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 18-SEP-2019, entry version 117. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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. 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 CC as a 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 iPTMnet; Q7TN88; -. DR PhosphoSitePlus; Q7TN88; -. DR PaxDb; Q7TN88; -. DR PRIDE; Q7TN88; -. DR GeneID; 76645; -. DR KEGG; mmu:76645; -. DR CTD; 114780; -. DR MGI; MGI:2664668; Pkd1l2. DR eggNOG; KOG3599; Eukaryota. DR eggNOG; ENOG410XR4U; LUCA. DR HOGENOM; HOG000169076; -. DR InParanoid; Q7TN88; -. DR KO; K04988; -. DR OrthoDB; 1276906at2759; -. DR PhylomeDB; Q7TN88; -. DR PRO; PR:Q7TN88; -. DR Proteomes; UP000000589; Unplaced. 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; 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; 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 Complete proteome; Disulfide bond; Glycoprotein; Lectin; Membrane; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 2461 Polycystic kidney disease protein 1-like FT 2. FT /FTId=PRO_0000322577. FT TRANSMEM 1346 1366 Helical. {ECO:0000255}. FT TRANSMEM 1554 1574 Helical. {ECO:0000255}. FT TRANSMEM 1596 1616 Helical. {ECO:0000255}. FT TRANSMEM 1816 1836 Helical. {ECO:0000255}. FT TRANSMEM 1863 1883 Helical. {ECO:0000255}. FT TRANSMEM 1940 1960 Helical. {ECO:0000255}. FT TRANSMEM 2186 2206 Helical. {ECO:0000255}. FT TRANSMEM 2222 2242 Helical. {ECO:0000255}. FT TRANSMEM 2273 2293 Helical. {ECO:0000255}. FT TRANSMEM 2315 2335 Helical. {ECO:0000255}. FT TRANSMEM 2380 2400 Helical. {ECO:0000255}. FT DOMAIN 33 152 C-type lectin. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 160 251 SUEL-type lectin. {ECO:0000255|PROSITE- FT ProRule:PRU00260}. FT DOMAIN 255 346 PKD. FT DOMAIN 424 1125 REJ. {ECO:0000255|PROSITE- FT ProRule:PRU00511}. FT DOMAIN 1280 1329 GPS. {ECO:0000255|PROSITE- FT ProRule:PRU00098}. FT DOMAIN 1391 1508 PLAT. {ECO:0000255|PROSITE- FT ProRule:PRU00152}. FT REGION 2381 2461 Interaction with GNAS and GNAI1. FT {ECO:0000250}. FT COMPBIAS 2103 2106 Poly-Gly. FT CARBOHYD 94 94 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 110 110 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 165 165 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 267 267 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 306 306 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 390 390 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 406 406 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 443 443 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 473 473 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 494 494 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1187 1187 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 54 151 {ECO:0000250}. FT DISULFID 126 143 {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 //