ID PK1L2_MOUSE Reviewed; 2461 AA. AC Q7TN88; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 07-APR-2021, entry version 125. DE RecName: Full=Polycystic kidney disease protein 1-like 2; DE AltName: Full=PC1-like 2 protein; DE AltName: Full=Polycystin-1L2; DE Flags: Precursor; GN Name=Pkd1l2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=12782129; DOI=10.1016/s0888-7543(03)00048-x; RA Li A., Tian X., Sung S.-W., Somlo S.; RT "Identification of two novel polycystic kidney disease-1-like genes in RT human and mouse genomes."; RL Genomics 81:596-608(2003). RN [2] RP ERRATUM OF PUBMED:12782129. RA Li A., Tian X., Sung S.-W., Somlo S.; RL Genomics 82:498-500(2003). CC -!- FUNCTION: May function as an ion-channel regulator. May function as a CC G-protein-coupled receptor (By similarity). {ECO:0000250}. CC -!- SUBUNIT: May interact via its C-terminus with GNAS and GNAI1. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY164484; AAO32797.1; -; mRNA. DR RefSeq; NP_083962.4; NM_029686.4. DR SMR; Q7TN88; -. DR STRING; 10090.ENSMUSP00000104721; -. DR GlyGen; Q7TN88; 11 sites. DR iPTMnet; Q7TN88; -. DR PhosphoSitePlus; Q7TN88; -. DR PaxDb; Q7TN88; -. DR PRIDE; Q7TN88; -. DR ProteomicsDB; 289590; -. DR GeneID; 76645; -. DR KEGG; mmu:76645; -. DR CTD; 114780; -. DR MGI; MGI:2664668; Pkd1l2. DR eggNOG; KOG3599; Eukaryota. DR InParanoid; Q7TN88; -. DR OrthoDB; 1276906at2759; -. DR PhylomeDB; Q7TN88; -. DR BioGRID-ORCS; 76645; 0 hits in 52 CRISPR screens. DR ChiTaRS; Pkd1l2; mouse. DR PRO; PR:Q7TN88; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q7TN88; protein. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI. DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central. DR CDD; cd01752; PLAT_polycystin; 1. DR Gene3D; 2.60.120.740; -; 1. DR Gene3D; 3.10.100.10; -; 1. DR InterPro; IPR001304; C-type_lectin-like. DR InterPro; IPR016186; C-type_lectin-like/link_sf. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR000203; GPS. DR InterPro; IPR000922; Lectin_gal-bd_dom. DR InterPro; IPR043159; Lectin_gal-bd_sf. DR InterPro; IPR002859; PKD/REJ-like. DR InterPro; IPR013122; PKD1_2_channel. DR InterPro; IPR003915; PKD_2. 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; IPR014010; REJ_dom. 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; PF02010; REJ; 1. DR PRINTS; PR01433; POLYCYSTIN2. DR SMART; SM00034; CLECT; 1. DR SMART; SM00303; GPS; 1. DR SMART; SM00308; LH2; 1. DR SUPFAM; SSF49299; SSF49299; 1. DR SUPFAM; SSF49723; SSF49723; 1. DR SUPFAM; SSF56436; SSF56436; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. DR PROSITE; PS50221; GPS; 1. DR PROSITE; PS50095; PLAT; 1. DR PROSITE; PS51111; REJ; 1. DR PROSITE; PS50228; SUEL_LECTIN; 1. PE 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Lectin; Membrane; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..2461 FT /note="Polycystic kidney disease protein 1-like 2" FT /id="PRO_0000322577" FT TRANSMEM 1346..1366 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1554..1574 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1596..1616 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1816..1836 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1863..1883 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 1940..1960 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 2186..2206 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 2222..2242 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 2273..2293 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 2315..2335 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 2380..2400 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 33..152 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 160..251 FT /note="SUEL-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260" FT DOMAIN 255..346 FT /note="PKD" FT DOMAIN 424..1125 FT /note="REJ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00511" FT DOMAIN 1280..1329 FT /note="GPS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098" FT DOMAIN 1391..1508 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT REGION 2381..2461 FT /note="Interaction with GNAS and GNAI1" FT /evidence="ECO:0000250" FT COMPBIAS 2103..2106 FT /note="Poly-Gly" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 165 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 267 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 306 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 390 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 406 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 443 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 473 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 494 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1187 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 54..151 FT /evidence="ECO:0000250" FT DISULFID 126..143 FT /evidence="ECO:0000250" SQ SEQUENCE 2461 AA; 271977 MW; 5F837EBA57D54BF3 CRC64; MAGLVFLGLA LSSGATVAKS EGGSLCSRSQ VFFRDACYEF VPLEHTFPGA QGWCEGHGGH LAFIPDEDTQ QFLQRHITQD REWWIGLTGG SGHNGTVGGS GTWLDTSNVN YSNWQEGQAT PAPGSCGYIG SGPSSQWAAL EDCTQTFAFV CEFGVGRSLA CEGHNATMHC DSGEVILVQD AFYGHQTPYL CTRGIWPPSD LEGECGWVSV KDEVAGQCQG LQACQVAVDG TYFGDPCPTR GSYLWVQYQC LEGLRLVVPN GSFIFDNVTI SLMWLLSPYT GNLSCVLSMG DGYTFDPYNP PSVSSNVTHQ FSSPGEFTVF AECTTSEWHV TAQKQVILCE KVETPRITGC TGLAGAGVGL LCQAVFGEPL WVQVDLDGGA GATYAVLSHN RTLAEFTAQR GSQLYNLTLD RDIQEMLGPG RHHLKIQAVS NEGTGTASAP SGNFTVYFVE PLSGLRASWA SDRVELGWDL VVNVSVARGT LEELTFEVAG LNANFSQEEE SVGQSSGNYH VAVPAEGTFL VTVHVRNAFS ELSLDIGNIT VTASSSLQEL SGINAEAKSG HKQDMKVFTE PELYVDPFTE VTLGWPDDDP GLNFHWSCGR CWAQWNACVG RQLLHTDQRL LVLHTFCLPP LNSAVTLHLA ILRGQELEKE TEQCLYVSAP LNLGPQISCE KNCRPVKADQ DVLLTVTVGD ETSVAVFSWY LDDTVPEEVE PLPAACRLRG FWPRSLTLLH SNSSVLLLNS SFLQTWGPVI PIRVTALTSH AYGEDTYMIS MLPRPEVPAC TIDPEEGSVL TSFTVSCSTP ATLGPVEYCF CLPSGFCLHC GPEPALPAVY LPLGEEKDGF VLPVVISVTN RAGDIEQTQV AVKVGHSYTG VEDVTFQEMV SERIATALHQ ESGREQLLLF AKAVSSELNS EVQSPGSGQL GMDIKRKVRE LMLRSLSVVT TGLQNMQRVQ ALAEVLREVT QRAEELTPAA QWEASCALQR ATEALLVAST KVRPEDQRRQ EATRAMFEAV GSVLEASLSH RSEEPMEANS SQVAYIVAQL LRVIDHFQSA LLLGTLPGGL PAILVTPSIS VYTDRIQPRS WQGSSVHTAA ADSVTFTLPA ATFLCPMEDS QEPVDIRMMS FSQNPFPSRS QFDVSGTVGG LRLTSSSGHP IPVKNLSQNI EILLPRISAH IEPKMLSLAS REALSVNVTA GDTALGIQLH WGPGVPLILS LGYGYHPNET SYDAQTHLPP VAATGDLPTW ILHPEDLPFG EGVYYLRVVP EADLESSSGR NLTVGITTFL AHCVFWDETQ ETWDDSGCQV GPRTTPSQTH CLCNHLTFFG SSFLVMPNAI DVRQTAELFA TFEDNPVVVT TVGCLCMLYV LVLIWARRKD IQDQAKVKVV VLEDNDPFAQ YHYLVTVYTG HRRGAATSSK VTLTLYGSDG ESEPHHLSDP DAAVFERGGV DVFLLSTLFP LGELQSLRLW HDNSGDRPSW YVSRVLVYDS VVDRKWYFLC NSWLSVDVGD CVLDKVFPVA TEQDRKQFSH LFFTKTSTGF QDGHIWYSVF CSATRSSFTR VQRVSCCFSM LLCTMLTSIM FWGVPKDPAE QKMDLGKIEF TWQEVMIGLE SSILMFPINL LIVQIFRNTR PRLPMGKDGR QKQGPPNLTP SAQPTEEGLL TPETGIQSLI SSLFKALKVQ PPASGWDSMN PVDINYLLTL MEDIICPEST EGPGFWEEAK GREDPITSTR GSVKPKENTW HPKPELAVRG LWKDSVYRRC LYLQLEHVER ELQLLGPQGF LHHHSHAQAL RQLHVLKGHL WGQPGTPALA YPSTSRVSKS PRGLPWWCVL VGWLLVATTS GVAAFFTMLY GLHYGRVSSL KWLISMAVSF VESVFITQPL KVLGFAAFFA LVLKREDDEE TLPLFPGHLS SPGPGVLFRS RRHSSERAYQ PPPMAAIEKM KTTRLKEQKA FALIREILAY LAFLWMLLLV AYGQRDPNAY HFHRHLERSF SQGFSPVLGF RGFFEWANTT LVKNLYGHHP GFVTDGNSKL VGSAHIRQVR VRESSCAVAQ QLQDSLDGCH GPYSLGIEDL VDYGEGWNAS AYNNSNGFPQ AWRYQSQSQR RGYPMWGKLT LYGGGGYVVP LGTDHQSASR ILQYLFDNSW LDALTRAVFV EFTVYNANVN LFCTVTLTLE TSGLGTFFSH VTLQSLRLYP FTDGWHPFVV AAELTYFLFL FYYMVVQGKL MRKQKWGYFC SKWNLLEVAI ILASWSALVV FVKRTILADR DLQRYREHRE GISFSETAAA DAALGYIIAF LVLLSTVKLW HLLRLNPKMN MITSALRRAW GDISGFVAVI LIMLLAYSFA SNLVFGWKLR SYKTLFDAAE TMVSLQLGIF NYEEVLDYSP ILGSLLIGSC IVFMTFVVLN LFISVILVAF SEEQKSDQLS EEGEIADLLL VKILSFLGIR CKREETWSSS EQPELPPQAL APQPAQALSR V //