PK1L2_MOUSE
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 25-MAY-2022, entry version 129.
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}.
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DR EMBL; AY164484; AAO32797.1; -; mRNA.
DR RefSeq; NP_083962.4; NM_029686.4.
DR AlphaFoldDB; Q7TN88; -.
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 DNASU; 76645; -.
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; 1 hit in 73 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; 2.60.220.50; -; 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; IPR046338; GAIN_dom_sf.
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 1623..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2381..2461
FT /note="Interaction with GNAS and GNAI1"
FT /evidence="ECO:0000250"
FT REGION 2438..2461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1705..1729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
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