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Database: UniProt
Entry: A0A2B4T2C8_STYPI
LinkDB: A0A2B4T2C8_STYPI
Original site: A0A2B4T2C8_STYPI 
ID   A0A2B4T2C8_STYPI        Unreviewed;      2319 AA.
AC   A0A2B4T2C8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Polycystic kidney disease protein 1-like 2 {ECO:0000313|EMBL:PFX34775.1};
GN   Name=Pkd1l2 {ECO:0000313|EMBL:PFX34775.1};
GN   ORFNames=AWC38_SpisGene266 {ECO:0000313|EMBL:PFX34775.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX34775.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
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:PRU00076}.
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:PFX34775.1}.
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DR   EMBL; LSMT01000002; PFX34775.1; -; Genomic_DNA.
DR   Proteomes; UP000225706; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002859; PKD/REJ-like.
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; IPR046791; Polycystin_dom.
DR   InterPro; IPR014010; REJ_dom.
DR   PANTHER; PTHR10877:SF150; POLYCYSTIC KIDNEY DISEASE AND RECEPTOR FOR EGG JELLY-RELATED PROTEIN; 1.
DR   PANTHER; PTHR10877; POLYCYSTIN FAMILY MEMBER; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF08016; PKD_channel; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   Pfam; PF20519; Polycystin_dom; 1.
DR   Pfam; PF02010; REJ; 1.
DR   PRINTS; PR01433; POLYCYSTIN2.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50095; PLAT; 1.
DR   PROSITE; PS51111; REJ; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706};
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        1292..1312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1501..1519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1544..1565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1598..1621
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1633..1660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1724..1746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1989..2010
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2022..2048
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2081..2099
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2119..2141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2188..2207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..93
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          92..135
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          143..295
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          300..1028
FT                   /note="REJ"
FT                   /evidence="ECO:0000259|PROSITE:PS51111"
FT   DOMAIN          1337..1454
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DISULFID        125..134
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1829..1843
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ   SEQUENCE   2319 AA;  260276 MW;  04C832F99EC194F7 CRC64;
     MYLETKGLRV VNRSQTSITV SWNPMESVSG YTIKYDKINN PEYIIVRSET TFEITGLEIN
     TIYKIQVGGL KDVDGEEKPE SYSSILEART LSNDLCDSSP CQNGGTCQDG GPPSSESSLP
     MYCQCAEKFS GRFCAVPKDS ADCQTALGME NYGIPNERVQ ASSEWKFDKA IHGRLHFQSR
     SGNQGAWSAK TKDANQWLQI DLGSVFTKVT GVATQGRYMY DQWVTKYKVQ FSNGGSTFTN
     YKEPGQAADK VFDGNTDQNT VVKHFLHAPF RARYIRFQPV TYYERISMRV ELYGCSDFVC
     QSPDVILPNI SPNASSNISI HRLRQFTIQS DVKFNCNIYY KASFLWRIYQ LGKEETLLLS
     RNSFSELQIT PHLLPVGEFL VRLNVSLIGT AVFGVGHGYF KVERSPLVAF IAGGNKVAKG
     LDRTLIFDAS LSYDPDEKSL RFSGLNFTWQ CKESPRHLNN SDEPGCHYRA DDKETVGYEL
     RINNSLLAEN TSYFITVQVT KHERQAVYTQ EVFIVPGDPP EVQIRCVENC AAKLNPSGIM
     ALQGMCTGAS CHGNLIFEWT ALKDLNNSSK SSHWAEISHI QELISTRVSS KSFVTRPEVL
     TPDTRYKFIL TAQRPGGNRG FSEYHVTSNS PPVGGVCNVS QTSGVTLITE FTFACNNWQD
     PDLQLQYEFI YLIDDNIFNV AYKGVKKSLT TKLPAGGRKN NFTIDFRVRV ADILGAYTEV
     RTPVQVSEPT FEPKDLVDMV ASLTSRDESE LNSLIKSGDV SRAAQLATAV LSVVDVVTQA
     ESAESQMKSN IIQQLSAVPV DTVVRVQQVS YVIASASSVI GEITVEAQKA ATEALEKMTV
     VLKTESTAGQ SYDTLFDGAK SLVTGLGSML RVTSHEASVD DAASKEESRL KASFITAYEG
     RLPKSQRRNL KSRISLSDVL TRTKRDGADL RLQARVKVET LLHSLEEVGS TILSRTLVGE
     EPKVLPAQAM SLLLLRQEPN LVAGTVLSNK GNSFRLPPVS KLFDNSTQFL DSQMVTTDFI
     PFSWDPSGAR VTTAVSSLEL KNSSGHLLNT TELIAPITLR LQSHQKFTNA SQFHYVGSNR
     TVFYKVNVNQ SGMALLLNIR PESNKTEFVV TVKYGERPSP SNSDLNLTLP DLSSCNKVPD
     GYVNCSSNPY VVFVNQDFVE NKGFGYYFFG LRAVSRISRV KRCSGHGRSK RSCVQYKEPP
     TMGPSYSVPQ YRVGDENYTI QVMPAACLFW NAELSKWTSE GCQVAEMTTQ DAIYCSCNHL
     SSFGGQLFVT PNPLDFDKVF IELTRLPDSG NIAVILAVSC VFGLYLSLLL WARKNDKLDN
     LKVGEKAFVG VPSEGSHFIE VQVSTGIWRN SGTTANVFVI LEGEIGTSRP YHLKDDSSIP
     FARGSIISFI LAIHDSIGPI RTVRVWHDNS GNSPSWFLNH IKVCELTNKK QWNFVCFAWL
     AVDRGDGLID RTLRGTSTVD KGIDFAVYVQ NRIAGEFSDS HLWFSVATRP PRYRFTRAQR
     LSCCLSLLLT TMLASAMFYE RETAMDDNQG SLRLGRFVVN FREFIIAVQS LMVVLPVNIL
     TVALFTHTRS SNENKEMALQ SNSHKKLARK SDISFPHWFI FVPWLLCFLL STCTASFVVF
     YSLQWGADKS EQWLVSVAMS VVLDIFVSKP VQIIVVAFML SHICKGGIQR FTRQPYHADA
     IVDVEDIKLS WLGNEDTDEE EIEIPKPLSK RQLRRARIAR MREVYMYTAL RNIVSYMLYL
     LILFIVCYGG RSQHGYLMTS TLKTTFGKLD SITNYFKTWD WARDVLVPGL FDDGKNLILN
     SHSLYIGSGD AVLVGMPRFR QLRVKEGSCD VSIEELKPPF NSCVATYTSN NEDKSSFHRT
     RWDQFSSSRN DSLNILYQIC PTAWHYSSAE RTQSLPLWGK LHLSNFYGEG GYLAELGYDK
     ATALKVISEL KLFDWIDRFT SAIIVEFTVF NSQVNLFGVI WIPIEFSPSG HVVSDPVIRG
     IHVYEIGGGY SAVTVVCQLL LVVYIIYFVV KETSKMIAGV RMYFAQFLNW VELTQTLTVI
     GFVVTHIFKQ AELFYNTEKL RNNTFQFISF DKGAFLEDLE TVLISLLMFL NTLKLLYLLK
     FNPHVRHLFY VMKGSARELV NCSVAFTLFM FACIHVGYFL FGSELYPFSS PVITLQSLLV
     EGVLGGRFDY FNDCCTVTGP VYVTALKLGL NLIFINVFVS VLVYNYGNIR DLTRGKFNLG
     NFIIVKIKEL MGFGVHSSAM DADSSCDPNT KNEENALPEV DEILTKLDRI NHHLNVLYAD
     EFGEDLDMFS LWFDLHMQRL EAKDTQRNEN DAEKDLEDA
//
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