS HCVFWDEVQE TWDDSGCQVG PRTSPYQTHC LCNHLTFFGS 1320
TFLVMSNAIN IHQTAELFAT FEDNPVVVTT VGCLCVVYVL VVIWARRKDA QDQAKVKVTV 1380
LEDNDPFAQY HYLVTVYTGH RRGAATSSKV TVTLYGLDGE REPHHLADPD TPVFERGAVD 1440
AFLLSTLFPL GELRSLRLWH DNSGDRPSWY VSRVLVYDLV MDRKWYFLCN SWLSINVGDC 1500
VLDKVFPVAT EQDRKQFSHL FFMKTSAGFQ DGHIWYSIFS RCARSSFTRV QRVSCCFSLL 1560
LCTMLTSIMF WGVPKDPAEQ KMDLGKIEFT WQEVMIGLES SILMFPINLL IVQIFQNTRP 1620
RVAKEQNTGK WDRGSPNLTP SPQPMEDGLL TPEAVTKDVS RIVSSLFKAL KVPSPALGWD 1680
SVNLMDINSL LALVEDVIYP QNTSGQVFWE EAKKREDPVT LTLGSSEMKE KSQCPKPKAA 1740
RSGPWKDSAY RQCLYLQLEH VEQELRLVGP RGFSQPHSHA QALRQLQTLK GGLGVQPGTW 1800
APAHASALQV SKPPQGLPWW CILVGWLLVA ATSGVAAFFT MLYGLHYGRA SSLRWLISMA 1860
VSFVESMFVT QPLKVLGFAA FFALVLKRVD DEEDTVAPLP GHLLGPDPYA LFRARRNSSR 1920
DVYQPPLTAA IEKMKTTHLK EQKAFALIRE ILAYLGFLWM LLLVAYGQRD PSAYHLNRHL 1980
QHSFTRGFSG VLGFREFFKW ANTTLVSNLY GHPPGFITDG NSKLVGSAQI RQVRVQESSC 2040
PLAQQPQAYL NGCRAPYSLD AEDMADYGEG WNATTLSEWQ YQSQDQRQGY PIWGKLTVYR 2100
GGGYVVPLGT DRQKHVKILR YLFDNTWLDA LTRAVFVEST VYNANVNLFC IVTLTLETSA 2160
LGTFFTHAAL QSLRLYPFTD GWHPFVVAAE LIYFLFLLYY MVVQGKRMSK ETWGYFCSKW 2220
NLLELAIILA SWSALAVFVK RAVLAERDLQ RCRNHREEGI SFSETAAADA ALGYIIAFLV 2280
LLSTVKLWHL LRLNPKMNMI TAALRRAWGD ISGFMIVILT MLLAYSIASN LIFGWKLRSY 2340
KTLFDAAETM VSLQLGIFNY EEVLDYSPVL GSFLIGSCIV FMTFVVLNLF ISVILVAFSE 2400
EQKYYQLSEE GEIVDLLLMK ILSFLGIKSK REEPGSSREQ PGSLSQTRHS RPAQALPKD 2459 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0030246; F:carbohydrate binding; IEA:InterPro.
 GO:0006811; P:ion transport; IEA:UniProtKB-KW.
 GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro. 
Interpro
 IPR001304; C-type_lectin.
 IPR016186; C-type_lectin-like.
 IPR016187; C-type_lectin_fold.
 IPR000203; GPS_dom.
 IPR000922; Lectin_gal-bd_dom.
 IPR008976; Lipase_LipOase.
 IPR001024; LipOase_LH2.
 IPR002859; PKD/REJ-like.
 IPR013122; PKD1_2_channel.
 IPR003915; PKD_2.
 IPR014010; REJ-like. 
Pfam
 PF02140; Gal_Lectin
 PF01825; GPS
 PF00059; Lectin_C
 PF08016; PKD_channel
 PF01477; PLAT
 PF02010; REJ 
SMART
 SM00034; CLECT
 SM00303; GPS
 SM00308; LH2 
PROSITE
 PS00615; C_TYPE_LECTIN_1
 PS50041; C_TYPE_LECTIN_2
 PS50221; GPS
 PS50095; PLAT
 PS51111; REJ
 PS50228; SUEL_LECTIN 
PRINTS
 PR01433; POLYCYSTIN2.